Enzyme-containing detergent compositions

Abstract

A detergent composition, particularly for laundry, comprising an alginate lyase enzyme and a booster enzyme selected from one or more of (i) a Pel-ase enzyme, (ii) a Psl-ase enzyme, (iii) an endo-β-1,3(4)-glucanase enzyme, and (iv) mixtures thereof. A method of treating fabrics by contacting the fabrics with an aqueous wash liquor having the detergent composition therein. The compositions and methods are particularly for improving the whiteness of fabrics, improved stain removal from fabrics, removal of malodors from fabrics, anti-wrinkle benefits, collar and / or cuff cleaning, anti-redeposition benefits, and / or improved drying of fabrics.

Description

[Technical field]

[0001] (Reference to sequence listing) The present specification contains a sequence listing in computer readable form, which is incorporated herein by reference.

[0002] FIELD OF THEINVENTION The present invention relates to detergent compositions, particularly for laundry, that contain an alginate lyase enzyme and a booster enzyme. The present invention also relates to cleaning methods that use the detergent compositions. [Background technology]

[0003] In particular in laundry cleaning applications, the loss of whiteness over time and the removal of dirt and stains continue to be problems. Many cleaning technologies exist that aim to alleviate these problems, but it is always a challenge to improve their effectiveness, especially in an environmentally friendly manner. In automatic washing machines, these problems are further exacerbated by the increasing use of low washing temperatures (e.g., cold water) and short washing cycles, which reduces the stain / soil removal effectiveness of detergent compositions and exacerbates the problem of redeposition of dirt on the fabric surface during the washing process and loss of whiteness over multiple washes. Thus, the accumulation of dirt over time is a problem for both colored and white fabrics, but can be particularly noticeable on white or light-colored fabrics, for example around collars and sleeves where incomplete washing occurs. It can also lead to malodors, which are problematic. The compositions and methods of the present invention are suitable for use in hand and automatic washing, as well as laundry detergent compositions. Summary of the Invention [Problem to be solved by the invention]

[0004] It is therefore an object of the present invention to provide a detergent composition, in particular for laundry, which can be used in the washing process even at low temperatures and short washing times, which composition prevents loss of whiteness and / or removes complex stains, for example allows removal of dark stains, thorough cleaning, removal of yellowing, cleaning in particular of collars and cuffs and / or improves whiteness / prevents whiteness loss, which can be useful even at low temperatures and short washing times. [Means for solving the problem]

[0005] The present invention provides a detergent composition, particularly for laundry, comprising: (a) 0.00005-5% by weight of an alginate lyase enzyme (active enzyme protein); and (b) 0.00005%-5% by weight of an enzyme (active enzyme protein) of a booster enzyme selected from one or more of: (i) Pel-ase enzyme, (ii) Psl-ase enzyme, (iii) endo-β-1,3(4)-glucanase enzyme, and (iv) mixtures thereof. Preferably, the composition also comprises 1-60% by weight of an anionic surfactant.

[0006] The present invention also provides a method of treating a fabric comprising contacting the fabric with an aqueous wash liquor comprising an alginate lyase enzyme and one or more booster enzymes selected from (i) a Pel-ase enzyme, (ii) a Psl-ase enzyme, (iii) an endo-β-1,3(4)-glucanase enzyme, and (iv) mixtures thereof, and optionally an anionic surfactant.

[0007] Preferably, the aqueous cleaning liquid comprises the anionic surfactant in an amount of from 0.05 g / l to 5 g / l, preferably from 0.01 g / l to 3 g / l.

[0008] The fabric is typically contacted with the aqueous wash solution at a temperature of 60° C. or less, preferably 40° C. or less or 35° C. or less, and most preferably 30° C. or less or even 25° C. or less, and (iii) optionally the surface is rinsed. The compositions and methods herein are particularly useful for treating any fabric surface, synthetic or natural, including blended fabrics such as cotton, wool, silk, polyester, nylon, elastane, or polycotton.

[0009] The present invention also relates to the use of the above compositions or methods for improving the whiteness or preventing loss of whiteness of fabrics, improving stain removal from fabrics, removing dark stains, thorough cleaning, removing or reducing yellowing, cleaning collars and / or cuffs, reducing or removing malodors from fabrics, preventing fabrics from wrinkling, improving fabric drying, and preventing soil redeposition. The compositions and methods described herein may also provide a biofilm disrupting effect. DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS

[0010] definition Parent or Parent Enzyme: The term "parent" or "parent enzyme" refers to an enzyme that is modified to produce an enzyme variant. A parent can be a naturally occurring (wild type) polypeptide or a variant thereof. For example, an alginate lyase parent can be any of SEQ ID NOs: 1, 2, 3, 4, 5, 6 or 7 listed herein.

[0011] Sequence identity: The relatedness between two amino acid sequences or between two nucleotide sequences is expressed 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 later. Optionally, the parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled "longest identity" (obtained using the -nobrief option) is used as the percentage identity, which is calculated as follows: (identical residues × 100) / (length of alignment − total number of gaps in alignment)

[0012] Alternatively, the optional parameters used can be a gap opening penalty of 10, a gap extension penalty of 0.5, and an EDNAFULL (the EMBOSS version of NCBI NUC4.4) substitution matrix. The output of Needle labeled "longest identity" (obtained using the -nobrief option) is used as the percent identity, which is calculated as follows: (identical deoxyribonucleotides × 100) / (length of alignment − total number of gaps in alignment)

[0013] Variant: The term "variant" refers to a polypeptide having enzymatic activity, which includes modifications / mutations, i.e. substitutions, insertions, and / or deletions, at one or more (e.g., several) positions relative to the parent. A substitution refers to the replacement of an amino acid occupying a position with a different amino acid, a deletion refers to the removal of an amino acid occupying a position, and an insertion refers to the addition of 1-3 amino acids adjacent to and immediately following the amino acid occupying a position.

[0014] Wild-type enzyme: The term "wild-type" enzyme refers to an enzyme expressed by a naturally occurring microorganism, such as a bacterium, algae, yeast, or filamentous fungus, as found in nature.

[0015] Detergent Composition The detergent composition comprises: (a) 0.00005-5% by weight of an alginate lyase enzyme (active enzyme protein); and (b) 0.00005%-5% by weight of an enzyme (active enzyme protein) of a booster enzyme selected from one or more of: (i) a Pel-ase enzyme, (ii) a Psl-ase enzyme, (iii) an endo-β-1,3(4)-glucanase enzyme, and (iv) mixtures thereof. The detergent composition optionally comprises a detergent adjuvant.

[0016] The detergent compositions of the present invention are preferably laundry detergents. The compositions may be in the form of compositions for use in the main wash step, or as pre-treatment or rinse-additive cleaning compositions for consumer or institutional use.

[0017] Alginate lyase enzyme The alginate lyase is preferably of microbial origin, preferably of bacterial or algae (eg from brown seaweeds (Phaeophyceae) such as Ascophyllum, Laminara, Macrocystis), most preferably of bacterial origin. The alginate lyase enzyme may be obtained from Aeromonas sp., Azotobacter sp., Bacillus sp., Flavobacterium sp., Klebsiella sp., Pseudomonas sp., Sphingomonas sp., Vibrio sp., Zobellia galactanivorans, and most preferably Flavobacterium sp.

[0018] Preferably, the alginate lyase enzyme is an alginate lyase having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:1; an alginate lyase having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:2; an alginate lyase having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:3. an alginate lyase having at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:4; an alginate lyase having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:5;The alginate lyases include those selected from an alginate lyase having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 6; an alginate lyase having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 7; or mixtures thereof. Preferred alginate lyase enzymes include alginate lyase enzymes corresponding to the wild type or preferably wild type variant of any one of SEQ ID NOs: 1, 2, 3, 4, 5, 6 or 7 as set forth herein, or mixtures thereof. SEQ ID NOs: 6, 7 and variants thereof, and mixtures thereof are particularly preferred.

[0019] Where the alginate lyase enzyme is a variant of a parent amino acid sequence, the parent alginate lyase enzyme preferably has at least 50%, or at least 60%, or at least 70%, or at least 80%, such as at least 85%, at least 90%, such as 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 one or more polypeptides of SEQ ID NOs: 1, 2, 3, 4, 5, 6, or 7, and has alginate lyase enzymatic activity. It may be preferred that the variant amino acid sequence differs from the parent alginate lyase by no more than 15, or no more than 10 amino acids, or no more than 5, or 4, or 3, or 2, or 1 amino acid from one or more polypeptides of SEQ ID NOs: 1, 2, 3, 4, 5, 6, or 7.

[0020] When the alginate lyase enzyme is a variant of a parent amino acid sequence, the parent may be obtained from any genus of microorganism. For the purposes of the present invention, the term "obtained from" when used herein in reference to a given source shall mean that the parent encoded by the polynucleotide is produced by that source or by a cell into which a polynucleotide from that source is inserted. In one embodiment, the parent is secreted extracellularly. Variants may be prepared using any mutagenesis technique known in the art, such as site-directed mutagenesis, synthetic gene construction, semi-synthetic gene construction, random mutagenesis, shuffling, etc.

[0021] The alginate lyase can be from any polysaccharide lyase (PL) family, including PL5, PL6, PL7, PL14, PL15, PL17, PL18, PL32, PL34, and PL36. Preferably, the alginate lyase is from PL family 7.

[0022] Preferably, the alginate lyase enzyme has activity towards poly(beta-D-mannuronate) (poly M activity) and activity towards poly(alpha-L-guluronate) (poly G activity). The alginate lyase enzyme may comprise a single alginate lyase enzyme to provide poly M activity and poly G activity, or may comprise two or more alginate lyase enzymes which in combination provide poly M and poly G activity. Preferably, the alginate lyase comprises an enzyme having both poly M activity and poly G activity. Preferably, the poly M activity as defined in Test Method 1 of the Testing section herein is at least 0.1 absorbance units, preferably at least 0.15 absorbance units, most preferably at least 2 absorbance units. Preferably, the poly G activity as defined in Test Method 1 of the Testing section herein is at least 0.3 absorbance units, preferably at least 0.4 absorbance units, or at least 0.5, or even at least 0.6 absorbance units. The alginate lyase enzyme may be incorporated into the cleaning compositions and methods of the present invention in the form of a substantially pure enzyme, or, particularly where the enzyme is a variant of a wild-type enzyme, the variant is not recovered, but rather a host cell expressing the enzyme is used as the source of the alginate lyase enzyme.

[0023] The alginate lyase enzyme may be in the form of a liquid or dry composition. For example, the composition may be in the form of particles or microparticles. The alginate lyase enzyme may be stabilized, including by encapsulation, according to methods known in the art.

[0024] The alginate lyase enzyme is present in the composition in an amount of 0.00005 to 5% by weight of active enzyme protein, preferably 0.0001 to 2% by weight of active enzyme protein, or 0.0005 or 0.001 to 1% by weight of active enzyme protein, or up to 0.5% by weight or 0.1% by weight or 0.05% by weight of active enzyme protein.

[0025] Preferably the alginate lyase enzyme is present in the aqueous wash liquor in an amount from 0.01 ppm to 1000 ppm, or from 0.05 or 0.1 ppm to 750 or 500 ppm of enzyme.

[0026] Pel-ase enzyme The Pel-ase enzyme exhibits glycoside hydrolase activity towards the Pel polysaccharide and typically or preferably belongs to the endo-alpha-1,4-polygalactosminidase class of enzymes (EC 3.2.1.109) having preferably at least 60% or 65% or more, more preferably at least 70% or 75% or 80% or 85% or 90% or 95% to 100% identity to one or more of SEQ ID NOs: 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, or 40.

[0027] Preferably, the Pel-ase glycoside hydrolase is an isolated glycoside hydrolase.

[0028] Preferably, the Pel-ase glycoside hydrolase enzyme is present in the cleaning composition in an amount of 0.001 to 1 wt %, based on the active protein in the composition, or 0.005 to 0.5 wt %, or 0.01 to 0.25 wt %, based on the weight of the composition.

[0029] Preferably, the Pel-ase glycoside hydrolase enzyme is present in the aqueous wash liquor in an amount of from 0.01 ppm to 1000 ppm enzyme, or from 0.05 or 0.1 ppm to 750 or 500 ppm based on active protein.

[0030] Pel-ase as described herein may also provide a biofilm disrupting effect or an anti-soil redeposition effect.

[0031] Psl-ase enzyme The Psl-ase enzyme exhibits glycoside hydrolase activity towards the Psl polysaccharide. The Psl-ase preferably has at least 60% or 65% or more, preferably at least 70% or 75% or 80% or 85% or 90% or 95% to 100% identity to one or more of SEQ ID NOs: 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, or 52.

[0032] Preferably, the Psl-ase glycoside hydrolase is an isolated glycoside hydrolase.

[0033] Preferably, the Psl-ase glycoside hydrolase enzyme is present in the cleaning composition in an amount of from 0.001 to 1 wt. %, or from 0.005 to 0.5 wt. %, or from 0.01 to 0.25 wt. % based on active protein.

[0034] Preferably the Psl-ase glycoside hydrolase enzyme is present in the laundry aqueous liquor in an amount from 0.01 ppm to 1000 ppm enzyme, or from 0.05 or 0.1 ppm to 750 or 500 ppm based on active protein.

[0035] Compositions including the Psl-ase glycoside hydrolase enzymes described herein may also provide or be useful in biofilm disruption or soil redeposition prevention effects.

[0036] Endo-beta-1,3(4)-glucanase enzyme The endo-beta-1,3(4)-glucanase enzyme typically or preferably belongs to class EC 3.2.1.6 and exhibits significant endo-beta-1,3-glucanase activity towards polysaccharides having an endo-beta-1,3-glucan backbone (e.g., curdlan, patiman, laminarin, scleroglucan, schizophyllan), as well as so-called "mixed linkage" glucan polysaccharides containing both beta-1,3- and beta-1,4 linkages, such as those found in cereals such as oats and barley. Activity towards both of these substrates can be confirmed using Test Method 2. The beta-1,3(4)-glucanase preferably has at least 60% or 65% or more, more preferably at least 70% or 75% or 80% or 85% or 90% or 95% to 100% identity to one or more of SEQ ID NOs: 53, 54, 55, 56, 57, or 58.

[0037] The booster enzymes include one or more of (i) a Pel-ase enzyme, (ii) a Psl-ase enzyme, (iii) an endo-β-1,3(4)-glucanase enzyme, and (iv) a mixture thereof. The booster enzymes may include a Pel-ase enzyme and a Psl-ase enzyme, and optionally an endo-β-1,3(4)-glucanase enzyme; a Pel-ase enzyme and an endo-β-1,3(4)-glucanase enzyme, and optionally a Psl-ase enzyme; or an endo-β-1,3(4)-glucanase enzyme and a Psl-ase enzyme, and optionally a Pel-ase enzyme.

[0038] The composition includes an optional cleaning adjunct. Typically, the cleaning adjunct is present in the composition in an amount of 1-98.9% by weight, more typically 5-90% by weight of the cleaning adjunct. Suitable cleaning adjuncts include additional surfactants, builders, bleaching agent components, colorants, chelating agents, dye transfer agents, deposition aids, dispersants, additional enzymes and enzyme stabilizers, catalytic materials, optical brighteners, photoactivators, fluorescent agents, fabric hueing agents (shading dyes), fabric conditioners, preformed peracids, polymeric dispersants, mud stain removers / anti-redeposition agents, filler salts, hydrotropes, brighteners, suds suppressors, structural stretch agents, fabric softeners, preservatives, antioxidants, shrinkage inhibitors, bactericides, fungicides, discoloration inhibitors, corrosion inhibitors, alkalinity sources, solubilizers, carriers, processing aids, pigments, dyes, fragrances and pH adjusters, encapsulating agents, polymers and mixtures thereof.For example, these include bleach components such as bleach activators, bleach accelerators such as imine bleach accelerators, bleach catalysts, hydrogen peroxide, hydrogen peroxide sources such as percarbonates and / or perborates, particularly percarbonates coated with materials such as carbonates and / or sulfates, silicates, borosilicates, and any mixtures thereof, preformed peracids including encapsulated forms of preformed peracids, transition metal catalysts; foam suppressors or foam suppressor systems, such as silicone-based foam suppressors and / or fatty acid-based foam suppressors; clay, silicone, and / or quaternary ammonium compounds. flocculants such as polyethylene oxide; dye transfer inhibitors such as polyvinylpyrrolidone, poly 4-vinylpyridine N-oxide, and / or copolymers of vinylpyrrolidone and vinylimidazole; fabric integrity components such as oligomers produced by the condensation of imidazole with epichlorohydrin; soil dispersants and soil anti-redeposition aids such as alkoxylated polyamines and ethoxylated ethyleneimine polymers; anti-redeposition components such as polyesters; carboxylate polymers, e.g., maleic acid, ethylenediamine, ethylenediaminetetraacetate ... fillers such as sodium sulfate and / or citrus fibers (although it may be preferred that the compositions are substantially free of fillers); silicates such as sodium silicates, including 1.6R and 2.0R sodium silicates, or sodium metasilicate; copolyesters of dicarboxylic acids and diols; cellulosic polymers such as methylcellulose, carboxymethylcellulose, hydroxyethoxycellulose, or other alkyl or alkylalkoxycelluloses; solvents such as 1,2 propanediol, monoethanolamine; diethylene glycol, ethanol, and any mixtures thereof; hydrotropes such as sodium cumene sulfonate, sodium xylene sulfonate, sodium toluene sulfonate, and any mixtures thereof; organic acids and their salts, such as citric acid / citrates; and any combinations thereof.The composition may be such that the cleaning adjunct comprises one or more selected from the group consisting of: (i) perfume microcapsules; (ii) fabric hueing agents; (iii) proteases; (iv) amphiphilic cleaning polymers; (v) lipases; or (vi) mixtures thereof.

[0039] Anionic Surfactants The inventors have found that the enzyme combination decomposes soils well, but the presence of an anionic surfactant improves the removal of substrate degradation products and soils containing them. Thus, the laundry detergent composition comprises 1-60% by weight of anionic surfactant. Preferably, the weight ratio of anionic surfactant to active alginate lyase enzyme protein is at least 500:1, preferably at least 1000:1, or at least 1500:1, or at least 2000:1, and is preferably not more than 500000:1, preferably not more than 400000:1, or not more than 200000:1, or at most 150000:1 or 100000:1 or 50000:1 or 10000:1. Preferably, the weight ratio of anionic surfactant to activity booster enzyme protein is at least 500:1, preferably at least 1000:1, or at least 1500:1, or at least 2000:1, preferably not more than 500000:1, preferably not more than 400000:1, or not more than 200000:1, or at most 150000:1 or 100000:1 or 50000:1 or 10000:1.

[0040] Preferred anionic surfactants are sulfonate and sulfate surfactants, preferably alkylbenzenesulfonates and / or (optionally alkoxylated) alkyl sulfates. Particularly preferred anionic surfactants include linear alkylbenzenesulfonates (LAS). Preferred alkyl sulfates include alkyl ether sulfates, especially C-9-15 alcohol ether sulfates, especially those having an average degree of ethoxylation of 0.5-7, preferably 1-5, C8-C16 ester sulfates, and C10-C14 ester sulfates, such as monododecyl ester sulfate. In a preferred composition, the anionic surfactant comprises an alkylbenzenesulfonate and, optionally, an optionally ethoxylated alkyl sulfate, preferably having an ethoxylation degree of 0-7, more preferably 0.5-3. Isomers of LAS, branched alkylbenzene sulfonates (BABS), phenylalkane sulfonates, alpha-olefin sulfonates (AOS), olefin sulfonates, alkenesulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS), e.g. sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ether sulfates (AES or AEOS or FES, alcohol ethoxy sulfates or aliphatic Also suitable anionic surfactants are fatty acid derivatives of amino acids, di- and monoesters of sulfosuccinic acid, or salts of fatty acids (soaps), and combinations thereof.

[0041] The anionic surfactant is preferably added to the detergent composition in the form of a salt. Preferred cations are alkali metal ions such as sodium and potassium. However, the salt form of the anionic surfactant may be formed in situ by neutralizing the acid form of the surfactant with an alkali such as sodium hydroxide, or an amine such as mono-, di-, or triethanolamine. The composition preferably comprises 1-60%, or 1-50%, or 2, or 5-40% anionic surfactant by weight of the composition. The surfactant preferably comprises a surfactant system comprising an anionic surfactant and one or more additional surfactants which may be non-ionic, including semi-polar and / or cationic and / or zwitterionic and / or amphoteric and / or semi-polar non-ionic and / or mixtures thereof.

[0042] The present invention also provides a cleaning composition comprising 0.00005-5% by weight (active enzyme protein) of an alginate lyase enzyme, 0.00005-5% by weight of a booster enzyme (active enzyme protein), and a surfactant, wherein the surfactant comprises an anionic surfactant and a nonionic surfactant, and the weight ratio of the anionic to the nonionic is preferably 30:1-1:2, preferably 20:1-2:3 or 1:1.

[0043] Suitable nonionic surfactants include alcohol ethoxylates (AE), alcohol propoxylates, propoxylated fatty alcohols (PFAs), alkoxylated fatty acid alkyl esters, such as ethoxylated and / or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APEs), nonylphenol ethoxylates (NPEs), alkyl polyglycosides (APGs), alkoxylated amines, fatty acid monoethanolamides (FAMs), fatty acid diethanolamides (FADAs), ethoxylated fatty acid monoethanolamides (EFAMs), propoxylated fatty acid monoethanolamides (PFAMs), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GAs, or fatty acid glucamides, FAGAs), as well as products available under the trade names SPAN and TWEEN, and combinations thereof. Alcohol ethoxylates are particularly preferred, preferably having alkyl chains of C9-18 or preferably C12-15, and an average degree of ethoxylation preferably of 3 to 9, more preferably of 3 to 7. Commercially available non-ionic surfactant cleaners include Plurafac™, Lutensol™, and Pluronic™ from BASF, the Dehypon™ series from Cognis, and the Genapol™ series from Clariant.

[0044] The detergent composition preferably comprises from 0.5% to about 40% by weight of a nonionic surfactant, preferably from 1 to 30% by weight of the composition.

[0045] The detergent composition preferably comprises one or more additional enzymes. Thus, a preferred composition comprises (a) an alginate lyase; (b) a booster enzyme; and (c) one or more additional enzymes selected from the group consisting of aminopeptidase, amylase, carbohydrase, carboxypeptidase, catalase, cellulase, chitinase, cutinase, cyclodextrin glycosyltransferase, esterase, alpha-galactosidase, beta-galactosidase, glucoamylase, alpha-glucosidase, beta-glucosidase, haloperoxidase, hexosaminidase, invertase, laccase, lipase, mannanase, mannosidase, nuclease, oxidase, pectolytic enzyme, peptidoglutaminase, peroxidase, phytase, polyphenol oxidase, proteolytic enzyme, transglutaminase, xylanase, xanthan lyase, xanthanase, endo-β-1,3-glucanase, and mixtures thereof. Preferably, the cleaning composition comprises an additional enzyme selected from a nuclease such as DNase or RNase, mannanase, xanthan lyase, xanthanase, amylase, and mixtures thereof.

[0046] The composition preferably comprises an additional enzyme selected from xanthan lyase, xanthanase, mannanase, and mixtures thereof, with mannanase being particularly preferred.

[0047] The additional enzyme may be, for example, an Aspergillus species, such as Aspergillus aculetus, Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger, or Aspergillus oryzae; Fusarium species, such as Fusarium bactridioides, Fusarium cerealis, Fusarium cloquewellens, Fusarium culmorum, Fusarium graminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negunji, Fusarium okinawanii, Fusarium oxalis ... Fusarium cisporum, Fusarium reticulatum, Fusarium roseum, Fusarium sambusinum, Fusarium sarcochromium, Fusarium sulphureum, Fusarium torulosum, Fusarium trichothesioides, or Fusarium bennitum; Humicola, for example Humicola insolens or Humicola lanuginosa; or Trichoderma, for example Trichoderma harzianum, Trichoderma koningii, Trichoderma longibrachiatum, Trichoderma reesi, or Trichoderma viride.

[0048] Preferably, the composition comprises a protease or a mixture of two or more proteases, a lipase or a mixture of two or more lipases, a peroxidase or a mixture of two or more peroxidases, one or more starch degrading enzymes, such as alpha-amylase, glucoamylase, maltogenic amylase, and / or cellulase or a mixture thereof.

[0049] Generally, the properties of the enzyme selected should be compatible with the detergent selected (i.e., pH optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.) and the enzyme should be present in an effective amount.Preferably, the products of the invention contain at least 0.01 mg, preferably from about 0.05 to about 10, more preferably from about 0.1 to about 6, especially from about 0.2 to about 5 mg of additional active enzyme per gram of composition.

[0050] Protease: The composition of the present invention preferably comprises a protease. A mixture of two or more proteases can contribute to improved cleaning over a wider temperature, cycle duration, and / or substrate range. Suitable proteases include metalloproteases and serine proteases, including neutral or alkaline microbial serine proteases, such as subtilisin (EC 3.4.21.62). Suitable proteases include those of animal, vegetable or microbial origin. In one aspect, such suitable proteases may be of microbial origin. Suitable proteases include chemically or genetically modified variants of the aforementioned suitable proteases. In one aspect, suitable proteases may be serine proteases, such as alkaline microbial proteases or / and trypsin-type proteases. Examples of suitable neutral or alkaline proteases include:

[0051] Subtilisins (EC 3.4.21.62), in particular WO 2004067737, WO 2015091989, WO 2015091990, WO 2015024739, WO 2015143360, U.S. Pat. Nos. 6,312,936(B1), 5,679,630, 4,760,025, and German Patent Application Publication No. 102006022216(A1). Bacillus species described in International Publication Nos. 102006022224(A1), 2015089447, 2015089441, 2016066756, 2016066757, 2016069557, 2016069563, 2016069569, and 2016174234. from the genus Bacillus, such as B. sp., B. lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, B. pumilus, B. gibsonii, and B. akibaii, specifically those with the mutations S9R, A15T, V66A, A188P, V199I, Q239R, N255D (savinase numbering system).

[0052] Trypsin-type or chymotrypsin-type proteases such as trypsin (e.g., of porcine or bovine origin), including the Fusarium proteases described in WO 89 / 06270, and the chymotrypsin proteases from Cellulomonas described in WO 05 / 052161 and WO 05 / 052146.

[0053] Metalloproteases, in particular those from Bacillus amyloliquefaciens as described in WO 07 / 044993(A2), those from Bacillus, Brevibacillus, Thermoactinomyces, Geobacillus, Paenibacillus, Lysinibacillus or Streptomyces spp. as described in WO 2014194032, WO 2014194054 and WO 2014194117, and those from Kribella aluminosa as described in WO 2015193488. alluminosa, and those from the genera Streptomyces and Lysobacter described in WO2016075078.

[0054] A protease having at least 90% identity to the subtilase from Bacillus sp. TY145, NCIMB40339 described in WO 92 / 17577 (Novozymes A / S), including variants of the Bacillus sp. TY145 subtilase described in WO 2015024739 and WO 2016066757.

[0055] Particularly preferred proteases for the cleaning compositions of the present invention have at least 90%, preferably at least 95%, more preferably at least 98%, even more preferably at least 99%, especially 100% identity to the wild-type enzyme from Bacillus lentus and have the following positions: S9R, A15T, V68A, N76D, N87S, S99D, S99SD, S99A, S101G, S101M, S103A, V104N / I, G118V, G and / or M222S (using the BPN' numbering system and amino acid abbreviations as exemplified in WO 00 / 37627, incorporated herein by reference).

[0056] Most preferably, the protease is selected from the group of proteases that contain the following mutations (BPN numbering system) relative to either the PB92 wild type (SEQ ID NO: 2 of WO 08 / 010925) or the subtilisin 309 wild type (sequence according to the PB92 backbone but containing the naturally occurring mutation N87S): (i) G118V+S128L+P129Q+S130A (ii)S101M+G118V+S128L+P129Q+S130A (iii)N76D+N87R+G118R+S128L+P129Q+S130A+S188D+N248R (iv)N76D+N87R+G118R+S128L+P129Q+S130A+S188D+V244R (v)N76D+N87R+G118R+S128L+P129Q+S130A (vi) V68A+N87S+S101G+V104N (vii) S99AD (viii)S9R+A15T+V68A+N218D+Q245R

[0057] Suitable commercially available protease enzymes include those sold by Novozymes A / S (Denmark) under the trade names Alcalase®, Savinase®, Primase®, Durazym®, Polarzyme®, Kannase®, Liquanase®, Liquanase Ultra®, Savinase Ultra®, Ovozyme®, Neutrase®, Everlase®, Coronase®, Blaze®, Blaze Ultra® and Esperase®; those sold under the trade names Maxatase®, Maxacal®, Maxapem®, Properase®, Purafect®, Purafect Prime®, Purafect Ox®, FN3®, FN4®, Excellase®, Ultimase® and Purafect those sold by Dupont under the trade names Opticlean® and Optimase® by Solvay Enzymes; and those available from Henkel / Kemira, namely, BLAP (whose sequence is shown in FIG. 29 of U.S. Pat. No. 5,352,604 and has the mutations S99D+S101R+S103A+V104I+G159S, hereinafter referred to as BLAP), BLAP R (BLAP with S3T+V4I+V199M+V205I+L217D), BLAP X (BLAP with S3T+V4I+V205I) and BLAP F49 (BLAP with S3T+V4I+A194P+V199M+V205I+L217D); and KAP from Kao (Bacillus alkalophilus subtilisin with the mutations A230V+S256G+S259N).

[0058] Commercially available proteases selected from the group consisting of Properase®, Blaze®, Ultimase®, Everlase®, Savinase®, Excellase®, Blaze Ultra®, BLAP and BLAP variants are particularly preferred for use herein.

[0059] Preferred concentrations of protease in the products of the present invention include from about 0.05 to about 10, more preferably from about 0.5 to about 7, and especially from about 1 to about 6 mg of active protease per gram of composition.

[0060] Lipase: The composition preferably comprises a lipase. The presence of oils and / or fats can further increase the recovery of stains containing mannans and other polysaccharides. Thus, the presence of lipase in the enzyme package can further improve the removal of such stains. Suitable lipases include those of bacterial or fungal or synthetic origin. Chemically modified or genetically engineered variants of the protein are included. Examples of useful lipases include lipases from the genus Humicola (also known as Thermomyces), such as H. lanuginosa (T. lanuginosus) or H. insolens; lipases from the genus Pseudomonas, such as P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. stutzeri, P. fluorescens, Pseudomonas sp. SD705, P. wisconsinensis; lipases from B. subtilis (Dartois et al. (1993), Biochemica et Biophysica Examples of lipases include those from the genus Bacillus, such as Bacillus stearothermophilus, Bacillus pumilus, and the like.

[0061] The lipase may be a "first cycle lipase" as described in U.S. Patent No. 6,939,702 (B1) and U.S. Patent Application Publication No. 2009 / 0217464. In one aspect, the lipase is a first wash lipase, preferably a variant of wild-type lipase from Thermomyces lanuginosus, including the T231R and N233R mutations. The wild-type sequence is Swiss-Prot Accession No. Swiss-Prot O59952 (269 amino acids (amino acids 23-291) from Thermomyces lanuginosus (Humicola lanuginosa)). Preferred lipases include those sold under the trade names Lipex®, Lipolex®, and Lipoclean®.

[0062] Other suitable lipases include, for example, Liprl 139 as described in WO 2013 / 171241, TfuLip2 as described in, for example, WO 2011 / 084412 and WO 2013 / 033318, Pseudomonas stutzeri lipase as described in, for example, WO 2018228880, Microbulbifer thermotolerans lipase as described in, for example, WO 2018228881, Sulfobacillus acidocaldarius lipase as described in, for example, EP 3299457, acidocaldarius lipases, such as LIP062 lipase as described in WO2018209026, PinLip lipase as described in WO2017036901, and Absidia species lipases as described in WO2017005798.

[0063] Suitable lipases are (a) Substitution T231R (b) Substitution N233R or N233C (c) a variant of SEQ ID NO:5 comprising at least three additional substitutions selected from E1C, D27R, N33Q, G38A, F51V, G91Q, D96E, K98L, K98I, D111A, G163K, H198S, E210Q, Y220F, D254S, I255A, and P256T; Here, the positions correspond to those of SEQ ID NO:5, and 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 the variant has lipase activity.

[0064] One preferred lipase is a variant of SEQ ID NO:5 that contains the following substitutions: T231R, N233R, D27R, G38A, D96E, D111A, G163K, D254S, and P256T.

[0065] One preferred lipase is a variant of SEQ ID NO:5 that includes the following substitutions: T231R, N233R, N33Q, G91Q, E210Q, I255A.

[0066] Suitable lipases are commercially available from Novozymes, for example as Lipex Evity 100L, Lipex Evity 200L (both liquid ingredients) and Lipex Evity 105T (granules), which have a different structure to the products Lipex 100L, Lipex 100T and Lipex Evity 100T, which are outside the scope of the present invention.

[0067] Cellulase: Suitable cellulases include cellulases of bacterial or fungal origin. These include chemically modified or genetically engineered variants of proteins. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, such as the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum, as disclosed in U.S. Patent Nos. 4,435,307, 5,648,263, 5,691,178, 5,776,757, and 5,691,178.

[0068] In one aspect, preferred enzymes include endoglucanases from microorganisms exhibiting endo-beta-1,4-glucanase activity (EC 3.2.1.4), preferably selected from the group comprising: (a) a bacterial polypeptide endogenous to a member of the genus Bacillus having a sequence that is at least 90%, 94%, 97%, or even 99% identical to the amino acid sequence of SEQ ID NO:2 in U.S. Patent No. 7,141,403(B2), preferred substitutions include one or more positions corresponding to positions 292, 274, 266, 265, 255, 246, 237, 224, and 221 of the mature polypeptide of SEQ ID NO:2, wherein the variant has cellulase activity; (b) a glycosyl hydrolase having enzymatic activity on both xyloglucan and amorphous cellulose substrates, the glycosyl hydrolase being selected from GH family 5, 7, 12, 16, 44 or 74; (c) glycosyl hydrolases having a sequence that is at least 90%, 94%, 97%, and even 99% identical to the amino acid sequence of SEQ ID NO: 3 of WO 09 / 148983; (d) A variant exhibiting at least 70% identity to SEQ ID NO: 5 in WO2017106676. Preferred substitutions are at one or more positions corresponding to positions 4, 20, 23, 29, 32, 36, 44, 51, 77, 80, 87, 90, 97, 98, 99, 102, 112, 116, 135, 136, 142, 153, 154, 157, 161, 163, 192, 194, 204, 208, 210, 212, 216, 217, 221, 222, 225, 227, and 232; (e) and mixtures thereof.

[0069] Suitable endoglucanases are sold under the trade names Celluclean® and Whitezyme® (Novozymes A / S, Bagsvaerd, Denmark). Examples include Celluclean® 5000L, Celluclean® Classic 400L, Celluclean® Classic 700T, Celluclean® 4500T, Whitezyme® 1.5T, Whitezyme® 2.0L.

[0070] Other commercially available cellulases include Celluzyme®, Carezyme®, Carezyme® Premium (Novozymes A / S), Clazinase®, Puradax HA®, Revitalenz® 1000, Revitalenz® 2000 (Genencor International Inc.), KAC-500(B)® (Kao Corporation), Biotouch® FCL, Biotouch® DCL, Biotouch® DCC, Biotouch® NCD, Biotouch® FCC, Biotouch® FLX1 (AB Enzymes).

[0071] Suitable glucanases include endo-β-1,3-glucanases, preferably from EC class 3.2.1.39, preferably obtained from a microorganism of the genus Paenibacillus, Zobellia galactanivorans, Thermotoga petrophila, or Trichoderma, preferably Paenibacillus or Zobellia galactanivorans, most preferably Paenibacillus.

[0072] Amylase: Preferably, the composition of the present invention comprises an amylase. Suitable alpha-amylases include those of bacterial or fungal origin. Chemically or genetically modified variants are included. Preferred alkaline alpha-amylases are derived from Bacillus species, such as Bacillus licheniformis, Bacillus amyloliquefaciens, Bacillus stearothermophilus, Bacillus subtilis, or other Bacillus species, such as Bacillus species NCBI12289, NCBI12512, NCBI12513, DSM9375 (U.S. Pat. No. 7,153,818), DSM12368, DSMZ No. 12649, KSM AP1378 (WO 97 / 00324), KSM K36, or KSM K38 (EP 1,022,334). Preferred amylases include the following: (a) variants described in U.S. Pat. No. 5,856,164, and in WO 99 / 23211, WO 96 / 23873, WO 00 / 60060, WO 06 / 002643, and WO 2017 / 192657, in particular those at the following positions relative to the AA560 enzyme described as SEQ ID NO: 12 in WO 06 / 002643: 26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193, 202, 214, 231, 246, 256, 257, 258, 269, 270, 272, 283, 295, 296, 298, 299, 303, 304, 305, 311, 314, 315, 318, 319, 339, 345, 361, 378, 383, 419, 421, 437, 441, 444, 445, 446, 447, 450, 461, 471, 482, 484, preferably D183 * and G184 * Variants that also contain deletions. (b) variants exhibiting at least 85%, preferably 90% identity with SEQ ID NO: 4 in WO 06 / 002643, the wild-type enzyme from Bacillus sp. SP722, in particular variants in which positions 183 and 184 are deleted, as well as variants described in WO 00 / 60060, WO 2011 / 100410 and WO 2013 / 003659, in particular the following positions relative to SEQ ID NO: 4 in WO 06 / 002643, which is incorporated herein by reference: Those with one or more substitutions at positions 51, 52, 54, 109, 304, 140, 189, 134, 195, 206, 243, 260, 262, 284, 347, 439, 469, 476, and 477. (c) variants exhibiting at least 90% identity with the wild-type enzyme from Bacillus sp. 707 (SEQ ID NO: 7 in U.S. Pat. No. 6,093,562), in particular those comprising one or more of the following mutations: M202, M208, S255, R172, and / or M261. Preferably, the amylase comprises one or more of M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N and / or R172Q. Particularly preferred are those comprising the M202L or M202T mutations. Additional associated mutations / deletions based on the SP707 backbone are W48, A51, V103, V104, A113, R118, N125, V131, T132, E134, T136, E138, R142, S154, V165, R182, G182, H183, E190, D192, T193, I206, M208, D209, E212, V213, V214, N214, L217, R218, N21 Includes 9, V222, T225, T227, G229, I235, K242, Y243, S244, F245, T246, I250, S255, A256, H286, V291, T316, V317, V318, N417, T418, A419, H420, P421, I428, M429, F440, R443, N444, K445, Q448, S451, A465, N470, S472. (d) a variant described in WO 09 / 149130, preferably SEQ ID NO: 1 or SEQ ID NO: 2 in WO 09 / 149130, which shows at least 90% identity to the wild-type enzyme from Geobacillus Stearophermophilus, or a truncated version thereof. (e) a variant described in WO 10 / 115021, in particular SEQ ID NO: 2 in WO 10 / 115021, which exhibits at least 75%, or at least 85%, or at least 90%, or at least 95% identity with the alpha-amylase from Bacillus sp. TS-23. (f) A variant exhibiting at least 89% identity to SEQ ID NO: 1 in WO2016091688, in particular one containing a deletion at positions H183+G184 and further containing one or more mutations at positions 405, 421, 422, and / or 428. (g) A variant described in WO 2014099523, in particular one that exhibits at least 60% amino acid sequence identity with “PcuAmyl α-amylase” from Paenibacillus curdlanolyticus YK9 (SEQ ID NO: 3 in WO 2014099523). (h) variants described in WO2014099523, in particular "CspAmy2 amylase" from Cytophaga species (showing at least 60% amino acid sequence identity with SEQ ID NOs: 1 and 6 in WO2014164777, in particular comprising one or more of the following deletions and / or mutations based on SEQ ID NO: 1 in WO2014164777: R178 * , G179 * , T38N, N88H, N126Y, T129I, N134M, F153W, L171R, T180D, E187P, I203Y, G476K, G477E, Y303D. (i) A variant exhibiting at least 85% identity to Bacillus subtilis (SEQ ID NO: 1 in WO 2009149271). (j) A variant showing at least 90% identity to the wild-type amylase derived from Bacillus sp. KSM-K38 under accession number AB051102. (k) variants according to WO2016180748, in particular those which exhibit at least 80% identity with the mature amino acid sequence of AAI10 from Bacillus species according to SEQ ID NO: 7 in WO2016180748; those which exhibit at least 80% identity with the mature amino acid sequence of amylase from Alicyclobacillus species according to SEQ ID NO: 8 in WO2016180748, and those which exhibit at least 80% identity with the mature amino acid sequence of SEQ ID NO: 13 in WO2016180748, in particular those which exhibit at least 80% identity with the mature amino acid sequence of SEQ ID NO: 13 in WO2016180748, * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G184T, N195F, V206L, K391A, P473R, G476K. (l) Variants described in WO2018060216, in particular variants exhibiting at least 70% identity to the mature amino acid sequence of SEQ ID NO: 4 in WO2018060216, fusion molecules of Bacillus amyloliquefaciens and Bacillus licheniformis. In particular, those containing one or more substitutions at positions H1, N54, V56, K72, G109, F113, R116, T134, W140, W159, W167, Q169, Q172, L173, A174, R181, G182, D183, G184, W189, E194, N195, V206, G255, N260, F262, A265, W284, F289, S304, G305, W347, K391, Q395, W439, W469, R444, F473, G476, and G477.

[0073] A preferred amylase is a genetically engineered enzyme in which one or more of the amino acids susceptible to bleaching oxidation are replaced by amino acids that are less susceptible to oxidation. In particular, it is preferred that the methionine residue is replaced by any other amino acid. In particular, it is preferred that the methionine that is most susceptible to oxidation is replaced. Preferably, the methionine at position corresponding to 202 in SEQ ID NO: 11 is replaced. Preferably, the methionine at this position is replaced by threonine or leucine, preferably leucine.

[0074] Suitable commercially available alpha-amylases include DURAMYL®, LIQUEZYME®, TERMAMYL®, TERMAMYL ULTRA®, NATALASE®, SUPRAMYL®, STAINZYME®, STAINZYME PLUS®, FUNGAMYL®, ATLANTIC®, ACHIEVE ALPHA®, AMPLIFY® PRIME, INTENSA® and BAN® (Novozymes A / S, Bagsvaerd, Denmark), KEMZYM® AT 9000 (Biozym Biotech Trading GmbH, Wehlistrasse 27b A-1200 Wien Austria), RAPIDASE®, PURASTAR®, ENZYSIZE®, OPTISIZE HT PLUS®, POWERASE®, PREFERENZ S (registered trademark) series (including PREFERENZ S1000 (registered trademark) and PREFERENZ S2000 (registered trademark)), as well as PURASTAR OXAM (registered trademark) (DuPont., Palo Alto, California), and KAM (registered trademark) (Kao, 14-10 Nihonbashi Kayabacho, 1-chome, Chuo-ku Tokyo 103-8210, Japan).

[0075] Preferably, the composition contains at least 0.01 mg, preferably about 0.05 to about 10, more preferably about 0.1 to about 6, especially about 0.2 to about 5 mg of active amylase per gram of composition.

[0076] Peroxidase / Oxidase: Suitable peroxidase / oxidases include those of plant, bacterial, or fungal origin. Chemically modified or genetically engineered mutants of the protein are also included. Examples of useful peroxidases include peroxidases from the genus Coprinus, such as those from C. cinereus and variants thereof, as described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257.

[0077] Commercially available peroxidases include GUARDZYME® (Novozymes A / S).

[0078] Pectate lyases: Suitable pectate lyases include those sold under the trade names Pectawash®, Pectaway®, X-Pect®, (all from Novozymes A / S, Bagsvaerd, Denmark) and Preferenz® F1000 (DuPont Industrial Biosciences).

[0079] Mannanase. The composition preferably includes one or more additional mannanase enzymes. As used herein, the term "mannanase" or "galactomannanase" refers to a mannanase enzyme defined according to what is known in the art as mannan endo-1,4-beta-mannosidase, with the alternative names beta-mannanase and endo-1,4-mannanase, that catalyzes the hydrolysis of 1,4-beta-D-mannosidic linkages in mannans, galactomannans, glucomannans, and galactoglucomannans. Mannanase is classified as EC 3.2.1.78 according to enzyme nomenclature and belongs to glycosyl hydrolase families 5, 26, and 113. Many suitable mannanases belong to glycosyl hydrolase family 5. Commercially available mannanases include all those sold under the trade name Mannaway® (Novozymes A / S), such as Mannaway® 200L and Mannaway Evity 4.0T. Other commercially available mannanases include Effectenz® M1000, Mannastar® 375, Preferenz M100, and Purabrite® (all from DuPont Industrial Biosciences) and Biotouch M7 (AB Enzymes). Other suitable mannanases belong to glycosyl hydrolase family 26, such as those described in WO2018191135, WO2015040159, WO2017021515, WO2017021516, WO2017021517, and WO2019081515. Suitable mixtures of mannanases include the combination of glycosyl hydrolase family 5 mannanase and glycosyl hydrolase family 26 mannanase described in WO2019081515.

[0080] Nuclease: Preferably, the composition comprises a nuclease enzyme, such as RNase or DNase, or a mixture thereof. A nuclease enzyme is an enzyme capable of cleaving phosphodiester bonds between nucleotide subunits of nucleic acids. The nuclease enzyme herein is preferably a deoxyribonuclease or ribonuclease enzyme or a functional fragment thereof. By functional fragment or portion is meant the part of the nuclease enzyme that catalyzes the cleavage of phosphodiester bonds in the DNA backbone, and thus is the region of said nuclease protein that retains catalytic activity. It therefore includes truncated but functional versions of the enzyme and / or variants and / or derivatives and / or homologs in which functionality is maintained.

[0081] Preferably, the nuclease enzyme is a deoxyribonuclease preferably selected from any of the following classes: EC 3.1.21.x (wherein x=1, 2, 3, 4, 5, 6, 7, 8 or 9), EC 3.1.22.y (wherein y=1, 2, 4 or 5), EC 3.1.30.z (wherein z=1 or 2), EC 3.1.31.1, and mixtures thereof.

[0082] DNase: Suitable DNases include those set forth in SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, and 9 of WO 2017162836 (Novozymes) and SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 110, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, and 54, as well as mutants of Bacillus cibi DNase, including those described in WO 2018011277 (Novozymes), which are incorporated herein by reference. Preferred DNases are as claimed in EP 3476935(A).

[0083] RNases: Suitable RNases include wild-type and variants of DNases defined by SEQ ID NOs: 3, 6, 9, 12, 15, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 72 and 73 of WO2018178061 (Novozymes), which are incorporated herein by reference, and SEQ ID NOs: 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103 and 104 of WO2020074499 (Novozymes), which are incorporated herein by reference.

[0084] Hexosaminidase: The composition preferably further comprises one or more hexosaminidase enzymes. The term hexosaminidase includes "dispersant" and the abbreviation "Dsp" and refers to a polypeptide having hexosaminidase activity. Suitable enzymes are found in EC 3.2.1., which catalyze the hydrolysis of β-1,6-glycosidic bonds of N-acetyl-glucosamine polymers found in soils of microbial origin. The term "hexosaminidase" includes polypeptides having N-acetylglucosaminidase activity and β-N-acetylglucosaminidase activity. Hexosaminidase activity can be determined according to Assay II described in WO2018184873. Suitable hexosaminidases include those described in International Publication Nos. 2017186936, 2017186937, 2017186943, 2017207770, 2018184873, 2019086520, 2019086528, 2019086530, 2019086532, 2019086521, and 2019 086526, 2020002604, 2020002608, 2020007863, 2020007875, 2020008024, 2020070063, 2020070249, 2020088957, 2020088958, and 2020207944. Variants of Terribacillus saccharophilus hexosaminidase as defined by SEQ ID NO: 1 of WO 2020207944 are preferred, in particular the variants with improved thermostability disclosed therein.

[0085] Particularly preferred hexosaminidase enzymes are those having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 59, and those having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 60 herein, and mixtures thereof.

[0086] Xanthan gum degrading enzyme: The composition may contain one or more xanthan gum degrading enzymes. Enzymes suitable for degrading xanthan gum-based stains include xanthan endoglucanase, optionally in combination with xanthan lyase. As used herein, the term "xanthan endoglucanase" refers to an enzyme that exhibits endo-β-1,4-glucanase activity that can catalyze the hydrolysis of the 1,4-linked β-D-glucose polymer backbone of xanthan gum, optionally in combination with a suitable xanthan lyase enzyme. Suitable xanthan endoglucanases are described in WO 2013167581, WO 2015181299, WO 2015181292, WO 2017046232, WO 2017046260, WO 201837062, WO 201837065, WO 2019038059, and WO 2019162000. As used herein, the term "xanthan lyase" refers to an enzyme that cleaves the β-D-mannosyl-β-D-1,4-glucuronosyl bond of xanthan gum. Such enzymes belong to EC 4.2.2.12. Suitable xanthan lyases are described in WO 2015001017, WO 2018037061, WO 201837064, WO 2019038060, WO 2019162000, and WO 2019 / 38057.

[0087] Galactanase: Preferably, the composition comprises a galactanase, i.e., an extracellular polymer degrading enzyme, including an endo-beta-1,6-galactanase enzyme. The term "endo-beta-1,6-galactanase" or "polypeptide having endo-beta-1,6-galactanase activity" refers to an endo-beta-1,6-galactanase activity (EC 3.2.1.164) from glycoside hydrolase family 30 that catalyzes the hydrolytic cleavage of 1,6-3-D-galactooligosaccharides with a degree of polymerization (DP) higher than 3 and their acidic derivatives bearing a 4-O-methyl glucosyluronate or glucosyluronate group at the non-reducing end. For the purposes of this disclosure, endo-beta-1,6-galactanase activity is determined in Assay I according to the procedure described in WO2015185689. Suitable examples from classification EC 3.2.1.164 are described in WO2015185689, e.g. mature polypeptide SEQ ID NO:2.

[0088] The additional enzymes may be included in the detergent composition by adding a separate enzyme additive containing the additional enzymes or a mixed enzyme additive containing two or some or all of the additional enzymes. Such enzyme additives may be in the form of granules, liquids, or slurries, and preferably further include an enzyme stabilizer.

[0089] Preferably, the or each additional enzyme is present in an amount of at least 0.0001% to about 0.1% by weight of pure active enzyme protein, such as from about 0.0001% to about 0.01% by weight, from about 0.001% to about 0.01% by weight, or from about 0.001% to about 0.01% by weight, based on the weight of the composition.

[0090] Fabric hueing agents. The composition may include fabric hueing agents (sometimes referred to as tinting agents, bluing agents, or whitening agents / dyes). Typically, the hueing agents impart a blue or purple hue to the fabric. The hueing agents can be used either alone or in combination to create a particular hue shade and / or tint different types of fabric. This may be achieved, for example, by mixing red and green-blue dyes to produce a blue or purple shade. The hueing agent may be selected from any known chemical class of dyes, including, but not limited to, acridines, anthraquinones (including polycyclic quinones), azines, azos including premetallized azos (e.g., monoazos, diazos, trisazos, tetrakisazos, polyazos), benzodifurans and benzodifuranones, carotenoids, coumarins, cyanines, diazahemicyanines, diphenylmethanes, formazans, hemicyanines, indigoids, methanes, naphthalimides, naphthoquinones, nitro and nitroso, oxazines, phthalocyanines, pyrazoles, stilbenes, styryls, triarylmethanes, triphenylmethanes, xanthenes, and mixtures thereof. Azo dyes, particularly monoazo or bisazo dyes, triarylmethane dyes, and anthraquinone dyes are preferred.

[0091] Suitable fabric hueing agents include dyes, dye-clay conjugates, and organic and inorganic pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes classified under the Color Index (CI) classification of direct dyes, basic dyes, reactive dyes, or hydrolysis reactive dyes, solvent dyes, or disperse dyes. Examples of suitable small molecule dyes include, for example, the Color Index (Society of Dyers and Colorists). Colourists, Bradford, UK) Direct Violet dyes 9, 35, 48, 51, 66, and 99, etc. Direct Blue dyes 1, 71, 80, and 279, etc. Acid Red dyes 17, 73, 52, 88, and 150, etc. Acid Violet dyes 15, 17, 24, 43, 49, 50, and 51, etc. Acid Blue dyes 15, 17, 25, 29, 40, 45, 75, 80, 83, 90, and 1 No. 7,208,459 B2, and mixtures thereof.

[0092] Preferred are polymeric dyes, including polymers containing covalently attached (sometimes referred to as conjugated) chromogens (dye-polymer conjugates), such as polymers having chromogens copolymerized into the backbone of the polymer, and mixtures thereof, including those described in WO 2011 / 98355, WO 2011 / 47987, U.S. Patent Application Publication No. 2012 / 090102, WO 2010 / 145887, WO 2006 / 055787, and WO 2010 / 142503.

[0093] Preferred polymeric dyes include alkoxylated, preferably ethoxylated azo or anthraquinone, triarylmethane dyes. Particularly preferred are polymeric dyes selected from the group consisting of ethoxylated thiophene azo dyes, such as the fabric substantive colorants sold under the name Liquitint® (Milliken, Spartanburg, South Carolina, USA), dye-polymer conjugates formed from at least one reactive dye and a polymer selected from the group consisting of polymers comprising a moiety selected from the group consisting of hydroxyl moieties, primary amine moieties, secondary amine moieties, thiol moieties, and mixtures thereof. Suitable polymeric dyes include polymeric dyes selected from the group consisting of Liquitint® Violet CT, carboxymethylcellulose (CMC) (covalently bonded to a reactive blue, reactive violet, or reactive red dye, such as CMC conjugated with CI Reactive Blue 19 sold under the trade name AZO-CM-CELLULOSE, product code S-ACMC by Megazyme, Wicklow, Ireland), alkoxylated triphenyl-methane polymeric colorants, alkoxylated thiophene polymeric colorants, and mixtures thereof.

[0094] Preferred hueing dyes include the alkoxylated thiophene azo brighteners found in U.S. Patent Application Publication No. 2008 / 0177090, and optionally can be anionic, such as those selected from Examples 1-42 in Table 5 of WO 2011 / 011799. Other preferred dyes are disclosed in U.S. Patent No. 8,138,222.

[0095] Suitable pigments include those selected from the group consisting of Ultramarine Blue (CI Pigment Blue 29), Ultramarine Violet (CI Pigment Violet 15) and mixtures thereof. Pigments and / or dyes may also be added to add color for aesthetic reasons. Preferred are organic blue, purple, and / or green pigments.

[0096] Builders: The detergent composition may further contain builders such as builders based on carbonates, bicarbonates or silicates, which may be zeolites such as Zeolite A, Zeolite MAP (Maximum Aluminium type P). Zeolites suitable for use in laundry are preferably of the formula Na 12 (AlO2) 12 (SiO2) 12 ·27H2O, with particle sizes typically between 1-10 μm for zeolite A and 0.7-2 um for zeolite MAP. Another builder is the strongly alkaline sodium metasilicate (Na2SiO3·nH2O or Na2Si2O5·nH2O), preferably used in dishwashing. In preferred embodiments, the amount of detergent builder may be more than 5%, more than 10%, more than 20%, more than 30%, more than 40%, or more than 50%, but may also be less than 80%, less than 65%. In dishwashing detergents, the builder concentration is typically 40-65%, in particular 50-65%, or even 75-90%.

[0097] Encapsulated Agent: The composition may include an encapsulated benefit agent, comprising a core and a shell having an inner and outer surface, the shell encapsulating the core. The core may include a material selected from the group consisting of perfumes; brighteners, dyes, insect repellents, silicones, waxes, fragrances, vitamins, fabric softeners, skin care agents, and in one embodiment, paraffin; enzymes, antimicrobials, bleaches, sensates; and mixtures thereof. The shell may comprise a material selected from the group consisting of polyethylene, polyamide, polystyrene, polyisoprene, polycarbonate, polyester, polyacrylate, aminoplast (in one aspect, the aminoplast may comprise polyurea, polyurethane, and / or polyurea urethane, in one aspect, the polyurea may comprise polyoxymethylene urea and / or melamine formaldehyde), polyolefin, polysaccharide (in one aspect, the polysaccharide may comprise alginate and / or chitosan), gelatin, shellac, epoxy resin, vinyl polymer, water insoluble inorganic material, silicone, and mixtures thereof. A preferred encapsulant comprises a core that comprises a perfume. Such an encapsulant is a perfume microcapsule.

[0098] Enzyme stabilizers: The composition may include an enzyme stabilizer. Suitable enzyme stabilizers may be selected from the group consisting of: (a) inorganic salts selected from the group consisting of calcium salts, magnesium salts, and mixtures thereof; (b) carbohydrates selected from the group consisting of oligosaccharides, polysaccharides, and mixtures thereof, and sugars or sugar alcohols; (c) phenylboronic acid and derivatives thereof, such as aromatic borate esters, or phenylboronic acid derivatives, such as 4-formylphenylboronic acid, or peptide aldehydes, such as di-, tri-, or tetrapeptide aldehydes or aldehyde analogs (any form B1-B0-R, where R is H, CH3, CX3, CHX2, or CH2X (X=halogen), and B0 is a single amino acid residue (preferably an optionally substituted aliphatic or aromatic side chain); B1 consists of one or more amino acid residues (preferably 1, 2 or 3), optionally including an N-terminal protecting group], or as described in WO 09118375, WO 98 / 13459); (d) reversible protease inhibitors, such as boron-containing compounds; (e) polyols, such as propylene glycol or glycerol 1-2 propanediol; (f) calcium formate and / or sodium formate; (g) protein-type protease inhibitors, such as RASI, BASI, WASI (rice, barley and wheat bifunctional alpha-amylase / subtilisin inhibitor) or Cl2 or SSI, and (h) any combination thereof.

[0099] Structuring Agents: In one aspect, the composition may include a structuring agent selected from the group consisting of di- and triglycerides, ethylene glycol distearate, microcrystalline cellulose, cellulose-based materials, microfiber cellulose, biopolymers, xanthan gum, gellan gum, and mixtures thereof.

[0100] Polymers: The composition preferably comprises one or more polymers. Preferred examples include carboxymethylcellulose, poly(vinyl-pyrrolidone), poly(ethylene glycol), poly(vinyl alcohol), poly(vinylpyridine-N-oxide), poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic acid / acrylic acid copolymers, and lauryl methacrylate / acrylic acid copolymers, and amphiphilic polymers, and mixtures thereof.

[0101] Amphiphilic cleaning polymers: Preferably, the amphiphilic cleaning polymer has the following general structure: bis((C2H5O)(C2H4O)n)(CH3)-N + -C x H 2x -N + Compounds having the formula -(CH3)-bis((C2H5O)(C2H4O)n), where n=20-30 and x=3-8, or sulfated or sulfonated variants thereof.

[0102] The amphiphilic alkoxylated grease cleaning polymer of the present invention refers to any alkoxylated polymer that has balanced hydrophilic and hydrophobic properties to remove grease particles from fabrics and surfaces.Specific embodiments of the amphiphilic alkoxylated grease cleaning polymer of the present invention include a core structure and a plurality of alkoxylate groups attached to the core structure.These may include alkoxylated polyalkyleneimines, preferably having an inner polyethylene oxide block and an outer polypropylene oxide block.

[0103] The core structure may comprise a polyalkyleneimine structure comprising repeat units of formulae (I), (II), (III), and (IV) in condensed form:

[0104] [ka] (wherein # denotes in each case a link between a nitrogen atom and a group A of two adjacent repeating units of formula (I), (II), (III) or (IV). 1indicates half of the binding between the free binding sites of * indicates in each case half of a bond with one of the alkoxylate groups; A 1 are independently selected from linear or branched C2-C6-alkylene; the polyalkyleneimine structure consists of 1 repeat units of formula (I), x repeat units of formula (II), y repeat units of formula (III) and y+1 repeat units of formula (IV), where x and y in each instance have values ​​ranging from 0 to about 150; and the average weight average molecular weight Mw of the polyalkyleneimine core structure is a value ranging from about 60 to about 10,000 g / mol).

[0105] Alternatively, the core structure comprises a polyalkanolamine structure which is a condensation product of at least one compound selected from N-(hydroxyalkyl)amines of formula (Ia) and / or (Ib):

[0106] [ka] wherein A is independently selected from C1-C6-alkylene; R 1 , R 1* , R 2 , R 2* , R 3 , R 3* , R 4 , R 4* , R 5 , and R 5* is independently selected from hydrogen, alkyl, cycloalkyl, or aryl, where the alkyl, cycloalkyl, or aryl radicals are optionally substituted; R 6 is selected from hydrogen, alkyl, cycloalkyl, or aryl, where the alkyl, cycloalkyl, or aryl of said radicals may be optionally substituted.

[0107] The multiple alkyleneoxy groups attached to the core structure are independently selected from alkyleneoxy units of formula (V):

[0108] [ka] During the ceremony * represents in each case half of a bond to a nitrogen atom of a repeating unit of formula (I), (II) or (IV); A 2 is, in each occurrence, independently selected from 1,2-propylene, 1,2-butylene, and 1,2-isobutylene; A 3 is 1,2-propylene; R, in each occurrence, is independently selected from hydrogen and C1-C4 alkyl; m has an average value ranging from 0 to about 2; n has an average value ranging from about 20 to about 50; and p has an average value ranging from about 10 to about 50.

[0109] Carboxylate polymer: The composition may preferably include one or more carboxylate polymers, such as maleate / acrylate random copolymers or polyacrylate homopolymers. In one embodiment, the carboxylate polymer is a polyacrylate homopolymer having a molecular weight of 4,000 Da to 9,000 Da or 6,000 Da to 9,000 Da.

[0110] Soil Release Polymers: The composition preferably also includes one or more soil release polymers having a structure defined by one of the following structures (I), (II) or (III): (I)-[(OCHR 1 -CHR 2 ) a -O-OC-Ar-CO-] d (II)-[(OCHR 3 -CHR 4 ) b -O-OC-sAr-CO-] e (III)-[(OCHR 5 -CHR 6 ) c -OR 7 ] f During the ceremony, a, b and c are each 1 to 200; d, e and f are each 1 to 50; Ar is 1,4-substituted phenylene; sAr is a 1,3-substituted phenylene substituted at the 5-position with SO3Me; Me is Li, K, Mg / 2, Ca / 2, Al / 3, ammonium, mono-, di-, tri-, or tetra-alkylammonium (alkyl groups are C1-C 18 Alkyl or C2-C 10 hydroxyalkyl), or mixtures thereof; R 1 , R 2 , R 3 , R 4 , R 5 , and R 6 are independently H or C1-C 18 n- or iso-alkyl; R 7 is linear or branched C1-C 18 Alkyl, or linear or branched C2-C 30 alkenyl, or a cycloalkyl group having 5 to 9 carbon atoms, or C8 to C 30 Aryl group or C6-C 30 It is an arylalkyl group.

[0111] Suitable soil release polymers are polyester soil release polymers such as Repel-o-tex polymers including Repel-o-tex SF, SF-2 and SRP6 supplied by Rhodia. Other suitable soil release polymers include Texcare polymers including Texcare SRA100, SRA300, SRN100, SRN170, SRN240, SRN300 and SRN325 supplied by Clariant. Other suitable soil release polymers are Marloquest polymers such as Marloquest SL supplied by Sasol.

[0112] Cellulosic polymer: The composition may include one or more cellulosic polymers, preferably including those selected from alkyl cellulose, alkyl alkoxy alkyl cellulose, carboxy alkyl cellulose, alkyl carboxy alkyl cellulose. In one embodiment, the cellulosic polymer is selected from the group including carboxymethyl cellulose, methyl cellulose, methyl hydroxyethyl cellulose, methyl carboxymethyl cellulose, and mixtures thereof. In one embodiment, the carboxymethyl cellulose has a degree of carboxymethyl substitution of 0.5 to 0.9 and a molecular weight of 100,000 Da to 300,000 Da.

[0113] Bleaching system: The composition may contain a bleaching system that includes a H2O2 source, such as a perborate or percarbonate, which may be combined with a peracid-forming bleach activator, such as tetraacetylethylenediamine or nonanoyloxybenzenesulfonate. Alternatively, the bleaching system may include peroxyacids, such as amide, imide, or sulfone types. Generally, when a bleaching agent is used, the compositions of the present invention may include from about 0.1% to about 30%, or even from about 0.1% to about 25% of the bleaching agent, by weight of the subject cleaning composition.

[0114] Chelating Agents: The compositions preferably include a chelating agent, preferably in an amount of from 0.005% to about 15%, or even from about 3.0% to about 10% chelating agent by weight of the composition. Suitable chelating agents include copper, iron, and / or manganese chelating agents, and mixtures thereof. Preferred chelating agents (complexing agents) include DTPA (diethylenetriaminepentaacetic acid), HEDP (hydroxyethanediphosphonic acid), DTPMP (diethylenetriaminepenta(methylenephosphonic acid)), 1,2-dihydroxybenzene-3,5-disulfonic acid disodium salt hydrate, ethylenediamine, diethylenetriamine, ethylenediaminedisuccinic acid (EDDS), N-hydroxyethylethylenediaminetriacetic acid (HEDTA), triethylenetetraaminehexaacetic acid (TTHA), N-hydroxyethyliminodiacetic acid (HEIDA), dihydroxyethylglycine (DHEG), ethylenediaminetetrapropionic acid (EDTP), methyl-glycine-diacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), iminodisuccinic acid (IDS), carboxymethylinulin, and salts, derivatives and mixtures thereof. Preferred chelating agents are selected from the group consisting of methyl-glycine-diacetic acid (MGDA), its salts and derivatives, glutamic acid-N,N-diacetic acid (GLDA), its salts and derivatives, iminodisuccinic acid (IDS), its salts and derivatives, carboxymethylinulin, its salts and derivatives, and mixtures thereof. MGDA and its salts are particularly preferred, especially including the trisodium salt of MGDA.

[0115] The compositions may also contain other conventional detergent ingredients such as, for example, fabric conditioners including clays, suds boosters, suds suppressors, corrosion inhibitors, soil settling agents, soil redeposition inhibitors, dyes, bactericides, optical brighteners, hydrotropes, anti-fog agents, organic solvents such as ethanol, or fragrances.

[0116] How to use The present invention also provides a method for treating fabrics comprising, in a contacting step, contacting the fabric with an aqueous wash liquor comprising an alginate lyase enzyme as described above, preferably in an amount of 0.01 ppm to 10 ppm, preferably 0.1 ppm to 1 ppm, a booster enzyme as described above, preferably in an amount of 0.01 ppm to 10 ppm, preferably 0.1 ppm to 1 ppm, and preferably an additional anionic surfactant, preferably in an amount of 0.05 to 50 g / l, more preferably 0.2 g / l to 5 g / l or 0.5 g / l to 3 g / l.

[0117] The aqueous wash solution may be formed by adding the above-described composition to water, for example in a washing machine or hand washing process. Alternatively, the aqueous wash solution may be formed by adding the alginate lyase enzyme, booster enzyme, and optional cleaning adjuncts as separate components to water to form the wash solution. The fabric may then optionally be washed and / or rinsed and / or dried.

[0118] The alginate lyase enzyme, booster enzyme, and any additional enzymes may be present in the wash liquor in an amount equivalent to 0.001 to 100 mg of active enzyme protein per liter of wash liquor, preferably 0.005 to 5 mg of active enzyme protein per liter of wash liquor, more preferably 0.01 to 1 mg of enzyme protein per liter of wash liquor, and especially 0.1 to 1 mg of enzyme protein per liter of wash liquor.

[0119] It may be preferred to use mechanical agitation in the contacting step or a subsequent step to facilitate cleaning and removal of the decomposed soil by-products from the fabric. The pH of the wash liquor is preferably about 7 or about 8 to about 10.5. The composition can typically be used at a concentration of about 500 ppm to about 15,000 ppm in solution to form the wash liquor. The wash liquor preferably has a temperature of about 5° C. to about 40° C., or preferably 10 to 35° C. or 30° C. or 25° C. The water to fabric ratio is typically about 1:1 to about 30:1.

[0120] Test Method Test method 1 Enzyme activity towards β-D-mannuronic acid block (poly M activity) and α-L-guluronic acid block (poly G activity) Alginate lyase activity was measured using Mannuronic Block Oligosaccharide DP20-DP35 (product code: ALG601) and Guluronate oligosaccharide DP2-DP45 (product code: ALG610) manufactured by Elicityl France as substrates. Mannuronic Block Oligosaccharide DP20-DP35 was used to measure poly M activity, and Guluronate oligosaccharide DP2-DP45 was used to measure poly G activity.

[0121] A 2.5% solution of each substrate was suspended in Tris buffer, pH 8.3, and incubated with 3 ppm of each alginate lyase of interest in a 96-well plate for 60 min at 25°C.

[0122] The activity for each substrate is given as the delta absorbance at 235 nm in a spectrophotometer relative to the enzyme-free sample when the enzyme is contacted with each substrate. These values ​​are then used to evaluate the activity of each enzyme for β-D-mannuronic acid blocks (polyM) and / or α-L-guluronic acid blocks (polyG). An enzyme with activity for poly(beta-D-mannuronate) (polyM activity) preferably provides a delta absorbance relative to the enzyme-free of at least 0.1 absorbance units, more preferably at least 0.15 absorbance units, more preferably at least 0.2 absorbance units. An enzyme with activity for poly(alpha-L-guluronate) (polyG activity) preferably provides a delta absorbance relative to the enzyme-free of at least 0.3 absorbance units, preferably at least 0.4 or even 0.5 or 0.6 absorbance units.

[0123] Test method 2 Measurement of activity against beta-1,3-glucan and beta-1,3(4)-glucan The activity towards beta-1,3-glucan and beta-1,3(4)-glucan was measured using the red variant of the Discovery kit supplied by GlycoSpot A / S (Soborg, Denmark). This kit allows the simultaneous assay of a given enzyme across 16 different activities. The assay protocol is given below. A given enzyme is considered to have significant activity towards both beta-1,3-glucan and beta-1,3(4)-glucan if it shows more than 0.3 absorbance units towards curdlan (CPH0009) and beta-glucan from barley (CPH0003). 1. Add 200 μl of Activation Solution to each well of a 96-well plate. 2. Incubate for 10 minutes at room temperature without agitation. 3. Remove remaining solution by centrifugation (2700 x g for 10 minutes or vacuum). 4. Wash twice with 100 μl of water to completely remove the stabilizer. 5. Add samples and controls to each well of a 96-well plate. The control is 150 μl of 1 M Tris(hydroxymethyl)aminomethane hydrochloride (Tris-HCL) buffer (pH 8). The sample is 1 mg of active enzyme protein dissolved in 150 μl of the same Tris-HCL buffer. 6. Place the "product plate" underneath the substrate plate. 7. Incubate the reaction at 30°C for 30 hours. 8. The reaction products are transferred to the product plate by centrifugation (2700 x g for 10 minutes or vacuum). 9. Ensure that the volumes in each well are equal. 10. Detect absorbance (517 nm).

[0124] Detergent Example Examples 1-6. Granular laundry detergent compositions designed for hand washing or top loading washing machines.

[0125] [Table 1]

[0126] Examples 7-13. Granular laundry detergent compositions designed for use in front-loading automatic washing machines.

[0127] [Table 2] * DNase is given as mg of active enzyme per 100 g of detergent.

[0128] Examples 14 to 21. Heavy-duty liquid laundry detergent compositions

[0129] [Table 3-1]

[0130] [Table 3-2]

[0131] Examples 22-28. Unit dose laundry detergent compositions. Such unit dose formulations may contain one or more compartments.

[0132] [Table 4]

[0133] Example 29. Multicompartment unit dose composition Multi-compartment unit dose laundry detergent formulations of the present invention are provided below. In these examples, the unit doses have three compartments, but similar compositions can be made with two, four, or five compartments. The film used to encapsulate the compartments is polyvinyl alcohol.

[0134] [Table 5]

[0135] [Table 6]

[0136] Ingredients and notes for compositions of Examples 1 to 29 Linear alkylbenzene sulfonates with an average aliphatic carbon chain length of C11 to C18 C12-18 Dimethylhydroxyethylammonium Chloride AE3S is a C12-15 alkyl ethoxy (3) sulfate. AE7 is a C12-15 alcohol ethoxylate with an average degree of ethoxylation of 7. AE9 is a C12-16 alcohol ethoxylate with an average degree of ethoxylation of 9. HSAS is a mid-chain branched primary alkyl sulfate having a carbon chain length of about 16-17 as disclosed in US Pat. Nos. 6,020,303 and 6,060,443. Polyacrylate MW4500 is supplied by BASF. The carboxymethylcellulose is Finnfix® V supplied by CP Kelco (Arnhem, Netherlands). CHEC is a cationically modified hydroxyethyl cellulose polymer. An example of a phosphonate chelating agent is diethylenetetraaminepentaacetic acid (DTPA) hydroxyethane diphosphonate (HEDP). Savinase®, Natalase®, Stainzyme®, Lipex®, Celluclean™, Mannaway®, and Whitezyme® are all products of Novozymes (Bagsvaerd, Denmark). Purafect® and Purafect Prime® are products of Genencor International (Palo Alto, California, USA). Optical Brightener 1 is Tinopal® AMS, Optical Brightener 2 is Tinopal® CBS-X, Direct Violet 9 is Pergasol® Violet BN-Z, and NOBS is sodium nonanoyloxybenzene sulfonate. TAED is tetraacetylethylenediamine. S-ACMC is carboxymethylcellulose conjugated with CI Reactive Blue 19, trade name AZO-CM-CELLULOSE. The soil release agent is Repel-o-tex® PF. The acrylic acid / maleic acid copolymer has a molecular weight of 70,000 and an acrylate:maleate ratio of 70:30; EDDS is the sodium salt of ethylenediamine-N,N'-disuccinic acid, (S,S) isomer, suds suppressor aggregate supplied by Dow Corning (Midland, Michigan, USA). HSAS is a mid-chain branched alkyl sulfate. Liquitint® Violet CT is a polymeric hue pigment supplied by Milliken, Spartanburg, South Carolina, USA. The polyethoxylated azothiophene dye is Violet DD™ polymeric hue dye supplied by Milliken, Spartanburg, South Carolina, USA. 1 Random graft copolymers are polyvinyl acetate grafted polyethylene oxide copolymers having a polyethylene oxide backbone and multiple polyvinyl acetate side chains. The molecular weight of the polyethylene oxide backbone is about 6000, the weight ratio of polyethylene oxide to polyvinyl acetate is about 40-60, and there is not more than one grafting point per 50 ethylene oxide units. 2 Polyethylenimine (MW=600) with 20 ethoxylate groups per -NH. 3 The amphiphilic alkoxylated polymer is a polyethyleneimine (MW600) prepared from a polymer derivatized to contain 24 ethoxylate groups per --NH and 16 propoxylate groups per --NH. 4 Amylase is given as mg of active enzyme per 100 g of detergent. 5 DNase as described herein (in all of these examples given as mg active enzyme per 100 g detergent). DNase may contain trace amounts of superoxide dismutase impurity. 6 Alginate lyases as described herein (in all examples given as mg active enzyme per 100 g detergent) 7 Hexosaminidases as described herein (in all examples given as mg active enzyme per 100 g detergent) 8 Pel-ase as described herein (in all examples given as mg active enzyme per 100 g detergent) 9 Psl-ase as described herein (in all examples given as mg active enzyme per 100 g detergent) 10 Endo-beta-1,3(4)-glucanase as described herein (in all examples given as mg active enzyme per 100 g detergent). a Proxel GXL, 1,2-benzisothiazolin-3-one, 20% in dipropylene glycol in water, supplied by Lonza. bN,N-bis(hydroxyethyl)-N,N-dimethylammonium chloride fatty acid esters. The iodine value of the parent fatty acids of this material is 18-22. The material obtained from Evonik contains impurities in the form of free fatty acids, monoester forms of N,N-bis(hydroxyethyl)-N,N-dimethylammonium chloride fatty acid esters, and fatty acid esters of N,N-bis(hydroxyethyl)-N-methylamine. c MP10®, supplied by Dow Corning, 8% active d Expressed as 100% encapsulated perfume oil as described in U.S. Pat. No. 8,765,659. e Rheovis® CDE, a cationic polymeric thickener supplied by BASF f N,N-dimethyloctaneamide and N,N-dimethyldecanamide in a weight ratio of about 55:45, Steposol® M-8-10 available from Stepan Company

[0137] Dimensions and values ​​disclosed herein should not be understood as being strictly limited to the exact numerical values ​​recited. Instead, 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."

Claims

1. 1. A detergent composition, preferably a laundry detergent composition, comprising: (a) 0.00005 to 5% by weight of an alginate lyase enzyme (active enzyme protein); and (b) 0.00005% to 5% by weight of an enzyme (active enzyme protein) of a booster enzyme selected from one or more of: (i) a Pel-ase enzyme; (ii) a Psl-ase enzyme; (iii) an endo-β-1,3(4)-glucanase enzyme; and (iv) mixtures thereof.

2. 2. A detergent composition according to claim 1, wherein the alginate lyase enzyme is of microbial origin, preferably of bacterial or algal origin, most preferably of bacterial origin.

3. 3. A detergent composition according to claim 1 or 2, wherein the alginate lyase enzyme is obtained from Flavobacterium sp., Sphingomonas sp., Zobellia galactanivorans, preferably Flavobacterium sp.

4. The alginate lyase enzyme may be an alginate lyase having at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to one or more of SEQ ID NO:1, at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to one or more of SEQ ID NO:2, alginate lyases having at least 99%, or 100% sequence identity to SEQ ID NO:3, at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:4, at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or an alginate lyase having at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:5; an alginate lyase having at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:6; 6%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:7, alginate lyases having at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:7, and mixtures thereof, preferably wherein the alginate lyase enzyme is selected from:

4. The detergent composition according to any one of claims 1 to 3, comprising an alginate lyase selected from an alginate lyase having at least 60% sequence identity to one or more of SEQ ID NO:5, SEQ ID NO:6, and SEQ ID NO:7, or mixtures thereof, most preferably, the alginate lyase enzyme comprises an alginate lyase selected from an alginate lyase having at least 60% sequence identity to one or more of SEQ ID NO:6, and SEQ ID NO:7, and mixtures thereof.

5. 5. A detergent composition according to any one of claims 1 to 4, further comprising a surfactant, preferably said surfactant being present in an amount such that the weight ratio of surfactant to active alginate lyase enzyme protein is at least 500:1, preferably at least 1000:

1.

6. 6. The laundry detergent composition of any one of claims 1 to 5, wherein the alginate lyase enzyme provides activity against poly(beta-D-mannuronate) (poly M activity) and activity against poly(alpha-L-guluronate) (poly G activity).

7. 7. A detergent composition according to any one of claims 1 to 6, further comprising an enzyme selected from a nuclease enzyme, a hexosaminidase enzyme, an endo-β-1,3-glucanase enzyme, and mixtures thereof, wherein the or each enzyme is present in an amount of from 0.00005 to 5% by weight of active enzyme protein.

8. A detergent composition according to any preceding claim, wherein the composition further comprises a non-ionic surfactant, preferably in an amount of from 1 to 30% by weight of the composition.

9. 9. A detergent composition according to any one of the preceding claims, wherein the composition further comprises a surfactant, the surfactant comprising an anionic surfactant and a non-ionic surfactant, preferably in a weight ratio of anionic surfactant to non-ionic surfactant of from 30:1 to 1:2, preferably from 20:1 to 2:3, or up to 1:

1.

10. 10. The detergent composition of claim 1, wherein the booster enzymes comprise: (i) Pel-ase and Psl-ase enzymes and, optionally, endo-β-1,3(4)-glucanase enzymes; (ii) Pel-ase and endo-β-1,3(4)-glucanase enzymes and, optionally, Psl-ase; or (iii) endo-β-1,3(4)-glucanase and Psl-ase enzymes and, optionally, Pel-ase enzyme.

11. A detergent composition according to any one of claims 1 to 10 comprising an additional enzyme, preferably an enzyme selected from amylases, nucleases, hexosaminidases, mannanases, xanthan lyases, xanthanases and mixtures thereof.

12. 1. A method of treating a fabric, comprising contacting the fabric with an aqueous wash liquor comprising: (a) an alginate lyase enzyme; and 0.00005% to 5% by weight of (b) an enzyme (active enzyme protein) of a booster enzyme selected from one or more of: (i) a Pel-ase enzyme; (ii) a Psl-ase enzyme; (iii) an endo-β-1,3(4)-glucanase enzyme; and (iv) mixtures thereof; and (iii) optionally a cleaning adjunct.

13. 13. Use of a composition or method according to any one of claims 1 to 12 for improving the whiteness of fabrics, and / or for improved stain removal from fabrics, and / or for removal of malodours from fabrics, and / or for cleaning collars and / or cuffs, and / or for anti-wrinkle effect of fabrics, and / or for improved drying of fabrics.

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