Cleaning composition and use thereof

文档序号：1602449 发布日期：2020-01-07 浏览：41次中文

阅读说明：本技术 清洁组合物及其用途 (Cleaning composition and use thereof ) 是由 K.戈里 F.巴里恩托斯 M.戈杰尔曼森于 2018-04-06 设计创作，主要内容包括：本发明涉及组合物,如包含酶的混合的清洁组合物。本发明进一步涉及包含此类酶的组合物在清洁过程中和/或用于有机污垢的深度清洁的用途,用于去除或减少有机物质的组分的方法。(The present invention relates to compositions, such as mixed cleaning compositions, comprising enzymes. The invention further relates to the use of a composition comprising such an enzyme in a cleaning process and/or for deep cleaning of organic soils, a method for removing or reducing components of organic matter.)

1. A cleaning composition comprising dnase, rnase and a cleaning component.

2. The cleaning composition according to claim 1, wherein the DNase is a microorganism, preferably obtained from a bacterium or a fungus.

3. The cleaning composition according to claim 2, wherein the DNase is obtained from Bacillus, preferably from Bacillus foodborne, Bacillus horikoshii, Bacillus licheniformis, Bacillus subtilis, Bacillus hoponensis, Bacillus sick research, Bacillus algaes, Bacillus vietnaensis, Bacillus tsunefati, Bacillus indians, Bacillus flavi or Bacillus leysi.

4. The cleaning composition of claim 3, wherein the DNase comprises one or two motifs [ D/M/L ] [ S/T ] GYSR [ D/N ] (SEQ ID NO:73) or ASXNRSKG (SEQ ID NO: 74).

5. The cleaning composition according to any one of claims 2 to 4, wherein the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 13.

6. The cleaning composition according to any one of claims 2 to 4, wherein the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID No. 65.

7. The cleaning composition according to any one of claims 2 to 4, wherein the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 66.

8. The cleaning composition according to claim 2, wherein the DNase is a fungus, preferably obtained from Aspergillus, and even more preferably obtained from Aspergillus oryzae, and wherein the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO. 67.

9. The cleaning composition according to claim 2, wherein the DNase is a fungus, preferably obtained from Trichoderma, and even more preferably obtained from Trichoderma harzianum, and wherein the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 68.

10. The cleaning composition according to any preceding claims, wherein the rnase is selected from the group consisting of: an rnase comprising an amino acid sequence having:

i) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO 86,

ii) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO:87,

iii) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 88,

iv) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 89,

v) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 90,

vi) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 91,

vii) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO:92,

viii) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO:93,

ix) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 94,

x) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 95,

xi) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 96,

xii) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 97,

xiii) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 98,

xiv) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 99,

xv) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 100,

xvi) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 101,

xvii) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO:102,

xviii) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 103, and

xix) is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID No. 104.

11. The cleaning composition according to any preceding claims, wherein the DNase comprises one or both of the motifs [ V/I ] PL [ S/A ] NAWK (SEQ ID NO:75) or NPQL (SEQ ID NO:76) and the RNAse comprises one or more of the motifs EYTV (SEQ ID NO 82), [ YRF ] E [ AYFCWC ] D (SEQ ID NO 83), IGGD (SEQ ID NO 84), YPH, HTGA (SEQ ID NO 85) or DRV.

12. The cleaning composition according to any preceding claims, wherein the amount of DNase in the composition is from 0.01 to 1000ppm and the amount of RNAse is from 0.01 to 1000 ppm.

13. A cleaning composition according to any preceding claim, wherein the cleaning component is selected from surfactant, preferably anionic and/or nonionic, builder and bleach components.

14. Use of a cleaning composition according to any one of claims 1 to 13 for deep cleaning an article, wherein the article is a textile or a surface.

15. A method for formulating a cleaning composition according to any one of claims 1 to 13 comprising adding dnase, rnase and at least one cleaning component.

16. A kit intended for deep cleaning, wherein the kit comprises a solution containing an enzyme mixture of dnase, rnase and optionally protease.

17. A method of deep cleaning an article, the method comprising the steps of:

a) contacting an article with a cleaning composition according to any one of claims 1 to 13; and

b) and optionally rinsing the article, wherein the article is preferably a textile.

Background

The present invention relates to compositions, such as mixed cleaning compositions, comprising enzymes. The invention further relates to the use of a composition comprising such an enzyme in a cleaning process and/or for deep cleaning of organic soils, a method for removing or reducing components of organic matter.

Disclosure of Invention

The present invention relates to cleaning compositions comprising dnase, rnase and a cleaning component. The invention further relates to compositions (particularly to cleaning compositions) comprising at least 0.001ppm dnase and at least 0.001ppm rnase and a cleaning component, wherein the cleaning component is selected from the group consisting of

0.1 to 15 wt% of at least one surfactant;

0.5 to 20 wt% of at least one builder; and

c.0.01wt% to 10 wt% of at least one bleach component.

The invention further relates to the use of a cleaning composition comprising a dnase, an rnase and a cleaning component for deep cleaning of an article, wherein the article is a textile or a surface. The invention further relates to a method of formulating a cleaning composition comprising adding a dnase, an rnase and at least one cleaning component. The invention further relates to a kit intended for deep cleaning, wherein the kit comprises a solution containing an enzyme mixture of dnase, rnase and optionally protease. The invention further relates to a method for deep cleaning of an article, comprising the steps of:

a) contacting the article with a cleaning composition comprising a dnase, an rnase and a cleaning component; and

b) optionally rinsing the article, wherein the article is preferably a textile.

The invention further relates to a method for deep cleaning of an article, comprising the steps of: a) contacting an article with a solution comprising: an enzyme mixture comprising dnase and rnase and optionally protease; and a cleaning component, wherein the cleaning component is selected from 0.1 wt% to 15 wt% of at least one surfactant; 0.5 to 20 wt% of at least one builder; and 0.01 wt% to 10 wt% of at least one bleach component; and b) and optionally rinsing the article, wherein the article is preferably a textile. The invention also relates to a kit intended for deep cleaning, wherein the kit comprises a solution containing an enzyme mixture of dnase and rnase.

Detailed Description

A variety of enzymes are used in the cleaning process, each directed at a particular type of soil (e.g., protein, starch, and greasy soil). Enzymes are now standard ingredients in detergents for laundry and dish washing. The effectiveness of these commercial enzymes provides detergents that remove most soils. However, due to the complex nature of such organic materials, the organic materials contained in many biofilms, such as EPS (extracellular polymers), constitute a challenging type of fouling. None of the commercially available cleaning compositions are effective at removing or reducing EPS and/or biofilm related soils. The present invention provides compositions comprising a blend of at least one dnase and rnase that is effective in reducing or removing components of organic soils. Biofilms can be produced when cells of a group of microorganisms adhere to each other or to a surface (such as a textile, dishware, or hard surface) or another surface. These adherent cells are usually embedded in an autogenous matrix of Extracellular Polymer (EPS), which constitutes 50% to 90% of the total organic matter of the biofilm. EPS is composed primarily of polysaccharides (exopolysaccharides) and proteins, but includes other macromolecules such as eDNA, RNA, lipids, and other organic substances. Organic matter (e.g., biofilm) can be sticky or cohesive, causing redeposition or reverse staining of soil when present on the textile, resulting in graying of the fabric. Another disadvantage of organic matter (e.g. biofilm) is malodor, since many malodor-associated molecules are often associated with organic matter (e.g. biofilm). Furthermore, when soiled laundry items are washed with less soiled laundry items, the soil present in the wash liquor tends to adhere to organic matter (e.g., biofilm or biofilm components), and thus the laundered items are more "soiled" than before the wash. This effect may also be referred to as redeposition.

The compositions of the present invention are preferably cleaning compositions comprising at least one dnase and at least one rnase. Examples of useful dnases and rnases are mentioned in the "nuclease" section below.

The compositions of the present invention comprising a blend of dnase and rnase are effective in reducing or removing organic components and fouling from organic matter.

Nuclease enzymes

Nucleases are a general term for enzymes capable of cleaving phosphodiester bonds between nucleic acid monomers. Exonucleases digest nucleic acids from the ends. Endonucleases act on the region in the middle of the target molecule. Nucleases are further classified into dnase acting on DNA and rnase acting on RNA.

The present invention relates to compositions (e.g., cleaning compositions) comprising a blend of at least one polypeptide having dnase activity (dnase) and at least one polypeptide having rnase activity (rnase). Alternatively, the composition comprises a polypeptide having both dnase and rnase activity.

The compositions of the invention comprise at least one nuclease, wherein at least the composition comprises both rnase and dnase activity. This can be achieved by adding a nuclease that has both or either of rnase activity and dnase activity. Some nucleases are dnases with dnase activity only, and some dnases have less rnase activity but are still characterized as dnases, and the same is true for rnases. The compositions of the invention comprise nucleases having one and/or two activities. One embodiment relates to a composition comprising a dnase without rnase activity and an rnase without dnase activity. One embodiment relates to a composition comprising a nuclease that inhibits both dnase activity and rnase activity.

An example of a nuclease with DNase activity and RNAse activity is an endonuclease from Serratia marcescens (Serratia marcescens), under the name

The following are commercially available (available from Sigma Aldrich). Thus, the composition of the invention may comprise a nuclease selected from e.c.3.1.30.1 or e.c. 3.1.30.2.

Some suitable nucleases for inclusion in the compositions of the invention are listed below. Suitable nucleases include, but are not limited to, those listed below.

Polypeptides having DNase Activity (DNase)

The term "dnase" means a polypeptide having dnase (deoxyribonuclease) activity which catalyzes the hydrolytic cleavage of phosphodiester bonds in the DNA backbone, thereby degrading DNA. Exo-deoxyribonuclease cleaves or cleaves a residue at the end of a DNA backbone, wherein endo-deoxyribonuclease cleaves or cleaves within the DNA backbone. Dnases may cleave only double-stranded DNA or may cleave both double-stranded and single-stranded DNA. The terms "dnase" and "expressing" a polypeptide having dnase activity "are used interchangeably throughout the application. For the purposes of the present invention, DNase activity was determined according to the procedure described in assay I.

Preferably, the dnase is selected from any one of the enzymes e.c.3.1, preferably e.c.3.1.21, such as e.c.3.1.21.X (wherein X ═ 1,2, 3, 4, 5,6, 7, 8 or 9), or such as e.g. dnase I, dnase IV, type I site-specific dnase, type II site-specific dnase, type III site-specific dnase, CC-preferred endo-dnase, dnase V, T (4) dnase II, T (4) dnase IV, or e.c.3.1.22.Y (wherein Y ═ 1,2,4 or 5), such as dnase II, aspergillus dnase K (1), cross-linked (cross-linked) endo-dnase X.

Preferably, the polypeptide having dnase activity is obtained from a microorganism and the dnase is a microbial enzyme. The DNase is preferably of fungal or bacterial origin.

The DNA enzyme can be obtained from Bacillus, for example, Bacillus such as Bacillus licheniformis (Bacillus licheniformis), Bacillus subtilis (Bacillus subtilis), Bacillus species-62451, Bacillus horikoshii (Bacillus horikoshii), Bacillus species-62451, Bacillus species-16840, Bacillus species-62668, Bacillus species-13395, Bacillus hophilus (Bacillus horneckiae), Bacillus species-11238, Bacillus cibi (Bacillus), Bacillus research (Bacillus idensis), Bacillus species-62520, Bacillus species-16840, Bacillus species-62668, Bacillus algicium (Bacillus algicila), Bacillus Vietnamensis (Bacillus vietnamensis), Bacillus pumilus (Bacillus subtilis), Bacillus subtilis (Bacillus licheniformis), Bacillus licheniformis (Bacillus flavus), Bacillus licheniformis (Bacillus flaviviformis), Bacillus licheniformis (Bacillus flaviviformis), Bacillus subtilis (Bacillus subtilis), Bacillus subtilis (Bacillus subtilis) Bacillus luciferis (Bacillus luciferensis) and Bacillus species SA 2-6.

The dnase may also be obtained from any one of: ascophyllospora sp, Vibrisseaflavoscens, Setosphaeria rostrata, Endophoragrimacevaldina, Exponaria polyspora (Corynebacterium parvum), Microphyllomyces heterostemus (Paraphoma sp) XZ1965, Monilinia fructicola (Monilinia fructicola), Curvularia neoformans (Curvularia lunata), Penicillium dictyostelium (Penicillium reteticum), Penicillium Penicillium (Penicillium nigricans), Penicillium nigrostreatum (Penicillium nigrostreatum), Setophagoides, Alternaria (Alternaria), Alternaria sp.XZ 2545, Trichoderma reesei, Chaetomium thermophilum, Achillea thermophilum (Thermophila sp), Thermoplasma sp, Achillea sp, Thermoplasma, Trichoderma sp, Thermobasicola (Trichoderma sp), Trichoderma sp, Environmental sample O, Clavicipitaceae species (Clavicipitaceae sp) -70249, Westcase species (Westerkella sp.) AS85-2, Humicoopsis serosorioides, Neosartoryamasa, Roussoaella intermedia, Geospora (Pleospora), Phaeosphaera (Phaeosphaeria) or Didymosphaeria afutilis.

The dnase used in the composition of the present invention preferably belongs to NUC1 group of dnases. The NUC1 group of dnases comprises polypeptides other than those having dnase activity, which may comprise one or more of the following motifs: [ T/D/S ] [ G/N ] PQL (SEQ ID NO 69), [ F/L/Y/I ] A [ N/R ] D [ L/I/P/V ] (SEQ ID NO:70), or C [ D/N ] T [ A/R ] (SEQ ID NO: 71). One embodiment of the invention relates to compositions comprising an rnase and polypeptides having dnase activity, wherein the polypeptides comprise one or more of the following motifs: [ T/D/S ] [ G/N ] PQL (SEQ ID NO 69), [ F/L/Y/I ] A [ N/R ] D [ L/I/P/V ] (SEQ ID NO:70) or C [ D/N ] T [ A/R ] (SEQ ID NO: 71).

The DNase preferably comprises the NUC1_ A domain [ D/Q ] [ I/V ] DH (SEQ ID NO 72). In addition to comprising any of the domain motifs [ T/D/S ] [ G/N ] PQL, [ F/L/Y/I ] A [ N/R ] D [ L/I/P/V ] or C [ D/N ] T [ A/R ], the polypeptide having DNase activity for use in the compositions of the invention may comprise a NUC1_ A domain and may have the common motif [ D/Q ] [ I/V ] DH (SEQ ID NO 72). In one embodiment, the invention relates to a composition comprising an rnase and a polypeptide comprising one or more motifs selected from the group consisting of: [ E/D/H ] Hl/L/F/M ] X [ P/A/S ], [ T/D/S ] [ G/N ] PQL, [ F/L/Y/I ] AN/R ] D [ L/I/P/V ], C [ D/N ] T [ A/R ] and [ D/Q ] [ I/V ] DH, wherein these polypeptides have DNase activity.

The dnase added to the composition of the invention preferably belongs to the group of dnases comprised in the GYS-clade, which is the group of dnases on the same branch of the phylogenetic tree with similarities in both structure and function. These NUC1 and/or NUC1_ A DNases contain the conserved motif [ D/M/L ] [ S/T ] GYSR [ D/N ] (SEQ ID NO:73) or ASXNRSKG (SEQ ID NO:74) and share similar structural and functional properties. The DNase of the GYS-clade is preferably obtained from Bacillus.

One embodiment of the invention relates to a composition comprising a polypeptide of an RNase and a GYS clade with DNase activity, optionally wherein the polypeptide comprises one or two motifs [ D/M/L ] [ S/T ] GYSR [ D/N ] (SEQ ID NO:73), ASXNRSKG (SEQ ID NO:74), and wherein the polypeptide is selected from the group consisting of:

a) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 1,

b) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 2,

c) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 3,

d) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 4,

e) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 5,

f) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 6,

g) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 7,

h) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 8,

i) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 9,

j) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 10,

k) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 11,

l) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 12,

m) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 13,

n) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 14,

o) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 15,

p) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 16,

q) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 17,

r) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 18,

s) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 19,

t) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 20,

u) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 21,

v) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 22,

w) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 23,

x) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 24, and

y) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 25.

Polypeptides having dnase activity and comprising the GYS-clade motif have shown particularly good deep cleaning properties, e.g. the dnase is particularly effective in removing or reducing components of organic matter, such as biofilm, from an article, such as a textile or a hard surface. In addition, these dnases are particularly effective in removing or reducing malodours from articles such as textiles or hard surfaces. Furthermore, the GYS-clade dnase is particularly effective in preventing redeposition when washing items (such as textiles).

In one embodiment, the DNase to be added to the composition of the invention preferably belongs to the group of DNases comprised in the NAWK-clade, which is NUC1 and NUC1_ A DNase, which DNase may further comprise the conserved motif [ V/I ] PL [ S/A ] NAWK (SEQ ID NO:75) or NPQL (SEQ ID NO: 76).

One embodiment of the invention relates to a composition comprising a polypeptide of an RNase and a NAWK-clade with DNase activity, optionally wherein the polypeptide comprises one or two motifs [ V/I ] PL [ S/A ] NAWK (SEQ ID NO:75) or NPQL (SEQ ID NO:76), and wherein the polypeptide is selected from the group consisting of:

Polypeptides having dnase activity and comprising NAWK-clade motifs have shown particularly good deep cleaning properties, e.g. dnase is particularly effective in removing or reducing components of organic matter, such as biofilm, from an article, such as a textile or a hard surface. In addition, these dnases are particularly effective in removing or reducing malodours from articles such as textiles or hard surfaces. Furthermore, the NAWK-clade dnases are particularly effective in preventing redeposition when washing items (such as textiles).

The DNase to be added to the composition of the invention preferably belongs to the group of DNases comprised in the KNAW-clade, which is the NUC1 and NUC1_ A DNase, which DNase may further comprise the conserved motif P [ Q/E ] L [ W/Y ] (SEQ ID NO:77) or [ K/H/E ] NAW (SEQ ID NO: 78).

One embodiment of the invention relates to a composition comprising a polypeptide of an RNase and a KNAW clade with DNase activity, optionally wherein the polypeptide comprises one or two motifs P [ Q/E ] L [ W/Y ] (SEQ ID NO:77) or [ K/H/E ] NAW (SEQ ID NO:78), and wherein the polypeptide is selected from the group consisting of:

Polypeptides having dnase activity and comprising a KNAW-clade motif have shown particularly good deep-cleaning properties, e.g. the dnase is particularly effective in removing or reducing components of organic matter, such as biofilm, from an article, such as a textile or a hard surface. In addition, these dnases are particularly effective in removing or reducing malodours from articles such as textiles or hard surfaces. Furthermore, the KNAW-clade DNase is particularly effective in preventing redeposition when washing articles such as textiles.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus species-62451) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 1, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:1 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus horikoshii) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 2, and wherein the compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:2 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus species-62520) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide set forth in SEQ ID No. 3, and which compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:3 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus species-62520) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide set forth in SEQ ID No. 4, and which compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID No. 4 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus horikoshii) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 5, and wherein the compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO. 5 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus horikoshii) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 6, and the compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID No. 6 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from bacillus species-16840) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 7, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO. 7 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from bacillus species-16840) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 8, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:8 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus species-62668) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 9, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:9 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus species-13395) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 10, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:10 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus pophae) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 11, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:11 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus species-11238) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 12, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:12 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus foodborne) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 13, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:13 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus species-18318) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 14, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:14 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus sick & research) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 15, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 15.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., from bacillus algal) having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 16, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:16 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from an environmental sample J and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 17, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:17 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from bacillus vietnamensis) having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 18, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 18.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from tsunobacillus huajingensis) having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 19, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 19.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from paenibacillus mucilaginosus (paenibacillus mulilaginosus) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 20, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 20.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 21 obtainable from bacillus (e.g., obtainable from bacillus indiana), and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:21 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from bacillus thailabous) having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 22, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:22 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from bacillus leffensis) having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 23, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 23.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from bacillus thailabous) having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 24, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:24 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from bacillus species SA 2-6) and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 25, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 25.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from an echinospora species and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 26, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:26 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from vibrasulavovirens and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 27, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:27 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from a setosphareria border and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 28, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:28 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the present invention relates to compositions comprising an rnase and a polypeptide that is obtainable from endophragmiavaldina and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 29, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:29 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from corynespora spinosa and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 30, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:30 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from phoma sp XZ1965 and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 31, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 31.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from monilinia persica and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 32, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:32 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from Curvularia lunata and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID NO:33, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:33 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from penicillium reticulosporum and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 34, and the compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 34.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is available from penicillium quercetin and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 35, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:35 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from a species of the genus setophaeosepharia and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 36, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 36.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from alternaria species XZ2545 and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 37, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 37.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from alternaria and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 38, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 38.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from trichoderma reesei and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 39, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:39 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from chaetomium thermophilum and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 40, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:40 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide set forth in SEQ ID NO:41 obtainable from trichothecium thermophilum, and which have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 41.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from metaproteniauchlasporia and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 42, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:42 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from xylaria crassa and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 43, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:43 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from acremonium species XZ2007 and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 44, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:44 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from acremonium dichromophilae and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 45, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:45 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from cladosporium species XZ2014 and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 46, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 46.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from metarhizium species HNA15-2 and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 47, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:47 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from acremonium species XZ2414 and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 48, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 48.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from isaria tenuipes and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 49, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:49 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from alternaria convolvulus and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 50, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ id no: 50.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from metarhizium anisopliae and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 51, and the compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 51.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from thermomyces bisporus and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 52, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:52 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is available from sporomiafia etaria and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide set forth in SEQ ID No. 53, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 53.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is available from Pycnidiophora cf. dispera and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 54, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 54.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from environmental sample D and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 55, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:55 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from an environmental sample O and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 56, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:56 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from species-70249 of the family ergoviridae and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 57, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:57 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from westerella species AS85-2 and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 58, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 58.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from humicola rhodosporioides and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 59, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 59.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is available from neosrtoryamassa and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 60, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:60 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from Roussoella intermedia and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 61, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:61 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is available from the order glaucomatoidea and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID NO:62, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:62 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from the genus darkling mycosphaerella and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 63, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:63 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is available from didymosphaeriafitilis and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 64, and the compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:64 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from bacillus licheniformis) that has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 65, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:65 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide that is obtainable from bacillus (e.g., obtainable from bacillus subtilis) has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 66, and these compositions have dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:66 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 67, obtainable from aspergillus (e.g., from aspergillus oryzae), and having dnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:67 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising an rnase and a polypeptide having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID No. 68 obtainable from trichoderma, e.g., from trichoderma harzianum, and these compositions have dnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 68.

The above dnase may be combined with any of the following rnases to form a blend that is added to the composition according to the present invention.

Polypeptides having RNAse Activity (RNAses)

The term "rnase" is an abbreviation for the term ribonuclease, which means a nuclease with rnase activity (EC 3.1.2.7), catalyzing the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases. In one embodiment, the invention relates to, for example, endoribonucleases. For the purposes of the present invention, the rnase activity was determined according to the procedure described in assay II. Preferably, the RNase incorporated in the compositions of the invention comprises an RNase from the PF00545 family of rnases, e.g., the bacillus RNase Barnase, Swiss Prot P00648(SEQ ID NO 91) or a closely related homologue having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID 91.

In one embodiment, the rnase to be added to the composition of the invention is selected from rnases having e.c.3.1.26.X (wherein X ═ 1,2, 3, 4, 5,6, 7, 8, 9, 10, 11, 12 and 13), such as rnases; phycomyces multiceps (Physarum multicephalum) RNase, RNase alpha, RNase III, RNase C, RNA enzyme H, RNA enzyme HII, RNase P, RNA enzyme IV, RNase P4, RNase M5, RNase poly-U specific, RNase IX, RNase Z, RNA enzyme E, RNA enzyme L or retroviral RNase H. Rnases may also be selected from ec.3.1.27.Y (where Y ═ 1,2, 3, 4, 5,6, 7, 8, 9, 10), for example rnases; RNAse T (2), Bacillus subtilis RNAse, RNAse T (1), RNAse U (2), pancreatic RNAse, RNAse A, RNA enzyme I, Enterobacter RNAse, RNAse F, RNA enzyme V, rRNA endonuclease, and RNAse B glycoprotein standards, e.g., from bovine pancreas.

In one embodiment, the rnase is any one of: rnase a (bovine pancreas) UniProt-P61823, rnase HI (e.coli) UniProt-P0A7Y4, rnase HII (e.coli) UniProt-P10442, rnase III (e.coli) UniProt-P0A7Y0, rnase T1 (aspergillus oryzae) UniProt-P00651, rnase T2 (aspergillus oryzae) UniProt-P10281, or closely related homologues of rnases, e.g. having at least 80%, or at least 85% or at least 90% or at least 95% or at least 98% sequence identity thereto.

RNAses are available from Paenibacillus species, such as Paenibacillus species-18057, Paenibacillus species-62770, Paenibacillus species-18006, Paenibacillus species-62724, Paenibacillus jellmaniae (Paenibacillus thuringiensis). Alternatively, the RNase may be obtained from Amycolatopsis coelicolor (Amycolatopsis azurea), Acremonium acremophilum (Acremonium alcalophilum), Erwinia persicae (Erwinia apericina), Saccharothrix sp-62935, Saccharopolyspora endophytica (Saccharopolyspora endophytica), circi Amycolatopsis (Amycolatopsis), Alcaligenes sp-62516, Nonomuraea (Nonomuraea dietziae).

In preferred embodiments, the rnase comprises any or all of the following motifs: EYTV (SEQ ID NO 82), [ YRF ] E [ AYFCC ] D (SEQ ID NO 83), IGGD (SEQ ID NO 84), YPH, HTGA (SEQ ID NO 85) or DRV.

One embodiment of the invention relates to a composition comprising a polypeptide having rnase activity, optionally wherein the polypeptide comprises one or all of the motifs EYTV (SEQ ID NO 82), [ YRF ] E [ aypwc ] D (SEQ ID NO 83), IGGD (SEQ ID NO 84), YPH, HTGA (SEQ ID NO 85) or DRV, and wherein the polypeptide is selected from the group consisting of:

In some preferred embodiments of the invention, the dnase of the invention is combined with an rnase, wherein the rnase is any one of:

in some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from paenibacillus species-18057 and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID No. 86, and these compositions have rnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:86 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the present invention relates to compositions comprising polypeptides that are obtainable from paenibacillus species-62770 and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID NO:87, and these compositions have rnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:87 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from amycolatopsis coelicolor and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID NO:88, and these compositions have rnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:88 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the present invention relates to compositions comprising polypeptides that are obtainable from population E of environmental samples and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides set forth in SEQ ID No. 89, and which have rnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID No. 89 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from acremonium and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID No. 90, and which have rnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 90.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from Stenotrophomonas rhizophila (Stenotrophomonas rhizozophia) and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID No. 92, and which have rnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 92.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from erwinia persicinia and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID NO:93, and which have rnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 93.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from paenibacillus freezes and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID No. 94, and these compositions have rnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 94.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from saccharothrix species-62935 and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID No. 95, and these compositions have rnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ id No. 95 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from saccharopolyspora endophyta and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID NO:96, and these compositions have rnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 96.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from circi amycolatopsis and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID NO:97, and which have rnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:97 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the present invention relates to compositions comprising polypeptides that are obtainable from paenibacillus species-62770 and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID NO:98, and these compositions have rnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in seq id no:98 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the present invention relates to compositions comprising a polypeptide obtainable from paenibacillus species-18006 and having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 99, and which have rnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:99 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the present invention relates to compositions comprising polypeptides that are obtainable from paenibacillus species-62724 and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID No. 100, and these compositions have rnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 100.

In some embodiments, the invention relates to compositions comprising a polypeptide that is obtainable from alcaliophila species-62516 and has at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide shown in SEQ ID No. 101, and these compositions have rnase activity. In one aspect, these polypeptides differ from the mature polypeptide shown in SEQ ID NO:101 by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids.

In some embodiments, the invention relates to compositions comprising a polypeptide obtainable from Nomuraea diesei and having at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to a polypeptide shown in SEQ ID NO:102, and which compositions have RNase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 102.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from trichoderma harzianum and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID No. 103, and which have rnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 103.

In some embodiments, the invention relates to compositions comprising polypeptides that are obtainable from fusarium solani and have at least 60% (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptides shown in SEQ ID NO:104, and these compositions have rnase activity. In one aspect, these polypeptides differ by up to 10 (e.g., 1,2, 3, 4, 5,6, 7, 8, 9, or 10) amino acids from the mature polypeptide shown in SEQ ID NO: 104.

Composition comprising a metal oxide and a metal oxide

The present invention relates to cleaning (e.g. detergent) compositions comprising an enzyme combination of the invention in combination with one or more additional cleaning composition components. The selection of additional components is within the ability of the skilled artisan and includes conventional ingredients, including the exemplary non-limiting components described below. The enzyme blends of the present invention comprise dnase and rnase. One embodiment of the present invention is directed to a cleaning composition comprising a dnase, an rnase and a cleaning component.

The dnase is preferably microbial, preferably obtained from a bacterium or a fungus. One embodiment of the present invention relates to a cleaning composition comprising a dnase, an rnase and a cleaning component, wherein the dnase is microbial, preferably bacterial or fungal.

In one embodiment, the dnase is obtained from a bacterium. One embodiment of the invention relates to a cleaning composition comprising a dnase, an rnase, and a cleaning component, wherein the dnase is obtained from bacillus (preferably bacillus foodborne, bacillus horikoshii, bacillus licheniformis, bacillus subtilis, bacillus hophagi, bacillus sick & research, bacillus algal curis, bacillus vietnamensis, bacillus tsunekii, bacillus indians, bacillus huanghai, or bacillus leyaensis).

The RNase is preferably obtained from Paenibacillus (e.g., Paenibacillus species-18057, Paenibacillus species-62770, Paenibacillus species-18006, Paenibacillus species-62724, Paenibacillus jellmanii). Alternatively, the RNase may be obtained from amycolatopsis coelicolor, Acremonium, Erwinia persicinum, Saccharomycosis species-62935, Saccharopolyspora endophyticus, Circi Amycolatopsis, Alcaligenes species-62516, Nomuraea diesei, Trichoderma harzianum or Fusarium solani. One embodiment of the invention relates to a cleaning composition comprising a dnase, an rnase, and a cleaning component, wherein the dnase is obtained from bacillus (preferably bacillus foodborne, bacillus horikoshii, bacillus licheniformis, bacillus subtilis, bacillus hophagus, bacillus sick & research, bacillus algal curis, bacillus vietnamensis, bacillus tsunekii, bacillus indians, bacillus huanghaii, or bacillus luysi), and wherein the rnase is selected from rnases obtained from: paenibacillus species, such as Paenibacillus species-18057, Paenibacillus species-62770, Paenibacillus species-18006, Paenibacillus species-62724 and sky blue Amycolatopsis, Acremonium, Erwinia persicinia, Saccharomyces species-62935, Saccharopolyspora endoplasmic, circi Amycolatopsis, Alcaligenes species-62516, Nomuraea diesei, Trichoderma harzianum, and Fusarium solani. One embodiment of the invention relates to a cleaning composition comprising a dnase, an rnase, and a cleaning component, wherein the dnase is obtained from bacillus (preferably bacillus foodborne, bacillus horikoshii, bacillus licheniformis, bacillus subtilis, bacillus hophagus, bacillus sick & research, bacillus algal curis, bacillus vietnamensis, bacillus tsunekii, bacillus indians, bacillus huanghaii, or bacillus luysi), and wherein the rnase is selected from:

e) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to a polypeptide set forth in SEQ ID NO. 90;

f) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 91;

g) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO 92;

h) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 93;

i) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO 94;

j) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 95;

k) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 96;

The DNase preferably belongs to the NUC1 group of DNases and comprises one or more of the motifs [ T/D/S ] [ G/N ] PQL (SEQ ID NO 69), [ F/L/Y/I ] A [ N/R ] D [ L/I/P/V ] (SEQ ID NO 70), or C [ D/N ] T [ A/R ] (SEQ ID NO: 71). Even more preferably, the DNase comprises the NUC1_ A domain [ D/Q ] [ I/V ] DH (SEQ ID NO 72). Furthermore, the DNase may comprise any of the motifs [ T/D/S ] [ G/N ] PQL, [ F/L/Y/I ] A [ N/R ] D [ L/I/P/V ] or C [ D/N ] T [ A/R ]. The dnase added to the composition of the invention preferably belongs to the group of dnases comprised in the GYS-clade, which is the group of dnases on the same branch of the phylogenetic tree with similarities in both structure and function. These NUC1 and/or NUC1_ A DNases contain the conserved motif [ D/M/L ] [ S/T ] GYSR [ D/N ] (SEQ ID NO:73) or ASXNRSKG (SEQ ID NO:74) and share similar structural and functional properties. The DNase of the GYS-clade is preferably obtained from Bacillus. One embodiment of the invention relates to a cleaning composition comprising a DNase, an RNase and a cleaning component, wherein the DNase comprises one or two motifs [ D/M/L ] [ S/T ] GYSR [ D/N ] (SEQ ID NO:73) or ASXNRSKG (SEQ ID NO: 74). One embodiment of the invention relates to a cleaning composition comprising a DNase, an RNase and a cleaning component, wherein the DNase comprises one or two motifs [ D/M/L ] [ S/T ] GYSR [ D/N ] (SEQ ID NO:73) or ASXNRSKG (SEQ ID NO:74), wherein the RNase is selected from the group consisting of:

d) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 89;

The RNase preferably comprises one or more of the motifs EYTV (SEQ ID NO 82), [ YRF ] E [ AYFCC ] D (SEQ ID NO 83), IGGD (SEQ ID NO 84), YPH, HTGA (SEQ ID NO 85) or DRV.

One embodiment of the invention relates to a cleaning composition comprising a DNase, an RNAase and a cleaning component, wherein the RNAase comprises one or more of the motifs EYTV (SEQ ID NO 82), [ YRF ] E [ AYFCC ] D (SEQ ID NO 83), IGGD (SEQ ID NO 84), YPH, HTGA (SEQ ID NO 85), DRV, and wherein the DNase comprises one or both of the motifs [ D/M/L ] [ S/T ] GYSR [ D/N ] (SEQ ID NO:73), ASNRSKG (SEQ ID NO:74), and wherein the DNase is selected from the group consisting of polypeptides of:

The DNase is preferably a Bacillus DNase, such as Bacillus foodborne, Bacillus subtilis or Bacillus licheniformis.

One embodiment of the invention relates to a cleaning composition comprising a dnase, an rnase and a cleaning component, wherein the dnase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 13.

The dnase may also be fungal, one embodiment of the present invention relates to a cleaning composition comprising a dnase, an rnase and a cleaning component, wherein the dnase is fungal, preferably obtained from aspergillus and even more preferably obtained from aspergillus oryzae, and wherein the dnase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID No. 67.

One embodiment relates to a cleaning composition comprising a dnase, an rnase and a cleaning component, wherein the dnase is fungal, preferably obtained from trichoderma and even more preferably obtained from trichoderma harzianum, and wherein the dnase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ id No. 68.

The present invention relates to cleaning compositions comprising the enzyme combination of the invention in combination with one or more additional cleaning composition components. The selection of additional components is within the ability of the skilled artisan and includes conventional ingredients, including the exemplary non-limiting components described below.

One embodiment of the present invention is directed to a composition comprising:

a) at least 0.001ppm of at least one dnase, wherein the dnase is selected from the group consisting of:

i) a DNase comprising one or more of the motifs [ T/D/S ] [ G/N ] PQL (SEQ ID NO 69), [ F/L/Y/I ] A [ N/R ] D [ L/I/P/V ] (SEQ ID NO:70), or C [ D/N ] T [ A/R ] (SEQ ID NO: 71);

ii) a DNase comprising the motif [ D/Q ] [ I/V ] DH (SEQ ID NO 72);

iii) a DNase comprising one or two motifs [ D/M/L ] [ S/T ] GYSR [ D/N ] (SEQ ID NO:73) or ASXNRSKG (SEQ ID NO: 74);

iv) a DNase comprising one or two motifs [ V/I ] PL [ S/A ] NAWK (SEQ ID NO:75) or NPQL (SEQ ID NO: 76);

v) a DNase comprising one or two motifs P [ Q/E ] L [ W/Y ] (SEQ ID NO:77) or [ K/H/E ] NAW (SEQ ID NO: 78);

vi) a dnase selected from the group consisting of: a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 1, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 2, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 3, a polypeptide having at least 60%, at least 65%, or 100% sequence identity to the polypeptide shown in SEQ ID NO. 4, A polypeptide having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 5, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 6, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 7, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% sequence identity to a polypeptide shown in SEQ ID NO, A polypeptide having at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 8, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 9, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 10, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 11, a polypeptide having at least 60%, or 100% sequence identity to the polypeptide set forth in SEQ ID, A polypeptide having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 12, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 13, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 14, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 14, A polypeptide having at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 15, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 16, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 17, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 18, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 19, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 20, a polypeptide having at least 60%, at least 65% or 100% sequence identity to the polypeptide shown in SEQ ID NO 21, A polypeptide having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 22, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 23, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 24, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% sequence identity to a polypeptide shown in SEQ ID NO, A polypeptide having at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 25, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 26, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 27, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 28, a polypeptide having at least 60%, or 100% sequence identity to the polypeptide set forth in SEQ ID, A polypeptide having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 29, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 30, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 31, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 31, A polypeptide having at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 32, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 33, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 34, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 35, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 36, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 37, a polypeptide having at least 60%, at least 65%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO 38, A polypeptide having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 39, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 40, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 41, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% sequence identity to a polypeptide shown in SEQ ID NO, A polypeptide having at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO:42, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO:43, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO:44, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO:45, a polypeptide having at least 60%, or 100% sequence identity to the polypeptide set forth in SEQ ID, A polypeptide having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 46, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 47, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 48, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 48, A polypeptide having at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 49, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 50, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 51, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 52, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 53, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 54, a polypeptide having at least 60%, at least 65% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 55, A polypeptide having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 56, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 57, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 58, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% sequence identity to a polypeptide shown in SEQ ID NO, A polypeptide having at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 59, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 60, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 61, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 62, a polypeptide having at least 60%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO 62, A polypeptide having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 63, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 63, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 64, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 65, At least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 66, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 67, and at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO. 68, and

b) at least 0.001ppm of one or more rnases, wherein the rnases are selected from the group consisting of:

i) an RNase comprising one or more of the motifs EYTV (SEQ ID NO 82), [ YRF ] E [ AYFCC ] D (SEQ ID NO 83), IGGD (SEQ ID NO 84), YPH, HTGA (SEQ ID NO 85) or DRV;

ii) an rnase selected from the group consisting of: a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 86, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 87, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 88, a polypeptide having at least 60%, at least 65%, at least 70% sequence identity to the polypeptide shown in SEQ ID NO 89, A polypeptide having at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 90, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to a polypeptide shown in SEQ ID NO. 91, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, (ii) at least, A polypeptide having at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 92, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 93, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO 95, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least, A polypeptide having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 96, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 85%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 97, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 98, A polypeptide having at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 99, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 100, a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 101, a polypeptide having at least 60% or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 102, At least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 103, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 104, and at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% sequence identity to the polypeptide set forth in SEQ ID NO. 104;

III) an rnase selected from the group of rnases comprised in e.c.3.1.26.X (wherein X ═ 1,2, 3, 4, 5,6, 7, 8, 9, 10, 11, 12 and 13), preferably a vacuolus polycephalus rnase, rnase α, rnase III, rnase C, RNA, rnase H, RNA, enzyme HII, rnase P, RNA, rnase P4, rnase M5, rnase poly-U specific, rnase IX, rnase Z, RNA, enzyme E, RNA, enzyme L, or retroviral rnase H;

iv) an rnase selected from the group of rnases comprised in ec.3.1.27.Y (wherein Y ═ 1,2, 3, 4, 5,6, 7, 8, 9, 10), preferably rnase T (2), bacillus subtilis rnase, rnase T (1), rnase U (2), pancreatic rnase, rnase A, RNA enzyme I, enterobacter rnase, rnase F, RNA enzyme V, rRNA endonuclease or rnase B; and

c) at least one cleaning component, preferably selected from surfactants, builders, bleaching components, polymers and dispersants.

Optionally, the cleaning composition comprises at least 0.001ppm of one or more protease selected from the group consisting of,

i) a protease variant of a protease parent, wherein the protease variant comprises one or more alterations in one or more of the following positions compared to the protease shown in SEQ ID NO 79 or SEQ ID NO 80: 3.4, 9, 15, 24, 27, 42, 55, 59, 60, 66, 74, 85, 96, 97, 98, 99, 100, 101, 102, 104, 116, 118, 121, 126, 127, 128, 154, 156, 157, 158, 161, 164, 176, 179, 182, 185, 188, 189, 193, 198, 199, 200, 203, 206, 211, 212, 216, 218, 226, 229, 230, 239, 246, 255, 256, 268 and 269, wherein the position corresponds to the position of the protease shown in SEQ ID NO 79, and wherein the protease variant has at least 80% sequence identity to SEQ ID NO 79, SEQ ID NO 80, or SEQ ID NO 81;

ii) a protease variant of a protease parent, wherein the protease variant comprises one or more mutations selected from the group consisting of: S3T, V4I, S9R, S9E, a15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, N85S, N85R, G96S, G96A, S97G, S99G, S101G, V102G, S104G, G116G, SEQ G116G, H118G, N120G, S G, P36127, S255G, N198, N72, N G, N36255, N G, N36255, N G;

iii) a protease comprising a substitution at one or more positions corresponding to positions 171, 173, 175, 179, or 180 of SEQ ID NO81 as compared to the protease shown in SEQ ID NO81, wherein the protease variant has at least 75% but less than 100% sequence identity to amino acids 1 to 311 of SEQ ID NO81,

a protease comprising the amino acid sequence shown in SEQ ID NO 79, 80 or 81, or a protease having at least 80% sequence identity to: a polypeptide comprising amino acids 1-269 of SEQ ID NO 79, a polypeptide comprising amino acids 1-311 of SEQ ID NO81, or a polypeptide comprising amino acids 1-275 of SEQ ID NO 80.

Rnases and dnases may be included in the cleaning compositions of the present invention at the following levels: from 0.01 to 1000ppm, from 1ppm to 1000ppm, from 10ppm to 1000ppm, from 50ppm to 1000ppm, from 100ppm to 1000ppm, from 150ppm to 1000ppm, from 200ppm to 1000ppm, from 250ppm to 750ppm, from 250ppm to 500 ppm. The above dnase may be combined with rnase to form a blend which is added to the wash solution according to the present invention. The concentration of DNase in the wash solution is typically in the range of from 0.00001ppm to 10ppm, from 0.00002ppm to 10ppm, from 0.0001ppm to 10ppm, from 0.0002ppm to 10ppm, from 0.001ppm to 10ppm, from 0.002ppm to 10ppm, from 0.01ppm to 10ppm, from 0.02ppm to 10ppm, 0.1ppm to 10ppm, from 0.2ppm to 10ppm, from 0.5ppm to 5ppm of the wash. The concentration of RNase in the wash solution is usually in the range of from 0.00001ppm to 10ppm, from 0.00002ppm to 10ppm, from 0.0001ppm to 10ppm, from 0.0002ppm to 10ppm, from 0.001ppm to 10ppm, from 0.002ppm to 10ppm, from 0.01ppm to 10ppm, from 0.02ppm to 10ppm, 0.1ppm to 10ppm, from 0.2ppm to 10ppm, from 0.5ppm to 5ppm of the wash. Dnase may be combined with any of the rnases mentioned above to form a blend that is added to the composition according to the present invention.

One embodiment relates to a cleaning composition comprising a dnase, an rnase and at least one cleaning component, wherein the amount of dnase in the composition is from 0.01 to 1000ppm and the amount of rnase is from 0.01 to 1000 ppm.

One aspect relates to a method of formulating a cleaning composition comprising a dnase, an rnase and at least one cleaning component, the method comprising adding the dnase, the rnase and the at least one cleaning component.

The selection of cleaning components may include (for textile care) the type of textile to be cleaned, the type and/or degree of soil, the temperature at which cleaning is carried out, and considerations of the formulation of the detergent product. Although the components mentioned below are classified by general headings according to specific functionality, this is not to be construed as a limitation, as the components may contain additional functionality as will be appreciated by the skilled person.

Surface active agent

The detergent composition may comprise one or more surfactants, which may be anionic and/or cationic and/or nonionic and/or semi-polar and/or zwitterionic, or mixtures thereof. In particular embodiments, the detergent composition comprises a mixture of one or more nonionic surfactants and one or more anionic surfactants. The one or more surfactants are typically present at a level of from about 0.1% to 60% (such as from about 1% to about 40%, or from about 3% to about 20%, or from about 3% to about 10%) by weight. The one or more surfactants are selected based on the desired cleaning application, and may include any conventional surfactant known in the art.

When included therein, the detergent will typically contain from about 1% to about 40% by weight of anionic surfactant, such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of anionic surfactant. Non-limiting examples of anionic surfactants include sulfates and sulfonates, specifically Linear Alkylbenzene Sulfonate (LAS), isomers of LAS, branched alkylbenzene sulfonate (BABS), phenylalkane sulfonate, alpha-olefin sulfonate (AOS), olefin sulfonate, alkene sulfonate, alkane-2, 3-diylbis (sulfate), hydroxyalkane sulfonate and disulfonate, Alkyl Sulfate (AS) such AS Sodium Dodecyl Sulfate (SDS), Fatty Alcohol Sulfate (FAS), Primary Alcohol Sulfate (PAS), alcohol ether sulfate (AES or AEOS or FES, also known AS alcohol ethoxy sulfate or fatty alcohol ether sulfate), Secondary Alkane Sulfonate (SAS), Paraffin Sulfonate (PS), ester sulfonate, sulfonated fatty acid glycerides, alpha-sulfonated fatty acid methyl esters (alpha-SFMe or SES) including Methyl Ester Sulfonate (MES), Alkyl or alkenyl succinic acids, dodecenyl/tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfosuccinic acid or fatty acid salts (soaps), and combinations thereof.

When included therein, the detergent will typically contain from about 1% to about 40% by weight of cationic surfactant, for example from about 0.5% to about 30%, particularly from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%. Non-limiting examples of cationic surfactants include alkyl dimethyl ethanol quaternary amine (ADMEAQ), Cetyl Trimethyl Ammonium Bromide (CTAB), dimethyl distearyl ammonium chloride (DSDMAC), and alkyl benzyl dimethyl ammonium, alkyl quaternary ammonium compounds, Alkoxylated Quaternary Ammonium (AQA) compounds, ester quaternary ammonium, and combinations thereof.

When included therein, the detergent will typically contain from about 0.2% to about 40% by weight of nonionic surfactant, for example from about 0.5% to about 30%, particularly from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%. Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, Propoxylated Fatty Alcohols (PFA), alkoxylated fatty acid alkyl esters (e.g., ethoxylated and/or propoxylated fatty acid alkyl esters), alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), Alkylpolyglycosides (APG), alkoxylated amines, Fatty Acid Monoethanolamides (FAM), Fatty Acid Diethanolamides (FADA), Ethoxylated Fatty Acid Monoethanolamides (EFAM), Propoxylated Fatty Acid Monoethanolamides (PFAM), polyhydroxy alkyl fatty acid amides, or N-acyl N-alkylglucamine derivatives thereof (glucamide (GA), or Fatty Acid Glucamides (FAGA)), as well as products available under the tradenames SPAN and TWEEN, and combinations thereof.

When included therein, the detergent will typically comprise from about 0.01% to about 10% by weight of a semi-polar surfactant. Non-limiting examples of semi-polar surfactants include Amine Oxides (AO), such as alkyl dimethylamine oxide, N- (cocoalkyl) -N, N-dimethylamine oxide, and N- (tallow-alkyl) -N, N-bis (2-hydroxyethyl) amine oxide, and combinations thereof.

When included therein, the detergent will typically comprise from about 0.01% to about 10% by weight of a zwitterionic surfactant. Non-limiting examples of zwitterionic surfactants include betaines, such as alkyl dimethyl betaines, sulfobetaines, and combinations thereof.

Builders and co-builders

The detergent composition may contain from about 0-65%, such as from about 5% to about 50%, by weight, of a detergent builder or co-builder, or mixtures thereof. In dishwashing detergents, the level of builder is typically from 40% to 65%, especially from 50% to 65%. The builder and/or co-builder may in particular be a chelating agent that forms a water-soluble complex with Ca and Mg. Any builder and/or co-builder known in the art for use in cleaning detergents may be utilized. Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium silicate, layered silicates (e.g., SKS-6 from Hoechst), ethanolamines such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2 '-iminodiethyl-1-ol), triethanolamine (TEA, also known as 2,2',2 "-nitrilotriethanol), and carboxymethyl inulin (CMI), and combinations thereof.

The detergent composition may also comprise 0-50% by weight, such as from about 5% to about 30% of a detergent co-builder. The detergent composition may comprise a co-builder alone or in combination with a builder, for example a zeolite builder. Non-limiting examples of co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly (acrylic acid) (PAA) or copoly (acrylic acid/maleic acid) (PAA/PMA). Additional non-limiting examples include citrates, chelating agents (such as aminocarboxylates, aminopolycarboxylates, and phosphates), and alkyl or alkenyl succinic acids. Additional specific examples include 2,2',2 "-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N, N' -disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid-N, N-diacetic acid (GLDA), 1-hydroxyethane-1, 1-diphosphonic acid (HEDP), ethylenediaminetetra (methylenephosphonic acid) (EDTMPA), diethylenetriaminepenta (methylenephosphonic acid) (DTMPA or DTPMPA), N- (2-hydroxyethyl) iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N, N-diacetic acid (ASDA), aspartic acid-N-monopropionic Acid (ASMP), iminodisuccinic acid (IDA), N- (2-sulfomethyl) -aspartic acid (SMAS), N- (2-sulfoethyl) -aspartic acid (SEAS), N- (2-sulfomethyl) -glutamic acid (SMGL), N- (2-sulfoethyl) -glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), alpha-alanine-N, N-diacetic acid (alpha-ALDA), serine-N, N-diacetic acid (SEDA), isoserine-N, N-diacetic acid (ISDA), phenylalanine-N, N-diacetic acid (PHDA), anthranilic acid-N, N-diacetic acid (ANDA), sulfanilic acid-N, N-diacetic acid (SLDA), taurine-N, N-diacetic acid (TUDA), and sulfomethyl-N, n-diacetic acid (SMDA), N- (2-hydroxyethyl) -ethylenediamine-N, N', N "-triacetate (HEDTA), Diethanolglycine (DEG), diethylenetriamine penta (methylene phosphonic acid) (DTPMP), aminotri (methylene phosphonic Acid) (ATMP), and combinations and salts thereof. Further exemplary builders and/or co-builders are described in e.g. WO 09/102854, US 5977053

Bleaching system

The detergent may contain 0-30% by weight, for example from about 1% to about 20% of a bleaching system. Any bleaching system comprising components known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include a source of hydrogen peroxide; a source of peracid; and a bleach catalyst or booster.

Hydrogen peroxide source:

suitable sources of hydrogen peroxide are inorganic persalts including alkali metal salts such as sodium percarbonate and sodium perborate (usually mono-or tetrahydrate), and hydrogen peroxide-urea (1/1).

A peracid source:

the peracid may be (a) incorporated directly as a preformed peracid, or (b) formed in situ in the wash liquor from hydrogen peroxide and a bleach activator (perhydrolysis), or (c) formed in situ in the wash liquor from hydrogen peroxide and catalase and a suitable substrate for the latter (e.g. an ester).

a) Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids (e.g., peroxycarboxylic acids)Peroxybenzoic acid) and its ring-substituted derivatives, peroxy-alpha-naphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, epsilon-phthalimidoperoxycaproic acid [ Phthalimidoperoxycaproic Acid (PAP)]And o-carboxybenzoylamino peroxycaproic acid; aliphatic and aromatic diperoxy dicarboxylic acids, such as diperoxydodecanedioic acid, diperoxynonadioic acid, diperoxydecanedioic acid, diperoxydecanoic acid, 2-decyldiperoxysuccinic acid, and diperoxyphthalic acid, -isophthalic acid and-terephthalic acid; perimidineic acid; peroxymonosulfuric acid; peroxydisulfuric acid; peroxyphosphoric acid; peroxysilicic acid; and mixtures of said compounds. It will be appreciated that in some cases it may be desirable to add the peracid as a suitable salt, such as an alkali metal salt (e.g. alkali metal salt)

) Or an alkaline earth metal salt.

b) Suitable bleach activators include those belonging to the class of esters, amides, imides, nitriles or anhydrides, and, where applicable, salts thereof. Suitable examples are Tetraacetylethylenediamine (TAED), sodium 4- [ (3,5, 5-trimethylhexanoyl) oxy ] benzene-1-sulfonate (ISONOBS), sodium 4- (dodecanoyloxy) benzene-1-sulfonate (LOBS), sodium 4- (decanoyloxy) benzene-1-sulfonate, sodium 4- (decanoyloxy) benzoic acid (DOBA), sodium 4- (nonanoyloxy) benzene-1-sulfonate (NOBS), and/or those disclosed in WO 98/17767. A particular family of bleach activators of interest is disclosed in EP624154 and particularly preferred in this family is Acetyl Triethyl Citrate (ATC). ATC or short chain triglycerides like triacetin have the advantage that they are environmentally friendly. In addition, acetyl triethyl citrate and triacetin have good hydrolytic stability in the product upon storage and are effective bleach activators. Finally, ATC is multifunctional in that citrate released in the perhydrolysis reaction may act as a builder.

Bleach catalysts and boosters

The bleaching system may also include a bleach catalyst or booster.

Some non-limiting examples of bleach catalysts that may be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese collagen, cobalt-amine catalysts and manganese triazacyclononane (MnTACN) catalysts; particular preference is given to complexes of manganese with 1,4, 7-trimethyl-1, 4, 7-triazacyclononane (Me3-TACN) or 1,2,4, 7-tetramethyl-1, 4, 7-triazacyclononane (Me4-TACN), in particular Me3-TACN, such as binuclear manganese complexes [ (Me3-TACN) Mn (O)3Mn (Me3-TACN) ] (PF6)2, and [2,2',2 "-nitrilotris (ethane-1, 2-diylazalkylidene-kappa N-methylidene) triphenolo-kappa 3O ] manganese (III). These bleach catalysts may also be other metal compounds, such as iron or cobalt complexes.

In some embodiments, where a source of peracid is included, an organic bleach catalyst or bleach booster having one of the following formulas may be used:

(iii) and mixtures thereof; wherein each R1 is independently a branched alkyl group containing from 9 to 24 carbons or a linear alkyl group containing from 11 to 24 carbons, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbons or a linear alkyl group containing from 11 to 18 carbons, more preferably each R1 is independently selected from the group consisting of: 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl and isotentadecyl.

Other exemplary bleaching systems are described in, for example, WO2007/087258, WO2007/087244, WO2007/087259, EP1867708 (vitamin K), and WO 2007/087242. Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.

Metal care agent

Metal care agents can prevent or reduce the tarnishing, corrosion or oxidation of metals, including aluminum, stainless steel and non-ferrous metals such as silver and copper. Suitable examples include one or more of the following:

(a) benzotriazoles, including benzotriazole or bis-benzotriazole and substituted derivatives thereof. Benzotriazole derivatives are those compounds in which the available substitution sites on the aromatic ring are partially or fully substituted. Suitable substituents include straight-chain or branched Ci-C20-alkyl groups (e.g. C1-C20-alkyl groups) and hydroxy, thio, phenyl or halogen (e.g. fluorine, chlorine, bromine and iodine);

(b) metal salts and complexes selected from the group consisting of: zinc, manganese, titanium, zirconium, hafnium, vanadium, cobalt, gallium and cesium salts and/or complexes, these metals being in one of the oxidation states II, III, IV, V or VI. In one aspect, suitable metal salts and/or metal complexes may be selected from the group consisting of: mn (II) sulfate, Mn (II) citrate, Mn (II) stearate, Mn (II) acetylacetonate, K ^ TiF6 (e.g., K2TiF6), K ^ ZrF6 (e.g., K2ZrF6), CoSO4, Co (NOs)2, and Ce (NOs)3, a zinc salt, e.g., zinc sulfate, hydrozincite, or zinc acetate;

(c) silicates including sodium or potassium silicate, sodium disilicate, sodium silicate, crystalline layered silicates, and mixtures thereof.

Further suitable organic and inorganic redox active substances for use as silver/copper corrosion inhibitors are disclosed in WO 94/26860 and WO 94/26859. Preferably, the composition of the present invention comprises from 0.1% to 5% by weight of the composition of the metal benefit agent, preferably the metal benefit agent is a zinc salt.

Hydrotropic agent

The detergent may comprise 0-10% by weight, such as 0-5% by weight, for example from about 0.5% to about 5%, or from about 3% to about 5% of a hydrotrope. Any hydrotrope known in the art for use in detergents can be utilized. Non-limiting examples of hydrotropes include sodium benzene sulfonate, sodium p-toluene sulfonate (STS), Sodium Xylene Sulfonate (SXS), Sodium Cumene Sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyethylene glycol ethers, sodium hydroxynaphthalene formate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfonate, and combinations thereof.

Polymer and method of making same

The detergent may contain 0-10% (e.g., 0.5% -5%, 2% -5%, 0.5% -2% or 0.2%) by weight1%) of a polymer. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as mentioned above, or may provide anti-redeposition, fibre protection, soil release, dye transfer inhibition, oil cleaning and/or suds suppression properties. Some polymers may have more than one of the above-mentioned properties and/or more than one of the below-mentioned motifs. Exemplary polymers include (carboxymethyl) cellulose (CMC), poly (vinyl alcohol) (PVA), poly (vinylpyrrolidone) (PVP), poly (ethylene glycol) or poly (ethylene oxide) (PEG), ethoxylated poly (ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers, hydrophobically modified CMC (HM-CMC) and silicone, copolymers of terephthalic acid and oligoethylene glycol, copolymers of poly (ethylene terephthalate) and poly (ethylene oxide terephthalate) (PET-POET), PVP, poly (vinylimidazole) (PVI), poly (vinylpyridine-N-oxide) (PVPO or PVPNO), and polyvinylpyrrolidone-vinylimidazole (PVPVI). Suitable examples include PVP-K15, PVP-K30, Chromabond S-400, Chromabond S-403E and Chromabond S-100 from Ashl and Aqualon, and from BASF

HP 165、

HP 50 (dispersant),

HP 53 (dispersant),

HP 59 (dispersant),

HP 56 (dye transfer inhibitors),

HP 66K (dye transfer)Migration inhibitors). Additional exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO), and diquaternary ammonium ethoxysulfate. Other exemplary polymers are disclosed in, for example, WO 2006/130575. Salts of the above-mentioned polymers are also contemplated. Particularly preferred polymers are ethoxylated homopolymers from BASFHP20, which helps prevent redeposition of soil in the wash liquor.

Fabric toner

The detergent composition of the present invention may also comprise a fabric hueing agent, such as a dye or pigment, which when formulated in a detergent composition, may deposit on a fabric when said fabric is contacted with a wash liquor which comprises said detergent composition and which therefore changes the colour of said fabric by absorption/reflection of visible light. Optical brighteners emit at least some visible light. In contrast, when fabric hueing agents absorb at least part of the visible spectrum, they change the color of the surface. Suitable fabric hueing agents include dyes and dye-clay conjugates, and may also include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include those selected from the group consisting of the following dyes falling into the color Index (Colour Index) (c.i.): direct blue, direct red, direct violet, acid blue, acid red, acid violet, basic blue, basic violet and basic red, or mixtures thereof, for example as described in WO2005/03274, WO2005/03275, WO2005/03276 and EP1876226 (which are hereby incorporated by reference). The detergent composition preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.0001 wt% to about 0.04 wt% fabric hueing agent. The composition may comprise from 0.0001 wt% to 0.2 wt% of a fabric hueing agent, which may be particularly preferred when the composition is in the form of a unit dose pouch. Suitable toners are also disclosed in, for example, WO 2007/087257 and WO 2007/087243.

Enzyme

The detergent additive together with the detergent composition may comprise one or more additional enzymes, such as one or more lipases, cutinases, amylases, carbohydrases, cellulases, pectinases, mannanases, arabinases, galactanases, xylanases, oxidases, such as laccases, and/or peroxidases.

In general, the characteristics of the enzyme or enzymes selected should be compatible with the detergent selected (i.e., pH optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme or enzymes should be present in an effective amount.

Protease enzyme

The term "protease" is defined herein as an enzyme that hydrolyzes peptide bonds. It includes any enzyme belonging to the EC3.4 enzyme group (including each of its 13 subclasses). EC numbering refers to Enzyme Nomenclature 1992[1992 Enzyme Nomenclature ], Academic Press [ Academic Press ], san Diego, Calif., from NC-IUBMB, included in Eur.J. biochem [ European journal of biochemistry ], 1223:1-5 (1994); biochem [ journal of european biochemistry ], 232:1-6 (1995); biochem [ european journal of biochemistry ], 237:1-5 (1996); biochem [ journal of european biochemistry ], 250:1-6 (1997); and supplement 1-5 published in Eur.J.biochem. [ European Biochemical journal ], 264: 610-. The protease most widely used in the detergent industry (e.g. laundry and dish wash) is serine protease. Serine proteases are a subgroup of proteases characterized by having a serine at the active site, forming a covalent adduct with a substrate. Serine proteases are characterized by having two active site amino acid residues other than serine, namely a histidine residue and an aspartic acid residue. According to Siezen et al, 1991, Protein Engng. [ Protein engineering ]4: 719-. Subtilases can be divided into 6 subsections, namely the subtilisin family, the thermolysin (thermolase) family, the proteinase K family, the lantibiotic peptidase family, the Kexin family and the Pyrolysin family. The term "protease activity" means proteolytic activity (EC 3.4). The protease enzyme useful in the cleaning compositions of the present invention is primarily an endopeptidase (EC 3.4.21). There are several protease activity types: the three main types of activity are: trypsin-like, where cleavage of the amide substrate occurs after Arg or Lys at P1, chymotrypsin-like, where cleavage occurs after one hydrophobic amino acid at P1, and elastase-like, where cleavage occurs after Ala at P1. For the purposes of the present invention, protease activity is determined according to the Suc-AAPF-pNA activity assay.

Suitable proteases for the compositions of the invention include those of bacterial, fungal, plant, viral or animal origin, for example of plant or microbial origin. Preferably of microbial origin. Chemically modified mutants or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. The serine protease may, for example, be of the S1 family (e.g.trypsin) or of the S8 family (e.g.subtilisin). The metalloprotease may for example be a thermolysin from e.g. the M4 family or other metalloprotease such as those from the M5, M7 or M8 families.

Examples of subtilases are those derived from Bacillus, such as Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii, described in US 7262042 and WO 09/021867; and subtilisin retardation (lentus), subtilisin noro (Novo), subtilisin Carlsberg (Carlsberg), bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO 89/06279 and protease PD138 described in WO 93/18140. Other useful proteases may be those described in WO 92/175177, WO 01/016285, WO 02/026024 and WO 02/016547. Examples of trypsin-like proteases are trypsin (e.g.of porcine or bovine origin) and Fusarium protease (described in WO 89/06270, WO 94/25583 and WO 05/040372), and chymotrypsin derived from Cellulomonas (described in WO05/052161 and WO 05/052146).

Further preferred proteases are alkaline proteases from Bacillus lentus DSM 5483 (as described in e.g.WO 95/23221), and variants thereof (described in WO 92/21760, WO 95/23221, EP 1921147 and EP 1921148).

Examples of metalloproteases are neutral metalloproteases as described in WO 07/044993 (Jenergic International Inc. (Genencor Int.)), such as those derived from Bacillus amyloliquefaciens.

Examples of useful proteases are the variants described in: WO 92/19729, WO 96/034946, WO 98/20115, WO 98/20116, WO 99/011768, WO 01/44452, WO 03/006602, WO 04/03186, WO 04/041979, WO 07/006305, WO 11/036263, WO 11/036264, in particular protease variants comprising substitutions at one or more of the following positions: 3.4, 9, 15, 24, 27, 42, 55, 59, 60, 66, 74, 85, 96, 97, 98, 99, 100, 101, 102, 104, 116, 118, 121, 126, 127, 128, 154, 156, 157, 158, 161, 164, 176, 179, 182, 185, 188, 189, 193, 198, 199, 200, 203, 206, 211, 212, 216, 218, 226, 229, 230, 239, 246, 255, 256, 268 and 269, wherein the positions correspond to the positions of the B.lentus protease shown in SEQ ID NO 69. More preferred protease variants may comprise one or more mutations selected from the group consisting of: S3T, V4I, S9R, S9E, a15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, N85S, N85R, G96S, G96A, S97G, S99G, S101G, V102G, S104G, G116G, H118G, N120G, S G, P36127, S255G, S42, S G, N198, N G, N36255, N G, N36255, N G. The protease variant is preferably a Bacillus lentus protease shown in SEQ ID NO 79Or the variant of bacillus amyloliquefaciens protease (BPN') shown in SEQ ID NO 80. These protease variants preferably have at least 80% sequence identity with SEQ ID NO 79 or SEQ ID NO 80.

A protease variant comprising a substitution at one or more positions corresponding to positions 171, 173, 175, 179 or 180 of SEQ ID No. 81, wherein said protease variant has at least 75% but less than 100% sequence identity to SEQ ID No. 81.

Suitable commercially available proteases include those sold under the following trade names:

Duralase^Tm、Durazym^Tm、

Ultra、

Ultra、Blaze

100T、Blaze

125T、Blaze

150T、

and(novicent corporation), those sold under the following trade names:

Purafect

ExcellenzP1000^TM、Excellenz P1250^TM、

Preferenz P100^TM、Purafect

Preferenz P110^TM、Effectenz P1000^TM、

Effectenz P1050^TM、

Effectenz P2000^TM、

and

(Danisco)/DuPont (DuPont)), Axappem^TM(Gistbres Brocases N.V.), BLAP (sequence shown in FIG. 29 of US 5352604) and variants thereof (Henkel AG) and KAP (Bacillus alcalophilus subtilisin) from Kao.

Cellulase enzymes

Suitable cellulases include those of bacterial or fungal origin. Chemically modified mutants or protein engineered mutants are included. Suitable cellulases include cellulases from bacillus, pseudomonas, humicola, fusarium, clostridium, acremonium, such as fungal cellulases produced by humicola insolens, myceliophthora thermophila and fusarium oxysporum as disclosed in US 4,435,307, US5,648,263, US5,691,178, US5,776,757 and WO 89/09259.

Particularly suitable cellulases are the alkaline or neutral cellulases having color care benefits. Examples of such cellulases are the cellulases described in EP 0495257, EP 0531372, WO 96/11262, WO 96/29397, WO 98/08940. Further examples are cellulase variants such as those described in WO 94/07998, EP 0531315, US5,457,046, US5,686,593, US5,763,254, WO 95/24471, WO 98/12307 and WO 99/001544.

Other cellulases are endo-beta-1, 4-glucanases having a sequence with at least 97% identity to the amino acid sequence from position 1 to position 773 of SEQ ID No. 2 of WO 2002/099091, or a family 44 xyloglucanase having a sequence with at least 60% identity to positions 40-559 of SEQ ID No. 2 of WO 2001/062903.

Commercially available cellulases include Celluzyme^TMAnd Carezyme^TM(Novozymes A/S), Carezyme Premium^TM(Novoxil Co., Ltd.) Celluclean^TM(Novoxil Co., Ltd.) Celluclean Classic^TM(Novoxin Co., Ltd.) Cellusoft^TM(Novoxin Co.), Whitezyme^TM(Novoxil, Inc.), Clazinase^TMAnd Puradax HA^TM(Jencology International Inc.) and KAC-500(B)^TM(Kao corporation )).

Mannanase

Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. The mannanase may be an alkaline mannanase of family 5 or 26. It may be a wild type from the genus Bacillus or Humicola, in particular Bacillus mucosae, Bacillus licheniformis, Bacillus alkalophilus, Bacillus clausii or Humicola insolens. Suitable mannanases are described in WO 1999/064619. The commercially available mannanase is Mannaway (novicent).

Peroxidase/oxidase

Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified mutants or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus (e.g., from Coprinus cinereus), and variants thereof, such as those described in WO 93/24618, WO 95/10602, and WO 98/15257. Commercially available peroxidases include Guardzyme^TM(Novixin Co.).

Lipase and cutinase:

suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipases from the genus Thermomyces, for example from Thermomyces lanuginosus (earlier named Humicola lanuginosa) as described in EP258068 and EP 305216; cutinases from the genus Humicola, such as Humicola insolens (WO 96/13580); lipases from strains of the genus pseudomonas (some of these are now renamed to burkholderia), such as pseudomonas alcaligenes or pseudoalcaligenes alcaligenes (EP218272), pseudomonas cepacia (EP331376), pseudomonas strain SD705(WO 95/06720 and WO 96/27002), pseudomonas wisconsiensis (p.wisconsinensis) (WO 96/12012); GDSL-type Streptomyces lipases (WO 10/065455); cutinases from Pyricularia oryzae (WO 10/107560); cutinases from pseudomonas mendocina (US5,389,536); lipases from Thermobifidafusca (WO 11/084412); geobacillus stearothermophilus lipase (WO 11/084417); lipases from Bacillus subtilis (WO 11/084599); and lipases (WO 12/137147) from Streptomyces griseus (WO 11/150157) and Streptomyces pristinaespiralis (S.pristinaespiralis).

Further examples are lipase variants, such as those described in EP407225, WO 92/05249, WO 94/01541, WO 94/25578, WO 95/14783, WO 95/30744, WO 95/35381, WO 95/22615, WO 96/00292, WO 97/04079, WO 97/07202, WO 00/34450, WO 00/60063, WO 01/92502, WO 07/87508 and WO 09/109500.

Preferred commercial lipase products include Lipolase^TM、Lipex^TM；Lipolex^TMAnd Lipoclean^TM(Novoxin, Inc.), Lumafast (from Jencoraceae, Inc. (Genencor)), and Lipomax (from Giste Brocads, Inc. (Gist-Brocades)).

Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, such as acyltransferase with homology to Candida antarctica lipase A (WO 10/111143), acyltransferase from Mycobacterium smegmatis (WO 05/56782), perhydrolase from the CE 7 family (WO 09/67279) and variants of Mycobacterium smegmatis perhydrolase, in particular the S54V variant used in commercial product title Power Bleach from Huntingman Textile dyeing, Inc. (Huntsman Textile Effects Pte Ltd) (WO 10/100028).

Amylase:

suitable amylases include alpha-amylase and/or glucoamylase and may be of bacterial or fungal origin. Chemically modified mutants or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a specific strain of Bacillus licheniformis (described in more detail in GB 1,296,839).

Suitable amylases include those having SEQ ID NO. 2 of WO 95/10603 or variants thereof having 90% sequence identity to SEQ ID NO. 3. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and in SEQ ID No. 4 of WO 99/019467, such as variants having substitutions in one or more of the following positions: 15. 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444.

Different suitable amylases include the amylase having SEQ ID NO 6 of WO 02/010355 or a variant thereof having 90% sequence identity to SEQ ID NO 6. Preferred variants of SEQ ID NO 6 are those having deletions in positions 181 and 182 and substitutions in position 193.

Other suitable amylases are hybrid alpha-amylases comprising residues 1-33 of the B.amyloliquefaciens-derived alpha-amylase shown in SEQ ID NO 6 of WO 2006/066594 and residues 36-483 of the B.licheniformis alpha-amylase shown in SEQ ID NO 4 of WO 2006/066594 or variants thereof having 90% sequence identity. Preferred variants of this hybrid alpha-amylase are those having a substitution, deletion or insertion in one or more of the following positions: g48, T49, G107, H156, A181, N190, M197, I201, A209, and Q264. Most preferred variants of hybrid alpha-amylases comprising residues 1-33 of the bacillus amyloliquefaciens derived alpha-amylase shown in SEQ ID No. 6 of WO 2006/066594 and residues 36-483 of SEQ ID No. 4 are those having the following substitutions:

M197T；

H156Y + a181T + N190F + a209V + Q264S; or

G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S。

Further suitable amylases are those having SEQ ID NO 6 of WO 99/019467 or variants thereof having 90% sequence identity to SEQ ID NO 6. Preferred variants of SEQ ID No. 6 are those having a substitution, deletion or insertion in one or more of the following positions: r181, G182, H183, G184, N195, I206, E212, E216 and K269. Particularly preferred amylases are those having a deletion in positions R181 and G182, or positions H183 and G184.

Further amylases which may be used are those having SEQ ID NO 1, SEQ ID NO 3, SEQ ID NO 2 or SEQ ID NO 7 of WO 96/023873 or variants thereof having 90% sequence identity to SEQ ID NO 1, SEQ ID NO 2, SEQ ID NO 3 or SEQ ID NO 7. Preferred variants of SEQ ID NO 1,2, 3 or 7 are those having substitutions, deletions or insertions in one or more of the following positions: 140. 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96/023873 for numbering. More preferred variants are those having a deletion in two positions selected from 181, 182, 183 and 184 (e.g., 181 and 182, 182 and 183, or positions 183 and 184). The most preferred amylase variants of SEQ ID NO 1, SEQ ID NO 2 or SEQ ID NO 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.

Other amylases which may be used are those having SEQ ID NO 2 of WO 08/153815, SEQ ID NO 10 of WO01/66712 or variants thereof having 90% sequence identity to SEQ ID NO 2 of WO 08/153815 or 90% sequence identity to SEQ ID NO 10 of WO 01/66712. Preferred variants of SEQ ID No. 10 in WO01/66712 are those having substitutions, deletions or insertions in one or more of the following positions: 176. 177, 178, 179, 190, 201, 207, 211 and 264.

Further suitable amylases are those of SEQ ID NO. 2 of WO 09/061380 or variants thereof having 90% sequence identity to SEQ ID NO. 2. Preferred variants of SEQ ID No. 2 are those having a C-terminal truncation and/or substitution, deletion or insertion in one or more of the following positions: q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444, and G475. More preferred variants of SEQ ID No. 2 are those having a substitution at one or more of the following positions: Q87E, R, Q98R, S125A, N128C, T131I, T165I, K178L, T182G, M201L, F202Y, N225E, R, N272E, R, S243 35243 243Q, a, E, D, Y305R, R309A, Q320R, Q359E, K444E, and G475K, and/or those having deletions at positions R180 and/or S181 or T182 and/or G183. The most preferred amylase variants of SEQ ID NO 2 are those having the following substitutions:

N128C+K178L+T182G+Y305R+G475K；

N128C+K178L+T182G+F202Y+Y305R+D319T+G475K；

S125A + N128C + K178L + T182G + Y305R + G475K; or

S125A + N128C + T131I + T165I + K178L + T182G + Y305R + G475K, wherein the variants are C-terminally truncated and optionally further comprise a substitution at position 243 and/or a deletion at position 180 and/or position 181.

Further suitable amylases are those having SEQ ID NO. 1 of WO 13184577 or variants thereof having 90% sequence identity to SEQ ID NO. 1. Preferred variants of SEQ ID No. 1 are those having a substitution, deletion or insertion in one or more of the following positions: k176, R178, G179, T180, G181, E187, N192, M199, I203, S241, R458, T459, D460, G476, and G477. More preferred variants of SEQ ID No. 1 are those having substitutions at one or more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241QADN, R458N, T459S, D460T, G476K, and G477K, and/or those with deletions in positions R178 and/or S179 or T180 and/or G181. The most preferred amylase variants of SEQ ID NO:1 are those having the following substitutions:

E187P+I203Y+G476K

E187P+I203Y+R458N+T459S+D460T+G476K

wherein the variants optionally further comprise a substitution at position 241 and/or a deletion at position 178 and/or position 179.

Further suitable amylases are those having SEQ ID NO. 1 of WO 10104675 or variants thereof having 90% sequence identity to SEQ ID NO. 1. Preferred variants of SEQ ID No. 1 are those having a substitution, deletion or insertion in one or more of the following positions: n21, D97, V128, K177, R179, S180, I181, G182, M200, L204, E242, G477 and G478. More preferred variants of SEQ ID No. 1 are those having substitutions at one or more of the following positions: N21D, D97N, V128I, K177L, M200L, L204YF, E242QA, G477K, and G478K, and/or those with deletions in positions R179 and/or S180 or I181 and/or G182. The most preferred amylase variants of SEQ ID NO:1 are those having the following substitutions:

N21D+D97N+V128I

wherein the variants optionally further comprise a substitution at position 200 and/or a deletion at position 180 and/or position 181.

Other suitable amylases are alpha-amylases with SEQ ID NO 12 in WO01/66712 or variants having at least 90% sequence identity with SEQ ID NO 12. Preferred amylase variants are those having substitutions, deletions or insertions in one or more of the following positions in SEQ id No. 12 in WO 01/66712: r28, R118, N174; r181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; r320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particularly preferred amylases include variants having deletions of D183 and G184 and having substitutions R118K, N195F, R320K and R458K, and additionally having substitutions in one or more positions selected from the group consisting of: m9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and a339, most preferred are variants additionally having substitutions in all these positions.

Other examples are amylase variants such as those described in WO 2011/098531, WO 2013/001078 and WO 2013/001087.

A commercially available amylase is Duramyl^TM、Termamyl^TM、Fungamyl^TM、Stainzyme^TM、StainzymePlus^TM、Natalase^TMLiquozyme X and BAN^TM(from Novit Inc.), and Rapidase^TM、Purastar^TM/Effectenz^TMPowerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Jenenaceae International Inc./DuPont).

Peroxidase/oxidase

The peroxidase according to the invention is an enzyme defined by the international commission on the nomenclature of the biochemistry and molecular biology alliance (IUBMB), encompassed by the enzyme classification EC 1.11.1.7, or any fragment derived therefrom which exhibits peroxidase activity.

Suitable peroxidases include those of plant, bacterial or fungal origin. Chemically modified mutants or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, for example Coprinus cinereus (C.cinerea) (EP 179,486), and variants thereof, such as those described in WO 93/24618, WO 95/10602 and WO 98/15257.

Suitable peroxidases include haloperoxidases, such as chloroperoxidase, bromoperoxidase, and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidase (e.c.1.11.1.10) catalyzes the formation of hypochlorite from chloride ions. Preferably, the haloperoxidase is a vanadium haloperoxidase, i.e. a vanadate-containing haloperoxidase. Haloperoxidases have been isolated from a number of different fungi, in particular from the group of the fungi hyphomycetes, such as the genera Caldariomyces (e.g. Hemeromyces coaliphora), Alternaria, Curvularia (e.g. Curvularia verruculosa) and Curvularia inequality (C.inaegus), Helminthosporium, Geobacillus and Botrytis.

Haloperoxidases have also been isolated from bacteria such as the genera Pseudomonas, such as P.pyrrolidonia, and Streptomyces, such as S.aureofaciens.

Suitable oxidases include in particular any laccase comprised by the enzyme classification EC 1.10.3.2 or any fragment derived therefrom exhibiting laccase activity, or compounds exhibiting similar activity, such as catechol oxidase (EC 1.10.3.1), o-aminophenol oxidase (EC 1.10.3.4) or bilirubin oxidase (EC 1.3.3.5). Preferred laccases are enzymes of microbial origin. The enzyme may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include laccases that may be derived from the following strains: aspergillus, neurospora (e.g., neurospora crassa), sphaerotheca, botrytis, lysimachia (colleibia), Fomes (Fomes), lentinus, pleurotus, trametes (e.g., trametes hirsutella and trametes versicolor), rhizoctonia (e.g., rhizoctonia solani (r. solani)), coprinus (e.g., coprinus cinereus, coprinus pilosus (c.comatus), coprinus floridus (c.friesii), and c.icatilis), podophyllum (psammophila) (e.g., podophyllum leucotrichum (p.condurana)), plenopus (e.g., podophyllum tricornutum (p.papiliacus)), myceliophthora (e.g., myceliophthora thermophilus), Schytalidium (e.g., s thermophilus), physalsolium (e.g., p.pinus), polyporus pinus (e.g., pinus), podophyllum (e.g., pinus), trichoderma guanidium (wo.857.857.g., trichoderma), or podophyllum (p.g., trichoderma). Suitable examples from bacteria include laccases which may be derived from strains of bacillus. Preferred are laccases derived from Coprinus or myceliophthora; in particular laccase derived from Coprinus cinereus, as disclosed in WO 97/08325; or from myceliophthora thermophila, as disclosed in WO 95/33836.

Dispersing agent

The cleaning compositions of the present invention may also contain a dispersant. In particular, the powdered detergent may contain a dispersant. Suitable water-soluble organic materials include homo-or co-polymeric acids or salts thereof, wherein the polycarboxylic acid comprises at least two carboxyl groups separated from each other by not more than two carbon atoms. Suitable dispersants are described, for example, in Powdered Detergents, Surfactant science series, volume 71, Marcel Dekker, Inc.

Dye transfer inhibitors

The cleaning compositions of the present invention may also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones, and polyvinylimidazoles or mixtures thereof. When present in the subject compositions, the dye transfer inhibiting agents may be present at a level of from about 0.0001% to about 10%, from about 0.01% to about 5%, or even from about 0.1% to about 3%, by weight of the composition.

Fluorescent whitening agent

The cleaning compositions of the present invention will preferably also comprise additional components which may colour the article being cleaned, for example optical brighteners or optical brighteners. When present, the brightener is preferably present at a level of about 0.01% to about 0.5%. Any fluorescent whitening agent suitable for use in laundry detergent compositions may be used in the compositions of the present invention. The most commonly used fluorescent whitening agents are those belonging to the following classes: diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and diphenyl-distyryl derivatives. Examples of diaminostilbene-sulphonic acid derivative types of optical brighteners include the following sodium salts: 4,4' -bis- (2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2, 2' -disulfonate, 4' -bis- (2, 4-dianilino-s-triazin-6-ylamino) stilbene-2, 2' -disulfonate, 4' -bis- (2-anilino-4- (N-methyl-N-2-hydroxy-ethylamino) -s-triazin-6-ylamino) stilbene-2, 2' -disulfonate, 4' -bis- (4-phenyl-1, 2, 3-triazol-2-yl) stilbene-2, 2' -disulfonate and sodium 5- (2H-naphtho [1,2-d ] [1,2,3] triazol-2-yl) -2- [ (E) -2-phenylethenyl ] benzenesulfonate. Preferred optical brighteners are Tianlibao (Tinopal) DMS and Tianlibao CBS available from Ciba-Geigy AG (Basel, Switzerland). Heliotrope DMS is the disodium salt of 4,4 '-bis- (2-morpholino-4-anilino-s-triazin-6-ylamino) stilbene-2, 2' -disulfonate. Celecoxib CBS is the disodium salt of 2,2' -bis- (phenyl-styryl) -disulfonate. It is also preferred that the optical brightener is commercially available as ParawhiteKX, supplied by Paramon Minerals and Chemicals, Inc., of Monmony, India. Other fluorescers suitable for use in the present invention include 1-3-diarylpyrazolines and 7-aminoalkylcoumarins. Suitable levels of fluorescent brightener include lower levels from about 0.01 wt%, from 0.05 wt%, from about 0.1 wt%, or even from about 0.2 wt% to higher levels of 0.5 wt% or even 0.75 wt%.

Soil release polymers

The cleaning compositions of the present invention may also include one or more soil release polymers that aid in the removal of soil from fabrics such as cotton and polyester based fabrics, and in particular the removal of hydrophobic soil from polyester based fabrics. Soil release polymers may for example be nonionic or anionic terephthalate based polymers, polyvinylcaprolactam and related copolymers, vinyl graft copolymers, polyester polyamides, see for example Powdered Detergents, Surfactant science series, volume 71, chapter 7, Marcel Dekker, Inc. Another type of soil release polymer is an amphiphilic alkoxylated greasy cleaning polymer comprising a core structure and a plurality of alkoxylated groups attached to the core structure. The core structure may comprise a polyalkyleneimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523 (incorporated herein by reference). In addition, random graft copolymers are suitable soil release polymers. Suitable graft copolymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/113314 (incorporated herein by reference). Suitable polyethylene glycol polymers include random graft copolymers comprising: (i) a hydrophilic backbone comprising polyethylene glycol; and (ii) one or more side chains selected from the group consisting of: C4-C25 alkyl groups, polypropylene, polybutylene, vinyl esters of saturated C1-C6 monocarboxylic acids, Cl-C6 alkyl esters of acrylic or methacrylic acid, and mixtures thereof. Suitable polyethylene glycol polymers have a polyethylene glycol backbone with randomly grafted polyvinyl acetate side chains. The average molecular weight of the polyethylene glycol backbone ranges from 2,000Da to 20,000Da, or from 4,000Da to 8,000 Da. The molecular weight ratio of the polyethylene glycol backbone to the polyvinyl acetate side chains may range from 1:1 to 1:5, or from 1:1.2 to 1: 2. The average number of grafting sites per ethylene oxide unit may be less than 1, or less than 0.8, the average number of grafting sites per ethylene oxide unit may be in the range of 0.5 to 0.9, or the average number of grafting sites per ethylene oxide unit may be in the range of 0.1 to 0.5, or 0.2 to 0.4. A suitable polyethylene glycol polymer is Sokalan HP 22. Other soil release polymers are substituted polysaccharide structures, especially substituted cellulose structures, such as modified cellulose derivatives, such as those described in EP 1867808 or WO 2003/040279 (both incorporated herein by reference). Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides, and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, non-ionically modified cellulose, cationically modified cellulose, zwitterionic modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methyl cellulose, carboxymethyl cellulose, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, ester carboxymethyl cellulose, and mixtures thereof.

Anti-redeposition agent

The cleaning compositions of the present invention may also include one or more anti-redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and/or polyethylene glycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimine. The cellulose-based polymers described above under soil release polymers may also function as anti-redeposition agents.

Rheology modifier

The cleaning compositions of the present invention may also include one or more rheology modifiers, structurants, or thickeners, other than viscosity reducers. The rheology modifier is selected from the group consisting of: non-polymeric crystalline, hydroxyl functional materials, polymeric rheology modifiers which impart shear thinning characteristics to the aqueous liquid phase matrix of the liquid detergent composition. The rheology and viscosity of the detergent may be modified and adjusted by methods known in the art, for example, as shown in EP 2169040.

Other suitable cleaning composition components include, but are not limited to, anti-shrink agents, anti-wrinkle agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam modulators, hydrotropes, perfumes, pigments, suds suppressors, solvents, and structurants and/or structure elasticizing agents for liquid detergents.

Formulation of detergent products

The cleaning composition of the present invention may be in any conventional form, such as a bar, a homogeneous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compressed powder, a granule, a paste, a gel, or a regular, compressed or concentrated liquid.

The bag may be configured as a single chamber or as multiple chambers. It may be of any form, shape and material suitable for holding the composition, e.g. not allowing the composition to be released from the bag before contact with water. The bag is made of a water-soluble film that contains an interior volume. The interior volume may be divided into chambers of bags. Preferred films are polymeric materials, preferably polymers that form films or sheets. Preferred polymers, copolymers or derivatives thereof are selected from polyacrylates, and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylates, most preferably polyvinyl alcohol copolymers and Hydroxypropylmethylcellulose (HPMC). Preferably, the level of polymer in the film, e.g., PVA, is at least about 60%. Preferred average molecular weights will typically be from about 20,000 to about 150,000. The film may also be a blend composition comprising a hydrolytically degradable and water soluble polymer blend, such as polylactic acid and polyvinyl alcohol (known under trade reference number M8630, as sold by MonoSol llc of indiana, usa) plus a plasticizer, like glycerol, ethylene glycol, propylene glycol, sorbitol, and mixtures thereof. These pouches may contain solid laundry cleaning compositions or part components and/or liquid cleaning compositions or part components separated by a water-soluble film. The chambers available for the liquid component may differ in composition from the chambers containing the solids: US2009/0011970A 1.

The detergent ingredients may be physically separated from each other by a compartment in a water soluble pouch or in a different layer of the tablet. Thus, poor storage interactions between the components can be avoided. The different dissolution profiles of each chamber in the wash solution may also cause delayed dissolution of the selected component.

Non-unit dose liquid or gel detergents may be aqueous, typically containing at least 20% and up to 95% by weight water, for example up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water. Other types of liquids including, but not limited to, alkanols, amines, glycols, ethers, and polyols may be included in the aqueous liquid or gel. The aqueous liquid or gel detergent may contain from 0-30% of an organic solvent. The liquid or gel detergent may be non-aqueous.

Granular detergent formulations

Dust-free granules may be produced, for example, as disclosed in US 4,106,991 and 4,661,452, and may optionally be coated by methods known in the art. Examples of waxy coating materials are poly (ethylene oxide) products (polyethylene glycol, PEG) having an average molecular weight of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; an ethoxylated fatty alcohol in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; a fatty alcohol; a fatty acid; and mono-and diglycerides, and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluid bed techniques are given in GB 1483591. The liquid enzyme preparation may be stabilized, for example, by adding a polyol (such as propylene glycol), a sugar or sugar alcohol, lactic acid or boric acid according to established methods. The protected enzymes may be prepared according to the methods disclosed in EP 238,216.

The dnase and rnase may be formulated as particles, e.g., as co-particles that bind one or more enzymes. Each enzyme will then be present in a number of particles which ensure a more uniform distribution of the enzyme in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes. A method for producing multi-enzyme co-particles for the detergent industry is disclosed in ip.

Another example of formulation of enzymes by use of co-particles is disclosed in WO2013/188331, which relates to a detergent composition comprising: (a) co-granulating with multiple enzymes; (b) less than 10wt zeolite (on an anhydrous basis); and (c) less than 10wt phosphate (on an anhydrous basis), wherein the enzyme co-particles comprise from 10 wt% to 98 wt% of a water sink component, and the composition additionally comprises from 20 wt% to 80 wt% of a detergent water sink component. The multi-enzyme co-granule may comprise an enzyme of the invention and one or more enzymes selected from the group consisting of: proteases, lipases, cellulases, xyloglucanases, perhydrolases, peroxidases, lipoxygenases, laccases, hemicellulases, proteases, cellulases, cellobiose dehydrogenases, xylanases, phospholipases, esterases, cutinases, pectinases, mannanases, pectin lyases, keratinases, reductases, oxidases, phenoloxidases, ligninases, pullulanases, tannases, pentosanases, lichenases, glucanases, arabinosidases, hyaluronidase, chondroitinase, amylases, and mixtures thereof. WO2013/188331 also relates to a method of treating and/or cleaning a surface, preferably a fabric surface, comprising the steps of: (i) contacting said surface in an aqueous wash liquor with a detergent composition as claimed and described herein, (ii) rinsing and/or drying the surface.

Embodiments of the invention relate to enzyme granules (granules/granules) comprising dnase and rnase. The granules are composed of a core and optionally one or more coatings (outer layers) surrounding the core.

Typically, the particles have a particle size (grain/particle size), measured as the equivalent spherical diameter (volume based average particle size), of from 20 to 2000 μm, in particular from 50 to 1500 μm, from 100-. The core may include additional materials such as fillers, fibrous materials (cellulosic or synthetic fibers), stabilizers, solubilizers, suspending agents, viscosity modifiers, light spheres, plasticizers, salts, lubricants, and fragrances. The core may include a binder, such as a synthetic polymer, wax, fat, or carbohydrate. The core, typically as a homogeneous blend, may comprise a salt of a multivalent cation, a reducing agent, an antioxidant, a peroxide decomposition catalyst, and/or an acidic buffer component. The core may consist of inert particles into which the enzyme is adsorbed or applied (e.g. by fluidized bed coating) onto the surface of the inert particles. The core may have a diameter of 20-2000 μm, in particular 50-1500 μm, 100-1500 μm or 250-1200 μm. The core may be prepared by granulating a blend of ingredients, for example by methods including granulation techniques such as crystallization, precipitation, pan-coating (pan-coating), fluid bed coating, fluid bed agglomeration, rotary atomization, extrusion, granulation (granulating), spheronization, size reduction, drum granulation, and/or high shear granulation.

Methods for preparing cores can be found in the Handbook of Powder Technology; particle size enlargement by capes [ Particle size enlargement ]; volume 1; 1980; elsevier [ Eschevir ].

The core of the enzyme granules (granules) may be surrounded by at least one coating, for example, to improve storage stability, to reduce dust formation during handling or for colouring the granules. The one or more optional coatings may include a salt coating, or other suitable coating materials, such as polyethylene glycol (PEG), methylhydroxy-propyl cellulose (MHPC), and polyvinyl alcohol (PVA). Examples of enzyme granules with various coatings are shown in WO 93/07263 and WO 97/23606. The coating may be applied in an amount of at least 0.1%, e.g., at least 0.5%, 1%, or 5% by weight of the core. The amount may be at most 100%, 70%, 50%, 40% or 30%. The coating is preferably at least 0.1 μm thick, in particular at least 0.5 μm, at least 1 μm or at least 5 μm. In one embodiment, the thickness of the coating is less than 100 μm. In another embodiment, the thickness of the coating is below 60 μm. In even more particular embodiments, the total thickness of the coating is less than 40 μm. The coating should seal the core unit by forming a substantially continuous layer. A substantially continuous layer is understood to be a coating having few or no holes such that the sealed/enclosed core unit has few or no uncoated areas. The layer or coating should be uniform in thickness. The coating may further contain other materials as known in the art, for example, fillers, antiblocking agents, pigments, dyes, plasticizers and/or binders, such as titanium dioxide, kaolin, calcium carbonate or talc. The salt coating may comprise at least 60% salt by weight w/w, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% by weight w/w. The salt may be derived from a salt solutionEither added (wherein the salt is completely dissolved) or added from a salt suspension (wherein the fine particles are less than 50 μm, such as less than 10 μm or less than 5 μm). The salt coating may comprise a single salt or a mixture of two or more salts. The salt may be water soluble and have a solubility in 100g of water of at least 0.1 g, preferably at least 0.5g/100g, for example at least 1g/100g, for example at least 5g/100g at 20 ℃. The salt may be an inorganic salt, for example a sulphate, sulphite, phosphate, phosphonate, nitrate, chloride or carbonate salt or a salt of a simple organic acid (less than 10 carbon atoms, such as 6 or less carbon atoms) such as a citrate, malonate or acetate salt. Examples of cations in these salts are alkali or alkaline earth metal ions, ammonium ions or metal ions of the first transition series, such as sodium, potassium, magnesium, calcium, zinc or aluminum. Examples of anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, dihydrogenphosphate, dibasic phosphate, hypophosphite, dihydrogenpyrophosphate, tetraborate, borate, carbonate, bicarbonate, silicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, butyrate, propionate, benzoate, tartrate, ascorbate, or gluconate. In particular, alkali or alkaline earth metal salts of sulfates, sulfites, phosphates, phosphonates, nitrates, chlorides or carbonates or salts of simple organic acids such as citrates, malonates or acetates can be used. The salt in the coating may have a constant humidity of more than 60%, in particular more than 70%, more than 80% or more than 85% at 20 ℃, or it may be another hydrate form (e.g. anhydrate) of this salt. The salt coating may be as described in WO 00/01793 or WO 2006/034710. A specific example of a suitable salt is NaCl (CH)_20℃＝76％)、Na₂CO₃(CH_20℃＝92％)、NaNO₃(CH_20℃＝73％)、Na₂HPO₄(CH_20℃＝95％)、Na₃PO₄(CH_25℃＝92％)、NH₄Cl(CH_20℃＝79.5％)、(NH₄)₂HPO₄(CH_20℃＝93,0％)、NH₄H₂PO₄(CH_20℃＝93.1％)、(NH₄)₂SO₄(CH_20℃＝81.1％)、KCl(CH_20℃＝85％)、K₂HPO₄(CH_20℃＝92％)、KH₂PO₄(CH_20℃＝96.5％)、KNO₃(CH_20℃＝93.5％)、Na₂SO₄(CH_20℃＝93％)、K₂SO₄(CH_20℃＝98％)、KHSO₄(CH_20℃＝86％)、MgSO₄(CH_20℃＝90％)、ZnSO₄(CH_20℃90%) and sodium Citrate (CH)_25℃86%). Other examples include NaH₂PO₄、(NH₄)H₂PO₄、CuSO₄、Mg(NO₃)₂And magnesium acetate. The salt may be in anhydrous form or it may be a hydrated salt, i.e. a crystalline salt hydrate with one or more bound waters of crystallization, as described in WO 99/32595. Specific examples include anhydrous sodium sulfate (Na)₂SO₄) Anhydrous magnesium sulfate (MgSO)₄) Magnesium sulfate heptahydrate (MgSO)₄.7H₂O), zinc sulfate heptahydrate (ZnSO)₄.7H₂O), disodium hydrogen phosphate heptahydrate (Na)₂HPO₄.7H₂O), magnesium nitrate hexahydrate (Mg (NO)₃)₂(6H₂O)), sodium citrate dihydrate, and magnesium acetate tetrahydrate. Preferably, the salt is used as a salt solution, for example using a fluidized bed.

One embodiment of the present invention provides a particle comprising:

(a) a core comprising DNase and RNAse, and

(b) optionally a coating consisting of one or more layers surrounding the core.

One embodiment of the present invention is directed to a particle comprising:

(a) a core comprising a dnase and an rnase, wherein the rnase is selected from the group consisting of: an rnase comprising an amino acid sequence having:

xix) at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 104,

and wherein the DNase has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 13, and