阅读说明：本技术 具有去污效果的衣物洗涤剂组合物 (Laundry detergent composition with soil release effect ) 是由 G·O·比安切蒂 内尔·约瑟夫·兰特 史蒂文·乔治·帕特森 于 2020-03-25 设计创作，主要内容包括：使用去污表面活性剂和包含黄原胶内切葡聚糖酶、黄原胶裂解酶和甘露聚糖酶的酶混合物的组合,满足了对改善污渍去除的衣物洗涤剂组合物的需要,该污渍包含甘露聚糖和其它多糖的组合。(The need for laundry detergent compositions with improved stain removal comprising a combination of mannans and other polysaccharides is met using a combination of a detersive surfactant and an enzyme mixture comprising xanthan endoglucanase, xanthan lyase and mannanase.)

1. A laundry detergent composition comprising:

a) a detersive surfactant, wherein the detersive surfactant comprises a combination of anionic surfactant and nonionic surfactant;

b) an enzyme system comprising:

i. a xanthan endoglucanase, wherein the xanthan endoglucanase comprises a polypeptide having at least 60% sequence identity to SEQ ID No. 1;

a xanthan lyase, wherein the xanthan lyase comprises a polypeptide having at least 60% sequence identity to SEQ ID NO:2, and

a mannanase, wherein the mannanase is selected from the group consisting of:

a) a mannanase enzyme having mannanase activity and a polypeptide having at least 85% sequence identity to residues 27-331 of SEQ ID No. 3, SEQ ID No. 3 corresponding to the full-length amino acid sequence of Man7 mannanase endogenous to bacillus hemicellulolyticus comprising a signal sequence;

b) a mannanase having mannanase activity and a polypeptide having at least 60% identity to SEQ ID No. 4, which mannanase, in one embodiment of the invention, has mannanase activity and a polypeptide having at least 80% identity to SEQ ID No. 4, SEQ ID No. 4 corresponding to the full-length amino acid sequence of Man4 mannanase endogenous to paenibacillus;

c) and mixtures thereof.

2. A laundry detergent composition according to claim 1, wherein the detersive surfactant is selected from the group consisting of: nonionic surfactants, anionic surfactants, amphoteric surfactants, and mixtures thereof.

3. A laundry detergent composition according to claim 2, wherein the detersive surfactant comprises an anionic surfactant, wherein the anionic surfactant comprises linear alkylbenzene sulphonate and alkyl alkoxylated sulphate, and the ratio of linear alkylbenzene sulphonate surfactant to alkyl alkoxylated sulphate surfactant is from 0.1 to 5, preferably from 0.25 to 3, more preferably from 0.6 to 1.1.

4. A laundry detergent composition according to any preceding claim, wherein the laundry detergent composition comprises a detersive surfactant at a level of from 1 wt% to 70 wt%, preferably from 10 wt% to 50 wt%, more preferably from 15 wt% to 35 wt%.

5. The laundry detergent composition according to any preceding claims, wherein the xanthan gum endoglucanase is a variant having at least 61%, at least 62%, at least 63%, at least 64%, at least 65%, at least 66%, at least 67%, at least 68%, at least 69%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, 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% or at least 99% sequence identity to SEQ ID No. 1.

6. A laundry detergent composition according to any preceding claim, wherein the xanthan gum endoglucanase has a substitution at one or more of the following positions of SEQ ID NO: 1: 17. 20, 51, 53, 55, 56, 60, 63, 79, 87, 186, 192, 302, 311, 313, 387, 388, 390, 403, 408, 410, 416, 448, 451, 471, 472, 476, 489, 507, 512, 515, 538, 598, 599, 602, 605, 609, 676, 688, 690, 694, 697, 698, 699, 711, 719, 754, 756, 760, 781, 786, 797, 833, 834, 835 and 1048.

7. A laundry detergent composition according to any preceding claims, wherein the xanthan gum endoglucanase has a substitution at one or more of the following positions: s17, F20, K51, E53, Y55, V56, Y60, S63, T87, a186, K192, I320, I302, H311, S313, I387, K388, K390, I403, E408, P410, Q416, a448, K451, G471, S472, D476, Q489, K507, K512, S515, S538, Y579, S598, a599, I602, V603, S605, G609, D676, a688, Y690, T694, T697, R698, T699, T711, W, K754, V756, V78760, S786, T719, N1048, T781, S824, N781, S7818, and F781.

8. The laundry detergent composition according to any preceding claims, wherein the xanthan lyase is a variant having at least 61%, at least 62%, at least 63%, at least 64%, at least 65%, at least 66%, at least 67%, at least 68%, at least 69%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, 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% or at least 99% sequence identity to SEQ ID No. 2.

9. A laundry detergent composition according to any preceding claim, wherein the xanthan lyase is a variant having an alteration at one or more positions selected from the group consisting of the following positions of SEQ ID NO: 2: 9. 15, 46, 58, 66, 89, 95, 100, 106, 109, 183, 188, 190, 203, 204, 221, 229, 234, 238, 240, 242, 243, 257, 258, 291, 293, 316, 320, 324, 329, 333, 339, 341, 352, 354, 360, 377, 399, 400, 419, 440, 450, 451, 454, 458, 481, 492, 567, 568, 578, 579, 582, 664, 672, 703, 728, 843, 855, 887, 892, 1008, and 1016.

10. A laundry detergent composition according to any preceding claim, wherein the xanthan lyase is a variant having an alteration at one or more positions selected from the group consisting of the following positions of SEQ ID NO: 2: 624. 631, 635, 649, 656, 752, 754, 757, 769, 775, 777, 800, 801, 875, 911, and 915.

11. A laundry detergent composition according to any preceding claim, wherein the mannanase has at least 90% sequence identity to residues 27-331 of SEQ ID NO 3.

12. A laundry detergent composition according to any preceding claims, wherein the mannanase is a variant of SEQ ID No. 3 comprising at least one substitution at position 123, 158, 180, 272, 285 or 307 or a combination thereof.

13. A laundry detergent composition according to any preceding claims, wherein the mannanase is a variant of SEQ ID No. 3 comprising at least one substitution at position M123, a158, F180, G272, T285 or T307 or a combination thereof.

14. A laundry detergent composition according to any preceding claim, wherein the mannanase comprises a polypeptide having at least 85% sequence identity to residues 27-331 of SEQ ID No. 3 and/or at least 60% sequence identity to SEQ ID No. 4.

15. A laundry detergent composition according to claim 14, wherein the mannanase is a variant of SEQ ID No. 3 comprising at least one substitution at position M123, a158, F180, G272, T307 or L316 or a combination thereof.

16. A laundry detergent composition according to claim 14, wherein the mannanase has at least 80% sequence identity to SEQ ID No. 4.

17. The laundry detergent composition of claim 16, wherein the mannanase comprises at least one, two, three, four, five, six, seven or more variants relative to SEQ ID No. 4 selected from the group consisting of:

(a) N10Q/T, P19E/V, S30T, T38E/I/L/M/Q/R/V, S59D/G/K/N/Q/T, L60F/M/V, T62E/I/Q/E, L66E/T/E67/D/E/P/Q/S/E/M/R/S/E/C/Q/E, Q78/D/L/E79E/F/E80/E97E/L/P/E, Y129E, T E, S135/C/E, K143E/S/W167/Y36167/Y E/Y129/E, Y E, T E, S E/C/E, P168A/E/G/L/M/S/T, Q184/F/H/L/M/P, N213E, K214C/Q, G225A/C/P/W, T A/G/H/I/K/S/V/Y, Y235/G/I/L/Q/S/V, Q S/E, K244A/C/G/L/M/P/S, S258A/D/E/G/M/N/P/T, G259A/E/R/S/W, N63261/M/P/Q/R/S/T/V/W/Y and D283G/H/T; or

(b) P19E/V, T E/I/L/M/Q/R/V, N67/D/E/G/P/Q/S/V, N97E/L/P/Q, Y M, K143Q/R, P168A/E/L/S/T, Q184D/F/H/L/M/P, G A/C/P/W, T228A/G/H/I/K/S/V/Y, Y G/I/L/Q/S/V, K A/C/G/L/M/P/S, S258A/D/E/G/M/N/P/T and N261I/M/P/Q/R/S/T/V- W/Y; or

(c) P19E/V, T38E/I/L/M/Q/R/V, N67A/D/E/P/Q/S/V, L85L, Y129M, P168A/E/G/L/M/S/T, Q184D/F/H/L/M/P, G225A/C/P/W, K244A/C/G/L/M/P/S, S258A/D/E/G/M/N/P/T and N261I/M/P/Q/R/S/T/V/W/Y; or

(d) P19E, S30T, T38E, S59V, L60Q, K63R, N67D, N97D, V103I, Y129M, F167Y, P168S, Q184L, G225C, T228V, Y235L, K244L, S258D and N261R.

18. A laundry detergent composition according to claim 16, wherein the mannanase is a variant of SEQ ID No. 4 comprising a plurality of variants of SEQ ID No. 4 selected from: P19E-T38E-N67D-N97D-Y129M-P168S-Q184L-K244L-S258D-N261R; N10T-P19E-G28S-S30T-T38E-N67D-N71D-N97D-Y129M-P168S-Q184L-G225C-Y235L-K244L-S258D-N261R-F297 FQ; P19E-S30T-T38E-S59V-L60Q-K63R-N67D-N97D-V103I-Y129M-F167Y-Q184L-G225C-T228V-Y235L-K244L-S258D-N261R-F297 FQ; N10T-P19E-S30T-T38E-S59V-L60Q-K63R-N67D-N97D-Y129M-K143Q-P168S-Q184L-G225C-T228V-Y235L-K244L-S258D-N261R-F297 FQ; N10T-P19E-S30T-T38E-S59V-L60Q-K63R-N67D-N97D-Y129M-K143Q-P168S-Q184L-G225P-T228V-Y235L-K244L-S258D-N261R-F297 FQ; N10T-P19E-S30T-T38E-S59V-L60Q-K63R-N67D-N71D-N97D-V103I-Y129M-K143Q-P168S-Q184L-G225P-T228V-Y235L-K244L-S258D-N261R-F297 FQ; A2S-P19E-G28S-S30T-T38E-K63R-N67D-N71D-N74E-K93R-N97D-Y129M-N150T-P168S-Q184L-N213A-G225C-Y235L-K244L-S258D-N261Q-F297 FQ; T3R-N10T-P19E-G28A-S30T-T38E-T62E-N67D-N71D-K93R-N97L-E111S-Y129M-D139M-P168S-Q184L-G225C-Y235L-K244L-S258D-N261Q-F297 FQ; and N10T-P19E-G28A-S30T-T38E-S59D-N67D-A68S-N71D-K93R-N97D-Y129M-K143Q-P168S-Q184D-G225C-Y235L-K244L-S258D-N261R-T284E-F297 FQ.

19. A laundry detergent composition according to any preceding claim, wherein the enzyme system of the composition further comprises a lipase, preferably a lipase variant of SEQ ID No. 5, comprising:

(a) the substitution T231R;

(b) substitution N233R or N233C; and

(c) at least three additional substitutions selected from the group consisting of E1C, D27R, N33Q, G38A, F51V, G91Q, D96E, K98L, K98I, D111A, G163K, H198S, E210Q, Y220F, D254S, I255A, and P256T;

wherein position corresponds to position of SEQ ID NO. 5 and wherein the lipase variant has at least 90% but less than 100% sequence identity to a polypeptide having the amino acid sequence of SEQ ID NO. 5 and wherein the variant has lipase activity.

20. A laundry detergent composition according to any preceding claim, wherein the composition further comprises a cleaning polymer, preferably wherein the cleaning polymer is obtainable by free radical copolymerisation of: at least one compound of formula (I),

wherein n is a number equal to or greater than 3,

with at least one compound of the formula (II),

wherein A is^-Represents an anion, in particular selected from halides such as fluoride, chloride, bromide, iodide, sulfate, hydrogen sulfate, alkyl sulfates such as methyl sulfate, and mixtures thereof.

21. A unit dose article comprising a laundry detergent composition according to any preceding claims, wherein the composition comprises less than 20 wt% water and the detergent composition is encapsulated in a water-soluble or water-dispersible film.

22. A method of laundering fabrics, preferably fabrics comprising a stain, wherein the stain comprises a combination of mannan and other polysaccharides, wherein the method comprises the steps of:

a) providing a laundry detergent composition according to any preceding claim;

b) diluting the laundry detergent composition to provide a wash liquor having a total surfactant concentration of greater than 300 ppm; and

c) washing the fabric in the washing liquid.

Technical Field

Laundry detergent compositions, especially liquid laundry detergent compositions for cleaning mixed food stains, are disclosed.

Background

Laundry detergent compositions are formulated to provide good cleaning to fabrics: the white fabric is kept white and the colored fabric is kept bright. Laundry detergent compositions are also typically formulated to remove stains. Stains are localized discolorations that can be clearly distinguished on the fabric on which they are present. They are particularly noticeable on fabrics because they cause discoloration that contrasts strongly with uncontaminated fabrics.

Certain mixed food stains, such as prepared sauces, remain challenging to remove, especially at low temperatures. Furthermore, despite the use of anti-redeposition aids, such stains have been found to redeposit on fabrics during laundering. Although improved removal of such stains can be achieved by increasing the level of active materials such as anti-redeposition aids, surfactants and builders, this increases the cost of the formulation and can lead to other problems such as stability.

Thus, there remains a need for a laundry detergent composition having improved efficacy against mixed food stains such as prepared sauces, while being stable and not requiring high levels of stain treatment active.

WO2019/038059 relates to detergent compositions comprising endoglucanase variants and methods of use of the compositions. WO2019/038060 relates to detergent compositions comprising xanthan lyase variants and methods of use of the compositions.

Disclosure of Invention

The present invention relates to a laundry detergent composition comprising: a detersive surfactant, wherein the detersive surfactant comprises a combination of anionic surfactant and nonionic surfactant; an enzyme system comprising: a xanthan endoglucanase, wherein the xanthan endoglucanase comprises a polypeptide having at least 60% sequence identity to SEQ ID No. 1; a xanthan lyase, wherein the xanthan lyase comprises a polypeptide having at least 60% sequence identity to SEQ ID No. 2; and a mannanase enzyme, wherein the mannanase enzyme comprises a polypeptide having at least 85% sequence identity to residues 27-331 of SEQ ID NO. 3 and/or at least 80% sequence identity to SEQ ID NO. 4.

The present invention also relates to a method of laundering a fabric, preferably a fabric comprising a stain, wherein the stain comprises a combination of mannan and polysaccharide, wherein the method comprises the steps of: providing a laundry detergent composition of the present invention; diluting the laundry detergent composition to provide a wash liquor having a total surfactant concentration of greater than 300 ppm; and washing the fabric in a wash liquor.

Detailed Description

It has been surprisingly found that the resilience of certain mixed food stains, such as certain prepared sauces, is attributed to the combination of mannan and other polysaccharides. Such sauces may include chili paste, vinegar paste and some ice cream. Examples of such mannans include locust bean gum, tara gum, guar gum, and the like, and mixtures thereof. Examples of polysaccharides include xanthan gum. It is believed that the combination of mannan and polysaccharide forms a gel when the soil dries, resulting in difficulty in stain removal. Furthermore, the resilience of such gels can be increased in the presence of fats or oily residues, such as animal fats (e.g. bacon fat, lard, shortening, butter) and vegetable oils (e.g. sunflower oil, rapeseed oil, cottonseed oil, olive oil, corn oil). Furthermore, even if the soil is removed, the gel-like structure causes the soil to remain together as a suspension during the wash cycle, resulting in greater redeposition. It is believed that the enzyme systems used in the present invention break down these gel structures more effectively than mannanases alone or endoglucanases alone, even when the gel structures contain oil or oily residues, resulting in improved removal of such stains. Furthermore, a reduced redeposition of soil is also achieved, since the enzyme system is able to break down such gel structures better.

Unless otherwise specified, all components or compositions are on average with respect to the active portion of that component or composition, and do not include impurities, such as residual solvents or by-products, that may be present in commercially available sources of such components or compositions.

All percentages and ratios are by weight unless otherwise indicated. All percentages and ratios are calculated based on the total composition, unless otherwise indicated.

All measurements were made at 25 ℃ unless otherwise indicated.

As used herein, articles including "a" and "an" when used in a claim should be understood to mean one or more of what is claimed or described.

Laundry detergent composition

The laundry detergent composition may be in any suitable form, such as a liquid, paste, granule, solid, powder, or in combination with a carrier such as a substrate. Preferred laundry detergent compositions are liquid or granular, with liquid being most preferred.

As used herein, "liquid detergent composition" refers to a liquid detergent composition that is fluid and preferably capable of wetting and cleaning fabrics, such as clothing in a domestic washing machine. As used herein, "laundry detergent composition" refers to compositions suitable for washing clothes. The composition may comprise a solid or a gas in a suitably subdivided form, but the overall composition does not include a generally non-fluid product form, such as a tablet or granule. The liquid laundry detergent composition preferably has a density in the range of from 0.9 to 1.3 grams per cubic centimeter, more specifically from 1.00 to 1.10 grams per cubic centimeter, excluding any solid additives, but including any air bubbles, if present.

Aqueous liquid laundry detergent compositions are preferred. For such aqueous liquid laundry detergent compositions, the water content may be present at a level of from 5% to 99%, preferably from 15% to 90%, more preferably from 25% to 80% by weight of the liquid detergent composition.

The pH of the detergent composition ranges from 6.0 to 8.9, preferably from 7 to 8.8.

The detergent composition may also be encapsulated in a water-soluble film to form a unit dose article. Such unit dose articles comprise a detergent composition of the present invention, wherein the detergent composition comprises less than 20 wt%, preferably less than 15 wt%, more preferably less than 10 wt% water, and the detergent composition is encapsulated in a water-soluble or water-dispersible film. Such unit dose articles may be formed using any method known in the art.

Suitable water-soluble pouch materials include polymers, copolymers or derivatives thereof. Preferred polymers, copolymers or derivatives thereof may be selected from the group consisting of: polyvinyl alcohols, polyvinyl pyrrolidones, polyalkylene oxides, acrylamides, acrylic acids, cellulose ethers, cellulose esters, cellulose amides, polyvinyl acetates, polycarboxylic acids and salts, polyaminoacids or peptides, polyamides, polyacrylamides, maleic/acrylic acid copolymers, polysaccharides (including starch and gelatin), natural gums (such as xanthan and carrageenan). More preferred polymers are selected from the group consisting of polyacrylates and water-soluble acrylate copolymers, methylcellulose, sodium carboxymethylcellulose, dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylates, and most preferably selected from the group consisting of polyvinyl alcohol, polyvinyl alcohol copolymers and Hydroxypropylmethylcellulose (HPMC), and combinations thereof.

Detersive surfactant

As used herein, detersive surfactant refers to a surfactant or mixture of surfactants that provide a cleaning, detersive, or laundry benefit to soiled material. Suitable detersive surfactants can be: anionic surfactants, nonionic surfactants, zwitterionic surfactants, and combinations thereof. Detersive surfactants include a combination of anionic and nonionic surfactants.

The laundry detergent composition may comprise a detersive surfactant at a level of from 3 wt% to 50 wt%, preferably from 10 wt% to 37.5 wt%, more preferably from 15 wt% to 30 wt%.

Suitable anionic surfactants may be selected from the group consisting of: alkyl sulfates, alkyl ethoxy sulfates, alkyl sulfonates, alkylbenzene sulfonates, fatty acids and salts thereof, and mixtures thereof. However, by its very nature, every anionic Surfactant known in the art of detergent compositions can be used, as disclosed in "Surfactant Science Series", 7 th edition, edited by w.m. linfield (Marcel Dekker). However, the composition preferably comprises at least a sulphonic acid surfactant, such as linear alkyl benzene sulphonic acid, although water soluble salt forms may also be used. Alkyl ethoxy sulfates or mixtures thereof are also preferred.

Anionic sulfonates or sulfonic acid surfactants suitable for use herein include straight or branched chain alkylbenzene sulfonates, alkyl ester sulfonates, paraffin sulfonates, alkyl sulfonated polycarboxylic acids, and mixtures thereof, in both acid and salt form. Suitable anionic sulfonate or sulfonic acid surfactants include: C5-C20 alkylbenzene sulfonate, more preferably C10-C16 alkylbenzene sulfonate, more preferably C11-C13 alkylbenzene sulfonate, C5-C20 alkyl ester sulfonate, C6-C22 primary or secondary paraffin sulfonate, C5-C20 sulfonated polycarboxylic acid, and any mixture thereof, but preferably C11-C13 alkylbenzene sulfonate. The above surfactants can vary widely within their 2-phenyl isomer content. Such sulfonate or sulfonic acid surfactants may be present at a level of from 1.0% to 20%, more preferably from 5.0% to 15%, and most preferably from 6.5% to 12.5% by weight of the composition.

Anionic sulfates suitable for use in the compositions of the present invention include primary and secondary alkyl sulfates having a linear or branched alkyl or alkenyl moiety containing from 9 to 22 carbon atoms or more preferably from 12 to 18 carbon atoms. Also useful are beta-branched alkyl sulfate surfactants or mixtures of commercially available materials having a weight average degree of branching (of the surfactant or mixture) of at least 50%.

Other suitable anionic surfactants for use herein include fatty acid methyl ester sulfonates and/or alkyl alkoxylated sulfates such as Alkyl Ethoxy Sulfates (AES) and/or alkyl polyalkoxylated carboxylates (AEC). When used, the alkyl alkoxylated sulfate surfactant is preferably a blend of one or more alkyl ethoxylated sulfates. Suitable alkyl alkoxylated sulfates include C10-C18 alkyl ethoxylates, more preferably C12-C15 alkyl ethoxylates having a degree of ethoxylation of from 1 to 5, preferably from 2 to 3. Such alkyl alkoxylated sulfates are preferably present at a level of from 1.0% to 10%, more preferably from 2.0% to 7.5%, and most preferably from 3.0% to 5%, by weight of the composition.

Suitable fatty acids include "natural" fatty acids, such as coconut, palm kernel, olive oil or tallow fatty acids, and mixtures thereof. Such fatty acid surfactants may be present at a level of from 1.0% to 15%, more preferably from 2.0% to 12.5%, and most preferably from 5.0% to 10% by weight of the composition.

Anionic surfactants are generally present in the form of their salts with alkanolamines or alkali metals such as sodium and potassium.

The liquid detergent composition may comprise a nonionic surfactant. The nonionic surfactant may be present in the liquid detergent composition at a level of from 1.0% to 20%, preferably from 2.5% to 15%, more preferably from 5.0% to 12.5% by weight of the composition.

Suitable nonionic surfactants include, but are not limited to, C12-C18 alkyl ethoxylates ("AEs") (including so-called narrow peak alkyl ethoxylates) and C6-C12 alkyl phenol alkoxylates (especially ethoxylates and mixed ethoxy/propoxy), block alkylene oxide condensates of C6-C12 alkyl phenols, alkylene oxide condensates of C8-C22 alkanols, and ethylene oxide/propylene oxide block polymers (Pluronic-BASF Corp.) as well as semi-polar nonionics (e.g., amine oxides and phosphine oxides) may be used in the compositions of the present invention. A broad disclosure of these types of surfactants can be found in U.S. Pat. No. 3,929,678 to Laughlin et al, published 1975, 12, 30.

Alkyl polysaccharides, such as those disclosed in U.S. Pat. No. 4,565,647 to Llenado, are also nonionic surfactants that may be used in the compositions of the present invention.

Also suitable are alkyl polyglucoside surfactants.

The nonionic surfactant used comprises the formula R₁(OC₂H₄)_nThose of OH, wherein R₁Is C10-C1A6 alkyl group or a C8-C12 alkylphenyl group, and n is preferably from 3 to 80. In some embodiments, the nonionic surfactant can be a condensation product of a C12-C15 alcohol with 5 to 20 moles of ethylene oxide per mole of alcohol, for example a C12-C13 alcohol condensed with 6.5 moles of ethylene oxide per mole of alcohol.

Suitable amine oxide surfactants are amine oxides having the formula: r₁R₂R₃NO, wherein R₁Is a hydrocarbon chain comprising from 1 to 30, preferably from 6 to 20, more preferably from 8 to 16 carbon atoms, and wherein R is₂And R₃Independently a saturated or unsaturated, substituted or unsubstituted, linear or branched hydrocarbon chain containing from 1 to 4 carbon atoms, preferably from 1 to 3 carbon atoms, and more preferably a methyl group. R₁And may be a saturated or unsaturated, substituted or unsubstituted, straight or branched hydrocarbon chain.

Amine oxides suitable for use herein are preferably those available, for example, from Albright&C commercially available from Wilson₁₂-C₁₄Dimethylamine oxide, tradenameLA from Clariant or under the trade nameC commercially available from AKZO Nobel as DMC₁₂-C₁₄Amine oxide.

Other suitable nonionic surfactants include polyhydroxy fatty acid amides represented by the formula:

wherein R is a C9-17 alkyl or alkenyl group, R1 is a methyl group, and Z is a glycidyl group derived from a reducing sugar or alkoxylated derivative thereof. Examples are N-methyl N-1-deoxyglucuroncocoamide and N-methyl N-1-deoxyglucuronoleamide. Methods for preparing polyhydroxy fatty acid amides are known and can be found in Wilson, U.S. Pat. No. 2,965,576 and Schwartz, U.S. Pat. No. 2,703,798.

The liquid detergent composition may comprise a zwitterion. The zwitterion may be present in an amount of from 0.1 to 5 wt.%, preferably from 0.2 to 2 wt.%, more preferably from 0.4 to 1 wt.%.

Suitable amphoteric or zwitterionic detersive surfactants include those known for use in hair care or other personal care cleansing. Non-limiting examples of suitable zwitterionic or amphoteric surfactants are described in U.S. Pat. Nos. 5,104,646(Bolich Jr. et al), 5,106,609(Bolich Jr. et al). Suitable amphoteric detersive surfactants include those surfactants broadly described as derivatives of aliphatic secondary and tertiary amines in which the aliphatic radical can be straight or branched chain and wherein one of the aliphatic substituents contains from 8 to 18 carbon atoms and one contains an anionic group, such as carboxy, sulfonate, sulfate, phosphate, or phosphonate. Amphoteric detersive surfactants suitable for use in the present invention include, but are not limited to: cocoamphoacetate, cocoamphodiacetate, lauroamphoacetate, lauroamphodiacetate, and mixtures thereof.

Surfactants comprising saturated alkyl chains are preferably used.

Enzyme system

The laundry detergent composition of the present invention comprises an enzyme cocktail, wherein the enzyme cocktail comprises xanthan gum endoglucanase, xanthan gum lyase and mannanase.

Definition of enzyme

Parent strain: the term "parent" refers to the enzyme from which the alteration is made to produce an enzyme variant. The parent may be a naturally occurring (wild-type) polypeptide or a variant thereof.

Sequence identity: the relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter "sequence identity". For The purposes of The present invention, The degree of sequence identity between two amino acid sequences is determined using The Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J.Mol.biol.48: 443) -453), as implemented in The Needle program of The EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al 2000, Trends Genet.16:276-277), preferably version 3.0.0 or more. Optional parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and an EBLOSUM62(EMBOSS version of BLOSUM62) substitution matrix. The Needle output labeled "longest identity" (obtained using the-nobrief option) is used as the percent identity and is calculated as follows:

(same residue X100)/(sequence Length-Total number of empty bits in sequence)

Alternatively, the parameters used may be a gap opening penalty of 10, a gap extension penalty of 0.5, and an EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. The Needle output labeled "longest identity" (obtained using the-nobrief option) is used as the percent identity and is calculated as follows:

(same deoxyribonucleotide X100)/(sequence length-number of total empty bits in sequence)

Variants: the term "variant" refers to a polypeptide having enzymatic activity that comprises an alteration/mutation (i.e., substitution, insertion, and/or deletion) at one or more (e.g., several) positions relative to a parent enzyme. Substitution refers to the replacement of an amino acid occupying a position with another, different amino acid; deletion refers to the removal of an amino acid that occupies a position; and insertion refers to the addition of 1-3 amino acids adjacent to and immediately after the amino acid occupying a position. Changes/mutations are generally described using the one-letter amino acid codes and symbols familiar to those skilled in the art. For example, S23D defines the substitution of the serine (S) residue with aspartic acid (D) at position 23; y30 defines the deletion of the tyrosine residue at position 30. G34GW defines the insertion of a tryptophan residue after the glycine at position 34.

Wild-type enzyme: the term "wild-type" refers to an enzyme encoded by the DNA of a naturally occurring organism, such as a bacterium, yeast or filamentous fungus found in nature.

Xanthan gum endoglucanase

As used herein, the term xanthan endoglucanase refers to an enzyme exhibiting endo- β -1, 4-glucanase activity capable of catalyzing hydrolysis of the 1, 4-linked β -D-glucose polymer backbone of xanthan gum in combination with a suitable xanthan lyase. The xanthan endoglucanase according to the invention has endo-beta-1, 4-glucanase activity and a polypeptide having at least 60% identity with SEQ ID No. 1. SEQ ID NO 1 corresponds to the amino acid sequence of a xanthan endoglucanase endogenous to Paenibacillus sp 62047.

In further embodiments of the invention, the xanthan endoglucanase is a variant having at least 61%, at least 62%, at least 63%, at least 64%, at least 65%, at least 66%, at least 67%, at least 68%, at least 69%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, 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% or at least 99% sequence identity to SEQ ID No. 1.

In a further embodiment of the invention, the xanthan endoglucanase has a substitution at one or more of the following positions of SEQ ID NO: 1: 17. 20, 51, 53, 55, 56, 60, 63, 79, 87, 186, 192, 302, 311, 313, 387, 388, 390, 403, 408, 410, 416, 448, 451, 471, 472, 476, 489, 507, 512, 515, 538, 598, 599, 602, 605, 609, 676, 688, 690, 694, 697, 698, 699, 711, 719, 754, 756, 760, 781, 786, 797, 833, 834, 835 and 1048.

In further embodiments of the invention, the xanthan endoglucanase has a substitution at one or more of the following positions: s17, F20, K51, E53, Y55, V56, Y60, S63, T87, a186, K192, I320, I302, H311, S313, I387, K388, K390, I403, E408, P410, Q416, a448, K451, G471, S472, D476, Q489, K507, K512, S515, S538, Y579, S598, a599, I602, V603, S605, G609, D676, a688, Y690, T694, T697, R698, T699, T711, W, K754, V756, V78760, S786, T719, N1048, T781, S824, N781, S7818, and F781.

Examples of suitable xanthan endoglucanases according to the invention are listed below, wherein the substitutions correspond to the following positions in SEQ ID No. 1:

xanthan gum lyase

As used herein, the term "xanthan lyase" refers to an enzyme that cleaves the β -D-mannosyl- β -D-1, 4-glucuronic acid bond of xanthan gum and has been described in the literature. Xanthan lyases are classified as EC 4.2.2.12 according to enzyme nomenclature and are known to be produced by many xanthan-degrading bacteria (including bacillus, corynebacterium and paenibacillus). The xanthan lyase according to the invention has xanthan lyase activity and comprises a sequence identical to SEQ ID NO:2 with at least 60% identity. SEQ ID NO:2 corresponds to the amino acid sequence of a xanthan lyase endogenous to paenibacillus.

In a further embodiment of the invention, the xanthan lyase is a xanthan lyase identical to SEQ ID NO:2, at least 61%, at least 62%, at least 63%, at least 64%, at least 65%, at least 66%, at least 67%, at least 68%, at least 69%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, 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%, or at least 99% sequence identity.

In another embodiment of the invention, the xanthan lyase is a variant having an alteration at one or more positions selected from the group consisting of the following positions of SEQ ID No. 2: 9. 15, 46, 58, 66, 89, 95, 100, 106, 109, 183, 188, 190, 203, 204, 221, 229, 234, 238, 240, 242, 243, 257, 258, 291, 293, 316, 320, 324, 329, 333, 339, 341, 352, 354, 360, 377, 399, 400, 419, 440, 450, 451, 454, 458, 481, 492, 567, 568, 578, 579, 582, 664, 672, 703, 728, 843, 855, 887, 892, 1008, and 1016.

In another embodiment of the invention, the xanthan lyase is a variant having an alteration at one or more positions selected from the group consisting of the following positions of SEQ ID No. 2: 624. 631, 635, 649, 656, 752, 754, 757, 769, 775, 777, 800, 801, 875, 911, and 915.

In another embodiment of the invention, the xanthan lyase is a variant having one or more substitutions selected from the group consisting of the following substitutions of SEQ ID No. 2: K9R, N15T, L46T, a 58T, S66T, Q89T, K95T, S100T, N106T, Q109T, K36183, K183T, V188T, a 190T, a 203T, K204T, a 221T 229T, E229T, I234T, I238T, I240T, N242T, G243T, Y257 36915, R258T, K291 36293T, a 293T, K316T, K320T, L36324, K329T, K329 36333, L36339, L3613472, S T, S36354, S T, N3678, N T, N3678, N T, N3678, N T, N3678, N T, N3678, N T, N3678, N T, N3678, N T, N3659T, N3678, N T, N3659, N3678, N T, N3659, N T, N3678, N T, N3678, N T, N3659, N T, N36.

In another embodiment of the invention, the xanthan lyase is a variant based on SEQ ID NO 2 having one of the following substitution sets.

Mannanase

As used herein, the term "mannanase" or "galactomannanase" refers to mannanases of the following: it is defined as an endo-1, 4-beta-mannosidase according to what is known in the art and has the alias beta-mannanase and endo-1, 4-mannanase and catalyzes the hydrolysis of the 1, 4-beta-D-mannosidic linkages in mannans, galactomannans, glucomannans and galactoglucomannans. Mannanases were classified as EC 3.2.1.78 according to enzyme nomenclature.

Suitable mannanases may be selected from the group consisting of:

a) a mannanase enzyme having mannanase activity and a polypeptide having at least 85% sequence identity to residues 27-331 of SEQ ID NO 3. 3 corresponds to the full-length amino acid sequence of the Man7 mannanase endogenous to Bacillus hemicellulolyticus (Bacillus hemicellulosiilyticus) comprising a signal sequence;

b) a mannanase having mannanase activity and a polypeptide having at least 60% identity to SEQ ID No. 4. In one embodiment of the invention, the mannanase has mannanase activity and a polypeptide having at least 80% identity to SEQ ID NO. 4.4 corresponds to the full-length amino acid sequence of the endogenous Man4 mannanase of Paenibacillus;

c) and mixtures thereof.

Thus, a suitable mannanase may have mannanase activity and a polypeptide having at least 85% sequence identity to residues 27-331 of SEQ ID NO. 3. SEQ ID NO:3 corresponds to the full-length amino acid sequence of the Man7 mannanase endogenous to bacillus hemicellulolyticus comprising a signal sequence. In one embodiment of the invention, the mannanase has at least 90% sequence identity to residues 27-331 of SEQ ID NO 3. In another embodiment of the invention, the mannanase is a variant of SEQ ID NO. 3 comprising at least one substitution at position 123, 158, 180, 272, 285 or 307 or a combination thereof. In another embodiment of the invention, the mannanase is a variant of SEQ ID NO. 3 comprising at least one substitution at position M123, A158, F180, G272, T285 or T307 or a combination thereof. In another embodiment of the invention, the mannanase is a variant of SEQ ID NO. 3 comprising at least one substitution at position M123, A158, F180, G272, T307 or L316 or a combination thereof. In one embodiment, the variant comprises one additional substitution, two additional substitutions, three additional substitutions, or four additional substitutions.

Alternatively or additionally, a suitable mannanase may have mannanase activity and a polypeptide having at least 60% identity to SEQ ID No. 4. In one embodiment of the invention, the mannanase has mannanase activity and a polypeptide having at least 80% identity to SEQ ID NO. 4. SEQ ID NO 4 corresponds to the full-length amino acid sequence of the Paenibacillus endogenous Man4 mannanase.

The mannanase may be a variant of SEQ ID No. 4 comprising one, two, three, four, five, six, seven or more variants selected from:

(i) N10Q/T, P19E/V, S30T, T38E/I/L/M/Q/R/V, S59D/G/K/N/Q/T, L60F/M/V, T62E/I/Q/E, L66E/T/E67/D/E/P/Q/S/E/M/R/S/E/C/Q/E, Q78/D/L/E79E/F/E80/E97E/L/P/E, Y129E, T E, S135/C/E, K143E/S/W167/Y36167/Y E/Y129/E, Y E, T E, S E/C/E, P168A/E/G/L/M/S/T, Q184/F/H/L/M/P, N213E, K214C/Q, G225A/C/P/W, T A/G/H/I/K/S/V/Y, Y235/G/I/L/Q/S/V, Q S/E, K244A/C/G/L/M/P/S, S258A/D/E/G/M/N/P/T, G259A/E/R/S/W, N63261/M/P/Q/R/S/T/V/W/Y and D283G/H/T; or

(ii) P19E/V, T E/I/L/M/Q/R/V, N67/D/E/G/P/Q/S/V, N97E/L/P/Q, Y M, K143Q/R, P168A/E/L/S/T, Q184D/F/H/L/M/P, G A/C/P/W, T228A/G/H/I/K/S/V/Y, Y G/I/L/Q/S/V, K A/C/G/L/M/P/S, S258A/D/E/G/M/N/P/T and N261I/M/P/Q/R/S/T/V- W/Y; or

(iii) P19E/V, T38E/I/L/M/Q/R/V, N67A/D/E/P/Q/S/V, L85L, Y129M, P168A/E/G/L/M/S/T, Q184D/F/H/L/M/P, G225A/C/P/W, K244A/C/G/L/M/P/S, S258A/D/E/G/M/N/P/T and N261I/M/P/Q/R/S/T/V/W/Y; or

(iv) P19E, S30T, T38E, S59V, L60Q, K63R, N67D, N97D, V103I, Y129M, F167Y, P168S, Q184L, G225C, T228V, Y235L, K244L, S258D and N261R;

provided that one or more of the variants are non-naturally occurring; and wherein the amino acid positions of the mannanase variant or recombinant polypeptide or active fragment thereof are numbered by correspondence with the amino acid sequence of SEQ ID NO. 4.

Alternatively or additionally, the mannanase may be a variant of SEQ ID NO. 4 comprising a combination of variants of SEQ ID NO. 4 selected from P19E-T38E-N67D-N97D-Y129M-P168S-Q184L-K244L-S258D-N261R; N10T-P19E-G28S-S30T-T38E-N67D-N71D-N97D-Y129M-P168S-Q184L-G225C-Y235L-K244L-S258D-N261R-F297 FQ; P19E-S30T-T38E-S59V-L60Q-K63R-N67D-N97D-V103I-Y129M-F167Y-Q184L-G225C-T228V-Y235L-K244L-S258D-N261R-F297 FQ; N10T-P19E-S30T-T38E-S59V-L60Q-K63R-N67D-N97D-Y129M-K143Q-P168S-Q184L-G225C-T228V-Y235L-K244L-S258D-N261R-F297 FQ; N10T-P19E-S30T-T38E-S59V-L60Q-K63R-N67D-N97D-Y129M-K143Q-P168S-Q184L-G225P-T228V-Y235L-K244L-S258D-N261R-F297 FQ; N10T-P19E-S30T-T38E-S59V-L60Q-K63R-N67D-N71D-N97D-V103I-Y129M-K143Q-P168S-Q184L-G225P-T228V-Y235L-K244L-S258D-N261R-F297 FQ; A2S-P19E-G28S-S30T-T38E-K63R-N67D-N71D-N74E-K93R-N97D-Y129M-N150T-P168S-Q184L-N213A-G225C-Y235L-K244L-S258D-N261Q-F297 FQ; T3R-N10T-P19E-G28A-S30T-T38E-T62E-N67D-N71D-K93R-N97L-E111S-Y129M-D139M-P168S-Q184L-G225C-Y235L-K244L-S258D-N261Q-F297 FQ; and N10T-P19E-G28A-S30T-T38E-S59D-N67D-A68S-N71D-K93R-N97D-Y129M-K143Q-P168S-Q184D-G225C-Y235L-K244L-S258D-N261R-T284E-F297 FQ; and wherein the amino acid positions of the mannanase variant are numbered by correspondence with the amino acid sequence of SEQ ID NO. 4.

Mannanase activity can be determined using readily available assay kits, including those available from Megazyme (Bray, Ireland) and Glycospot ((R))Denmark) commercially available.

Lipase enzyme

The enzyme system preferably further comprises a lipase. The presence of oil and/or grease may further increase the resilience of stains containing mannan and other polysaccharides. Thus, the presence of lipase in the enzyme package may further improve the removal of such stains. Suitable lipases include those of bacterial, fungal or synthetic origin, as well as variants thereof. Chemically modified or protein engineered mutants are also suitable. Examples of suitable lipases include lipases from Humicola (Humicola), the synonym Thermomyces (Thermomyces), for example from Humicola lanuginosa (h.

The lipase may be a "first cycle lipase", for example, such as those described in WO06/090335 and WO 13/116261. In one aspect, the lipase is a first wash lipase, preferably a variant of a wild-type lipase from thermomyces lanuginosus comprising a T231R and/or N233R mutation.

Preferred lipases include those known under the trade nameAndthose sold by Novozymes (Bagsvaerd, Denmark).

Other suitable lipases include: lipr 1139, e.g. as described in WO 2013/171241; TfuLip2, e.g. as described in WO2011/084412 and WO 2013/033318; pseudomonas stutzeri lipase, e.g. as described in WO 2018228880; thermotolerant micrococcus (Microbulbifer thermoleterans) lipase, e.g. as described in WO 2018228881; thermothiobacillus acidophilus (Sulfobacillus acidocalarius) lipase, e.g. as described in EP 3299457; LIP062 lipase, e.g. as described in WO 2018209026; PinLip lipase, e.g., as described in WO 2017036901; and Absidia (Absidia sp.) lipases, e.g. as described in WO 2017005798.

Suitable lipases are variants of SEQ ID NO. 5, which comprise:

(a) substitution T231R

And

(b) substitution N233R or N233C

And

(c) at least three additional substitutions selected from the group consisting of E1C, D27R, N33Q, G38A, F51V, G91Q, D96E, K98L, K98I, D111A, G163K, H198S, E210Q, Y220F, D254S, I255A, and P256T;

wherein said position corresponds to the position of SEQ ID NO. 5 and wherein said lipase variant has at least 90% but less than 100% sequence identity to a polypeptide having the amino acid sequence of SEQ ID NO. 5 and wherein said variant has lipase activity.

One preferred lipase is a variant of SEQ ID NO 5 comprising the following substitutions: T231R, N233R, D27R, G38A, D96E, D111A, G163K, D254S and P256T.

One preferred lipase is a variant of SEQ ID NO 5 comprising the following substitutions: T231R, N233R, N33Q, G91Q, E210Q, I255A.

Suitable lipases are commercially available from Novozymes, for example as Lipex event 100L, Lipex event 200L (two liquid feedstocks) and Lipex event 105T (granules). These lipases have different structures compared to the products Lipex 100L, Lipex 100T and Lipex event 100T which are outside the scope of the present invention.

Other enzymes

The enzyme system may comprise other enzymes. Suitable enzymes provide cleaning performance and/or fabric care benefits. Examples of other suitable enzymes include, but are not limited to, hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratanases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, mailanases, β -glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, and known amylases, or combinations thereof. Preferred enzyme systems also comprise mixtures of conventional detersive enzymes such as protease, lipase, cutinase and/or cellulase in combination with amylase. Detersive enzymes are described in more detail in U.S. Pat. No. 6,579,839.

Optional ingredients

The detergent composition may further comprise one or more of the following optional ingredients: external structurants or thickeners, enzymes, enzyme stabilizers, cleaning polymers, bleaching systems, optical brighteners, shading dyes, particulate matter, perfumes and other odor control agents, hydrotropes, suds suppressors, fabric care benefit agents, pH adjusting agents, dye transfer inhibiting agents, preservatives, non-fabric substantive dyes, and mixtures thereof. In a more preferred embodiment, the laundry detergent composition does not comprise a bleaching agent.

External structurant or thickener: preferred external structurants and thickeners are those that do not rely on charge-charge interactions to provide a structuring benefit. Likewise, particularly preferred external structurants are uncharged external structurants, such as those selected from the group consisting of: non-polymeric crystalline hydroxy-functional structurants such as hydrogenated castor oil; microfibrillated cellulose; uncharged hydroxyethyl cellulose; uncharged hydrophobically modified hydroxyethyl cellulose; hydrophobically modified ethoxylated urethanes; a hydrophobically modified nonionic polyol; and mixtures thereof.

Suitable polymeric structurants include naturally derived and/or synthetic polymeric structurants.

Examples of naturally-derived polymeric structurants useful in the present invention include: microfibrillated cellulose, hydroxyethyl cellulose, hydrophobically modified hydroxyethyl cellulose, carboxymethyl cellulose, polysaccharide derivatives and mixtures thereof. Non-limiting examples of microfibrillated cellulose are described in WO 2009/101545 a 1. Suitable polysaccharide derivatives include: pectin, alginate, arabinogalactan (gum arabic), carrageenan, gellan gum, xanthan gum, guar gum, and mixtures thereof.

Examples of synthetic polymeric structurants or thickeners for use in the present invention include: polycarboxylates, hydrophobically modified ethoxylated urethanes (HEUr), hydrophobically modified nonionic polyols and mixtures thereof.

Preferably, the aqueous liquid detergent composition has a viscosity of from 50 to 5,000mpa.s, preferably from 75 to 1,000mpa.s, more preferably from 100 to 500mpa.s, when measured at a shear rate of 100s "1 and a temperature of 20 ℃. To improve the phase stability and also to improve the stability of suspended ingredients, the aqueous liquid detergent composition has a viscosity of from 50 to 250,000mpa.s, preferably from 5,000 to 125,000mpa.s, more preferably from 10,000 to 35,000mpa.s, when measured at a shear rate of 0.05s "1 and a temperature of 20 ℃.

Cleaning polymer: the detergent composition preferably comprises a cleaning polymer. It is believed that such cleaning polymers at least partially remove stains from textile fibers and enable the enzyme system to more effectively break down complexes comprising mannan and other polysaccharides. Suitable cleaning polymers provide soil cleaning and/or soil suspension for a wide range of surfaces and fabrics. Non-limiting examples of suitable cleaning polymers include: an amphiphilic alkoxylated grease cleaning polymer; clay soil cleaning polymers; a soil release polymer; and soil-suspending polymers. Preferred cleaning polymers are obtainable by free-radical copolymerization of: at least one compound of formula (I),

wherein n is a number equal to or greater than 3,

with at least one compound of the formula (II),

wherein A is^-Represents an anion, in particular selected from halides such as fluoride, chloride, bromide, iodide, sulfate, hydrogen sulfate, alkyl sulfates such as methyl sulfate, and mixtures thereof. Such polymers are further described in EP3196283a 1.

For similar reasons, polyester-based soil release polymers, such as SRA300 supplied by Clariant, are also particularly preferred.

Other useful cleaning polymers are described in USPN 2009/0124528a 1. Detergent compositions may comprise amphiphilic alkoxylated grease cleaning polymers which may have balanced hydrophilic and hydrophobic properties which allow them to remove grease particles from fabrics and surfaces. Suitable amphiphilic alkoxylated grease cleaning polymers may include a core structure and a plurality of alkoxylate groups attached to the core structure. These may include, for example, alkoxylated polyalkyleneimines. Such compounds may include, but are not limited to, ethoxylated polyethyleneimine, ethoxylated hexamethylene diamine, and sulfated versions thereof. Polypropoxylated derivatives may also be included. A wide variety of amines and polyalkyleneimines can be alkoxylated to various degrees. One useful example is a 600g/mol polyethyleneimine core ethoxylated to 20 EO groups per NH and available from BASF. The alkoxylated polyalkyleneimines can have an internal polyethyleneoxy block and an external polypropyleneoxy block. The detergent composition may comprise from 0.1% to 10%, preferably from 0.1% to 8%, more preferably from 0.1% to 2%, by weight of the detergent composition, of a cleaning polymer.

Dye transfer inhibitors: the detergent composition may comprise a dye transfer inhibitor. Suitable dye transfer inhibiting agents may be selected from the group consisting of: polyvinylpyrrolidone (PVP), Polyvinylimidazole (PVI), copolymers of vinylpyrrolidone and vinylimidazole (PVP/PVI), polyvinylpyridine-N-oxide, poly-N-carboxymethyl-4-vinylchloride pyridine, and mixtures thereof, with polyvinylpyrrolidone (PVP), Polyvinylimidazole (PVI), copolymers of vinylpyrrolidone and vinylimidazole (PVP/PVI), and mixtures thereof being particularly preferred. The dye transfer inhibiting agent may be present at a level of from 0.05% to 5%, preferably from 0.1% to 3%, and more preferably from 0.2% to 2.5% by weight of the detergent composition.

Polymeric deposition aid: the laundry detergent composition may comprise from 0.1% to 7%, more preferably from 0.2% to 3% of a polymeric deposition aid. As used herein, "polymeric deposition aid" refers to any cationic polymer or combination of cationic polymers that significantly enhances the deposition of fabric care benefit agents onto fabrics during laundering. Suitable polymeric deposition aids may include cationic polysaccharides and/or copolymers, preferably cationic polysaccharides, and most preferably polyquaternium 7. As used herein, "fabric care benefit agent" refers to any material that can provide fabric care benefits. Non-limiting examples of fabric care benefit agents include: silicone derivatives, oily sugar derivatives, dispersed polyolefins, polymer latexes, cationic surfactants, and combinations thereof. Preferably, the deposition aid is a cationic polymer or an amphoteric polymer. The cationic charge density of the polymer is preferably in the range of 0.05 to 6 meq/g. The charge density is calculated by dividing the number of net charges per repeat unit by the molecular weight of the repeat unit. In one embodiment, the charge density varies from 0.1 meq/g to 3 meq/g. The positive charge may be located on the backbone of the polymer or on a side chain of the polymer.

Organic builders and/or chelating agents: what is needed isThe laundry detergent composition may comprise from 0.6 wt% to 10 wt%, preferably from 2 wt% to 7 wt%, of one or more organic builders and/or chelating agents. Suitable organic builders and/or chelating agents are selected from the group consisting of: MEA citrate, citric acid, aminoalkylene poly (alkylene phosphonates), alkali metal ethane 1-hydroxy bisphosphonates, and nitrilotrimethylene phosphonates, diethylenetriamine penta (methylene phosphonic acid) (DTPMP), ethylenediamine tetra (methylene phosphonic acid) (DDTMP), hexamethylenediamine tetra (methylene phosphonic acid), hydroxy-ethylene-1, 1-diphosphonic acid (HEDP), hydroxyethane dimethylene phosphonic acid, ethylenediamine disuccinic acid (EDDS), ethylenediamine tetraacetic acid (EDTA), hydroxyethylethylenediamine triacetic acid (HEDTA), nitrilotriacetic acid (NTA), methylglycine diacetate (MGDA), iminodisuccinic acid (IDS), hydroxyethyliminodisuccinic acid (HIDS), hydroxyethyliminodiacetic acid (HEIDA), glycine diacetate (GLDA), diethylenetriamine pentaacetic acid (DTPA), Catecholate sulfonates such as Tiron^TMAnd mixtures thereof.

Enzyme stabilizer: any known stabilizer system may be used to stabilize the enzyme, such as calcium and/or magnesium compounds, boron compounds and substituted boric acids, aromatic borate esters, peptides and peptide derivatives, polyols, low molecular weight carboxylic acid esters, relatively hydrophobic organic compounds [ e.g., certain esters, dialkyl glycol ethers, alcohol or alcohol alkoxylates ], alkyl ether carboxylates other than a source of calcium ions, benzamidine hypochlorite, lower aliphatic alcohols and carboxylic acids, N-bis (carboxymethyl) serine salts; (meth) acrylic acid- (meth) acrylate copolymer and PEG; lignin compounds, polyamide oligomers, glycolic acid or salts thereof; polyhexamethylene biguanide or N, N-bis-3-aminopropyldodecylamine or salt; and mixtures thereof.

Toning dye: the detergent composition may comprise a fabric hueing agent (sometimes referred to as a sunscreen, bluing agent, or whitening agent). Toners generally provide a blue or violet shade to a fabric. Toners can be used alone or in combination to create a particular shade of toning and/or to tone different fabric types. This may be provided, for example, by mixing red and blue-green dyes to produce a blue or violet hue. The toner may be selected from any known chemical class of dyes including, but not limited to, acridines, anthraquinones (including polycyclic quinones), azines, azos (e.g., monoazo, disazo, trisazo, tetrazo, polyazo), including premetallized azos, benzodifurans and benzodifuranones, carotenoids, coumarins, cyanines, diaza-hemicyanines, diphenylmethane, formazans, hemicyanines, indigoids, methane, naphthalimides, naphthoquinones, nitro and nitrosos, oxazines, phthalocyanines, pyrazoles, stilbenes, styryls, triarylmethanes, triphenylmethanes, xanthenes, and combinations thereof.

Optical brightening agent: the detergent composition may comprise from 0.005% to 2%, preferably from 0.01% to 0.1% of fluorescer (optical brightener) by weight of the total detergent composition. Fluorescent agents are well known and many are commercially available. Typically, these fluorescent agents are provided and used in the form of their alkali metal salts (e.g., sodium salts). A preferred class of fluorescent agents is: distyrylbiphenyl compounds such as Tinopal (trademark) CBS-X; diamine stilbene disulfonic acid compounds such as Tinopal DMS pure Xtra and Blankophor (trade Mark) HRH; and pyrazoline compounds such as Blankophor SN. Preferred fluorescent agents are: sodium 2- (4-styryl-3-sulfophenyl) -2H-naphthol [1,2-d ] triazole, disodium 4,4 ' -bis { [ (4-anilino-6- (N-methyl-N-2-hydroxyethyl) amino 1,3, 5-triazin-2-yl) ] amino } stilbene-2-2 ' disulfonate, disodium 4,4 ' -bis { [ (4-anilino-6-morpholino-1, 3, 5-triazin-2-yl) ] amino } stilbene-2-2 ' disulfonate, and disodium 4,4 ' -bis (2-sulfostyryl) biphenyl.

Hydrotrope: the detergent composition may comprise from 0% to 30%, preferably from 0.5% to 5%, more preferably from 1.0% to 3.0% by weight of the total detergent composition of a hydrotrope, which may prevent liquid crystal formation. Thus, the addition of a hydrotrope aids clarity/clarity of the composition. Suitable hydrotropes include, but are not limited to, urea, benzene sulfonate, toluene sulfonate, xylene sulfonate or cumene sulfonate. Preferably, the hydrotrope is selected from the group consisting of propylene glycol, xylene sulfonate, ethanol, and urea to provide optimal performance.

And (3) particle: the composition may further comprise particles, especially when the composition further comprises a structurant or thickener. The composition may comprise from 0.02% to 10%, preferably from 0.1% to 4%, more preferably from 0.25% to 2.5% of particles by weight of the total composition. The particles include beads, pearlescers, microcapsules, and mixtures thereof.

Microcapsule: suitable capsules are generally formed by at least partially, preferably completely, surrounding the beneficial agent with a wall material. Preferably, the capsules are perfume capsules, wherein the benefit agent comprises one or more perfume raw materials. The capsule wall material may include: melamine, polyacrylamide, silicone, silica, polystyrene, polyurea, polyurethane, polyacrylate based materials, gelatin, styrene maleic anhydride, polyamide, aromatic alcohol, polyvinyl alcohol, resorcinol based materials, polyisocyanate based materials, acetals (such as 1,3, 5-triol-benzene-glutaraldehyde and 1,3, 5-triol-benzene melamine), starch, cellulose acetate phthalate, and mixtures thereof. Preferably, the capsule wall comprises melamine and/or polyacrylate based material. The perfume capsules may be coated with a deposition aid, a cationic polymer, a nonionic polymer, an anionic polymer, or mixtures thereof. Preferably, the perfume capsules have a volume weighted median particle size of from 0.1 micron to 100 microns, preferably from 0.5 micron to 60 microns. The composition may further comprise one or more formaldehyde scavengers, especially when the composition comprises capsules having a shell formed at least in part from formaldehyde.

Process for making a laundry detergent composition：

The laundry detergent composition may be prepared using any suitable method known to the skilled person. Typically, the ingredients are blended together in any suitable order. Preferably, the detersive surfactant is added as part of a concentrated premix to which other optional ingredients are added. Preferably, the solvent is added last, or if an external structurant is added, immediately before the external structurant, when the external structurant is added as a final ingredient.

Method for washing fabrics：

The laundry detergent composition of the present invention is useful for washing fabrics. In such processes, the laundry detergent composition is diluted to provide a wash liquor having a total surfactant concentration of greater than 300ppm, preferably from 400ppm to 2,500ppm, more preferably from 600ppm to 1000 ppm. The fabric is then washed in a wash liquor and preferably rinsed.

The method of the invention is particularly suitable for removing stains, especially when the stain comprises a combination of mannans and other polysaccharides, and especially when the stain further comprises oils and/or fats, such as natural oils and/or natural fats, such as animal fats, vegetable fats, and mixtures thereof.

Method：

A) pH measurement：

The pH was measured at 25 ℃ using a Santarius PT-10P pH meter with a gel-filled probe (such as a Toledo probe, part number 52000100) calibrated according to the instructions. The pH was measured at 10% dilution in deionized water (i.e., 1 part laundry detergent composition and 9 parts deionized water).

B) Method for measuring viscosity：

Viscosity was measured using an AR 2000 rheometer from TA instruments using a cone-plate geometry with a diameter of 40mm and an angle of 1 °. Through heating at 20 deg.C for 3 min from 0.1s^-1To 1200s^-1Log shear rate scans to measure viscosity at different shear rates. At 0.05s^-1Low shear viscosity is measured at a continuous shear rate of (2).

Example (b):

the following are examples of liquid laundry detergent compositions of the present invention.

Enzyme content is given in mg of active enzyme protein per 100g of finished product

1Pro 104L, supplied by BASF

224L, supplied by Novozymes

3FLX1 supplied by AB Enzymes

4100L, supplied by Novozymes

5a xanthan endoglucanase comprising a sequence identical to SEQ ID NO:1, such as a variant of SEQ ID NO:1 having a substitution at F20P, I302D, S313D, E408D, D476R, Y579W, I602T, S636N, T697G, W719R, V756Y, a824D, N848D, V881Q, T887K, F906A, S928D, a937E, T999R, F1048W.

6 Xanthan lyase comprising a polypeptide having at least 60% sequence identity to SEQ ID NO 2, e.g. a variant of SEQ ID NO 2 having substitutions at E229S, N399K, D458S, K567R, S582K, S635E, N672D, G753E, S754E, A769D, L775A, D777R, D801G, K875T, N892Y.

7 mannanase comprising a variant of SEQ ID NO. 4, e.g. a variant of SEQ ID NO. 4 comprising the variant at N10T-P19E-G28A-S30T-T38E-S59D-N67D-A68S-N71D-K93R-N97D-Y129M-K143Q-P168S-Q184D-G225C-Y235L-K244L-S258D-N261R-T284E-F297 FQ.

Lipase variants of SEQ ID NO. 5, such as Lipex event 100L or 200L

9 hydroxy ethylidene diphosphonic acid

10 diethylene triamine penta (methylene phosphonic acid)

11 polyvinylpyrrolidone-polyvinylimidazole, wherein the proportion of N-vinylpyrrolidone is at least 50% by weight and the weight average molecular weight is about 40,000

The following are low water liquid laundry detergent compositions which may be encapsulated in a water-soluble film to provide the water-soluble unit dose articles of the present invention. Typically, 24g of the low water liquid laundry detergent composition may be encapsulated in a polyvinyl alcohol film to provide a water soluble unit dose article. The enzyme content is given in mg of active enzyme protein per 100g of finished product.

	Example 5
		Active substance in the formulation	By weight%
C14-C15 alkyl ethoxylate (degree of ethoxylation 7)	3.1
		C12-C14 alkyl ethoxylate (degree of ethoxylation 9)	0.9
C11-C13 alkyl benzene sulfonate	23.2
		C12-C15 alkyl ether sulfate (degree of ethoxylation 2.5)	15.9
Coconut oil fatty acid	6.4
		Citric acid	0.9
1, 2-propanediol	12.2
		Dipropylene glycol/tripropylene glycol	4.4
Monoethanolamine	8.6
		Glycerol	4.1
Protease enzyme1*	32
		Amylase2*	12
Cellulase enzymes3*	5
		Pectate lyase4*	13
Xanthan gum endoglucanase5*	18
		Xanthan gum lyase6*	9
Mannanase7*	10
		Lipase enzyme8*	11
DTPA (sodium salt)12	0.15
		Ethoxylated polyethyleneimine13	3.5
Amphiphilic graft polymers14	2.2
		Whitening agent	0.06
Perfume	0.5
		Water (W)	9.8
pH (Using NaOH)	To pH 8
		The balance (spice, preservative, antioxidant, etc.)	To 100

Enzyme content is given in mg of active enzyme protein per 100g of finished product

11 Diethylenetriaminepentaacetic acid, sodium salt

12 branched polyethyleneimine core having a weight average molecular weight of 600g/mol, each NH being ethoxylated to 20 EO groups, available from BASF

13 amphiphilic graft polymers based on water-soluble polyethylene oxide (a) as the graft base and side chains formed by polymerization of a vinyl ester component (B), said polymers having an average of ≦ 1 graft site per 50 alkylene oxide units and a weight average molecular weight of 3000 to 100000.

The dimensions and values disclosed herein are not to be understood as being strictly limited to the exact numerical values recited. Rather, unless otherwise specified, each such dimension is intended to mean both the recited value and a functionally equivalent range surrounding that value. For example, a dimension disclosed as "40 mm" is intended to mean "about 40 mm".