Cleaning compositions containing alginate lyase

Abstract

The present invention provides laundry detergent compositions comprising an alginate lyase enzyme and an anionic surfactant. The present disclosure also provides methods of treating a fabric by contacting the fabric with an aqueous wash liquor having a detergent composition therein. The compositions and methods are useful, inter alia, for improving whiteness of the fabric, for improving soil removal effect in the fabric, for malodor removal from the fabric, for anti-wrinkle benefit, anti-redeposition benefit, and / or for improving drying effect of the fabric.

Description

[0001] Reference to Sequence Listing

[0002] This application contains a Sequence Listing in computer readable form. The computer readable form is incorporated herein by reference. TECHNICAL FIELD

[0003] The present invention relates to laundry detergent compositions and cleaning methods comprising certain alginate lyases. One particular problem can be the build-up of soils over time. This is problematic for both colored and white fabrics, but can be especially pronounced on white or light colored fabrics, for example around the collar and cuffs where incomplete cleaning occurs. This can also be problematic as it can lead to malodors. The compositions and methods of the present invention are suitable for use in both hand washing and automatic laundry washing compositions. The present invention also relates to methods of washing and methods of making laundry detergent compositions. BACKGROUND

[0004] In laundry cleaning applications, whiteness reduction over time and soil or stain removal are ongoing problems. There are many cleaning technologies that aim to mitigate such problems, however, providing improved efficacy, especially in an environmentally friendly manner, has been a challenge. In automatic washing machines, these problems are complicated by the increasing use of low wash temperatures (e.g. cold water) and shorter wash cycles, which decrease the stain / soil removal efficacy of detergent compositions and exacerbate the problem of soil redeposition onto fabric surfaces during the wash process and whiteness loss over multiple washes.

[0005] It is therefore an object of the present invention to provide a laundry detergent composition that can be used in a wash process even at low temperatures and short wash times, which will counteract whiteness reduction and / or remove complex soils, for example enabling removal of dingy soils, deep cleaning, removal of yellowing, especially cleaning of collars and cuffs and / or improve whiteness / counteract whiteness loss, and which can even be usable at low temperatures and short wash times. SUMMARY

[0006] The present invention provides a laundry detergent composition comprising 0.00005 to 5 wt% alginate lyase (active enzyme protein) and 1 wt% to 60 wt% anionic surfactant, wherein the alginate lyase is from polysaccharide lyase family 7.

[0007] The present invention also provides a method of treating a fabric, the method comprising contacting a fabric with an aqueous wash liquor, the aqueous wash liquor comprising an alginate lyase; and an anionic surfactant, wherein the alginate lyase is from polysaccharide lyase family 7.

[0008] Preferably, the aqueous wash liquor comprises 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.

[0009] Preferably, the fabric is contacted with the aqueous wash liquor at a temperature of 60°C or lower, or more preferably at 40°C or lower or 35°C or lower, most preferably at 30°C or lower or even 25°C or lower; and (iii) rinsing the surface. The compositions and methods herein are useful for treating any synthetic or natural surface, including cotton, wool, silk, polyester, nylon, spandex or blended fabrics, such as polycotton, among others.

[0010] The present application also relates to the use of the compositions or methods as described above for improving whiteness or counteracting whiteness loss of a fabric; improving soil removal of a fabric; removing dingy soils; deep cleaning; removing or reducing yellowing; cleaning collars and / or cuffs; reducing or removing malodor from a fabric; anti-wrinkle benefit on a fabric; improving drying of a fabric; anti-soil redeposition benefit. DETAILED DESCRIPTION

[0011] Definitions

[0012] Parent or parent alginate lyase: The term "parent" or "parent alginate lyase" refers to an alginate lyase that is altered to produce an enzyme variant. The parent can be a naturally occurring (wild-type) polypeptide or a variant thereof. For example, the parent can be any one of SEQ ID NOs: 1, 2, 3, 4, 5, 6, or 7 listed herein.

[0013] Sequence identity: The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter "sequence identity". For the purpose of the present application, 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 the version 3.0.0 or later. The optional parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The Needle output is labeled "longest identity" (obtained using the -nobrief option) is used as the percent identity, and is calculated as follows:

[0014] (Same residues x 100) / (Sequence length - Total number of gaps in sequence)

[0015] Alternatively, the parameters used can be a gap opening penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of the NCBI NUC4.4) substitution matrix. The Needle output labeled "Longest Identity" (obtained using the -nobrief option) is used as percent identity, and is calculated as follows:

[0016] (Same deoxyribonucleotides x 100) / (Sequence length - Total number of gaps in sequence)

[0017] Variant: The term "variant" refers to a polypeptide having alginate lyase 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 alginate lyase. A substitution refers to the replacement of an amino acid occupying a position by another, 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 an amino acid occupying a position.

[0018] Wild-type enzyme: The term "wild-type" alginate lyase refers to an alginate lyase expressed by a naturally-occurring microorganism, such as a bacterium, an alga, a yeast, or a filamentous fungus present in nature.

[0019] Alginate lyase

[0020] Alginate lyases include alginate lyases from the polysaccharide lyase family 7.

[0021] The alginate lyase is preferably of microbial origin, preferably bacterial or algal (e.g., from brown seaweed (Phaeophyceae), such as Ascomycetes, Ulvales, and Megacarpales), most preferably bacterial. The alginate lyase can be obtained from the genus Aeromonas, Azospirillum, Bacillus, Flavobacterium, Klebsiella, Pseudomonas, Sphingomonas, Vibrio, Xanthobacter halogenerans, most preferably Flavobacterium.

[0022] Preferably, the alginate lyase comprises an alginate lyase selected from the group consisting of 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 with 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 with 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 with SEQ ID NO: 3; 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 with 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 with SEQ ID NO: 5; 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 with 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 with SEQ ID NO: 7; 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 with SEQ ID NO: 7; or mixtures thereof. Thus, preferred alginate lyases include alginate lyases corresponding to the wild type of any of the SEQ ID NOs: 1, 2, 3, 4, 5, 6 or 7 or variants of the wild type which are preferred. Especially preferred are SEQ ID NO 6 and SEQ ID NO 7 and variants thereof.

[0023] When the alginate lyase is a variant of a parent amino acid sequence, the parent alginate lyase having alginate lyase activity 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%, for example 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 the polypeptide of one or more of SEQ ID NOs: 1, 2, 3, 4, 5, 6, or 7. It can be preferred that the variant amino acid sequence differs from the parent alginate lyase by no more than fifteen, or no more than ten amino acids, or differs from the polypeptide of one or more of SEQ ID NOs: 1, 2, 3, 4, 5, 6, or 7 by no more than five, or four or three or two or one amino acids.

[0024] When the alginate lyase is a variant of a parent amino acid sequence, the parent can be derived from a microorganism of any genus. For the purposes of the present invention, the term "derived from" in relation to a given source will mean that the parent alginate lyase is encoded by a polynucleotide from that source or from a cell into which a polynucleotide from that source has been inserted. In one aspect, the parent is secreted outside the cell. The variant can be prepared using any mutagenesis process known in the art, for example site-directed mutagenesis, synthetic gene construction, semi-synthetic gene construction, random mutagenesis, shuffling, and the like.

[0025] and an anionic surfactant, preferably the alginate lyase has poly(β-D-mannuronic acid) activity (polyM activity) and poly(α-L-guluronic acid) activity (polyG activity). The alginate lyase can comprise a single alginate lyase to provide both polyM activity and polyG activity, or can comprise two or more alginate lyases, the combination of which provides polyM activity and polyG activity. Preferably, the alginate lyase comprises an enzyme having both polyM activity and polyG activity. Preferably, the polyM activity as defined in the test section herein is at least 0.1 absorbance units, preferably at least 0.15 absorbance units, and most preferably at least 2 absorbance units. Preferably, the polyG activity as defined 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 polyM activity and polyG activity can be measured according to the tests listed below. The alginate lyase can be incorporated into the cleaning compositions and methods of the present invention in the form of substantially pure enzyme. Alternatively, especially when the enzyme is a variant of a wild-type enzyme, the variant is not recovered, but rather the host cell expressing the enzyme is used as the source of the alginate lyase.

[0026] The alginate lyase can be in the form of a liquid or dry composition. For example, the composition can be in the form of a granule or a microparticle. The alginate lyase can be stabilized by encapsulation according to methods known in the art.

[0027] The alginate lyase is preferably present in the composition in an amount of 0.00005 to 5 wt% active enzyme protein, preferably 0.0001 to 2 wt% active protein or 0.0005 or 0.001 to 1 wt% active protein, or to 0.5 or to 0.1 or to 0.05 wt% active enzyme protein.

[0028] Anionic surfactant

[0029] The present inventors have found that this enzyme provides good soil disintegrating ability, however the removal effect of the substrate and the disintegration products of the soil comprising these substrates is improved by the presence of an anionic surfactant. Thus, the laundry detergent composition comprises 1 to 60 wt% of an anionic surfactant. Preferably, the weight ratio of anionic surfactant to active alginate lyase 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.

[0030] Preferred anionic surfactants are sulfonate and sulfate surfactants, preferably alkyl benzene sulfonate and / or (optionally alkoxylated) alkyl sulfate. Especially preferred anionic surfactants include linear alkyl benzene sulfonate (LAS). Preferred alkyl sulfates include alkyl ether sulfates, especially C-9-15 alcohol ether sulfates (especially those with an average degree of ethoxylation of 0.5 to 7, preferably 1 to 5), C8-C16 ester sulfates, and C10-C14 ester sulfates (such as monododecyl ester sulfates). In preferred compositions, the anionic surfactant includes alkyl benzene sulfonate and optionally in addition ethoxylated alkyl sulfate, preferably with a degree of ethoxylation of 0 to 7, more preferably 0.5 to 3. Isomers of LAS, branched alkyl benzene sulfonate (BABS), phenylalkane sulfonate, alpha-olefin sulfonate (AOS), polyolefin sulfonate, monoolefin sulfonate, alkane-2,3-diyl bis(sulfate), hydroxyalkyl sulfonate, and disulfonate, alkyl sulfate (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfate (FAS), primary alcohol sulfate (PAS), alcohol ether sulfate (AES or AEOS or FES, also known as alcohol ethoxysulfate or fatty alcohol ether sulfate), secondary alkyl sulfonate (SAS), paraffin sulfonate (PS), ester sulfonate, sulfonated fatty acid glycerol ester, alpha-sulfofatty acid methyl ester (alpha-SFMe or SES) (including methyl ester sulfonate (MES)), alkyl or alkenyl succinate, dodecyl / tetradecyl succinate (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfosuccinic acid or salts of fatty acids (soaps), and combinations thereof are also suitable anionic surfactants.

[0031] The anionic surfactant is preferably added to the detergent composition in the form of a salt. The preferred cation is an alkali metal ion such as sodium and potassium. However, the salt form of the anionic surfactant can be formed in situ by neutralizing the acid form of the surfactant using a base such as sodium hydroxide or an amine such as mono-, di-, or triethanolamine. The composition preferably comprises from 1 wt% to 60 wt%, or from 1 wt% to 50 wt%, or from 2 wt% or 5 wt% to 40 wt% of the composition of anionic surfactant. The surfactant preferably comprises a surfactant system comprising anionic surfactant and in addition, a mixture of one or more additional surfactants, which can be nonionic (including semi-polar) and / or cationic and / or zwitterionic and / or amphoteric and / or gemini and / or semi-polar nonionic and / or mixtures thereof.

[0032] The present application also provides a cleaning composition comprising: 0.00005 wt% to 5 wt% (active enzyme protein) of an alginate lyase; and a surfactant, wherein the surfactant comprises an anionic surfactant and a non-ionic surfactant, preferably having a weight ratio of the anionic surfactant to the non-ionic surfactant of 30: 1 to 1 :2, preferably 20: 1 to 2:3 or to 1 : 1.

[0033] Suitable non-ionic surfactants include alcohol ethoxylates (AE), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters such as ethoxylated and / or propoxylated fatty acid alkyl esters, alkyl phenol ethoxylates (APE), nonyl phenol ethoxylates (NPE), alkyl polyglycosides (APG), alkoxylated amines, fatty acid mono-ethanolamides (FAM), fatty acid di-ethanolamides (FADA), ethoxylated fatty acid mono-ethanolamides (EFAM), propoxylated fatty acid mono-ethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof. Especially preferred are alcohol ethoxylates, which preferably have a C9-18 or preferably C12-15 alkyl chain, and preferably have an average degree of ethoxylation of 3 to 9, more preferably 3 to 7. Commercially available non-ionic surfactant cleaning includes Plurafac TM , lutensol TM , and pluronic TM , Dehypon TM series from Cognis, and Cognis and genapol TM series from Clariant.

[0034] The detergent composition preferably comprises 0.5 wt% to about 40 wt% of non-ionic surfactant, preferably 1 wt% to 30 wt% of non-ionic surfactant of the composition.

[0035] Cleaning composition

[0036] The detergent composition of the present application is a laundry detergent. The composition can be in the form of a composition for use in the main wash step, or as a pre-treatment or add-rinse cleaning composition for consumer or institutional use.

[0037] The composition comprises optional cleaning adjuncts. Typically, cleaning adjuncts will be present in the composition in an amount of from 1 wt% to 98.9 wt%, more typically from 5 wt% to 90 wt% of cleaning adjuncts. Suitable cleaning adjuncts include: additional surfactants, builders, bleach ingredients, colorants, chelants, dye transfer agents, deposition aids, dispersants, additional enzymes and enzyme stabilizers, catalytic materials, optional brighteners, photoactivators, fluorescers, fabric hueing agents (hueing dyes), fabric conditioners, pre-formed peracids, polymeric dispersing agents, clay soil removal / anti-redeposition agents, filler salts, hydrotropes, whitening agents, suds suppressors, structure elasticizing agents, fabric softeners, preservatives, antioxidants, anti-shrinkage agents, antibacterial agents, fungicides, anti-tarnishing agents, anti- yellowing agents, alkalinity sources, solubilizing agents, carriers, processing aids, pigments, dyes, perfumes and pH control agents, encapsulates, polymers, and mixtures thereof. For example, these can include: bleach ingredients such as bleach activators; bleach boosters such as imine bleach boosters; bleach catalysts; hydrogen peroxide; sources of hydrogen peroxide such as percarbonate and / or perborate, particularly percarbonate coated with a material such as carbonate and / or sulfate, silicate, borosilicate, and any mixture thereof; preformed peracid, including preformed peracid in encapsulated form; transition metal catalysts; suds suppressors or suds suppression systems, such as silicone-based suds suppressors and / or fatty acid based suds suppressors; fabric softeners such as clays, silicones 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, for example oligomers produced by condensation of imidazole and epichlorohydrin; soil dispersants and soil anti-redeposition aids, for example alkoxylated polyamines and ethoxylated ethyleneimine polymers; anti-redeposition components such as polyesters; carboxylate polymers such as maleic polymers or copolymers of maleic and acrylic acid; perfumes such as perfume microcapsules, starch encapsulated accords, perfume sprays; suds circles; aesthetic particles; aesthetic dyes; fillers such as sodium sulfate and / or citrus fibers, although the composition can preferably be substantially free of fillers; silicates such as sodium silicate (including 1.6R and 2.0R sodium silicate) or sodium metasilicate; copolyesters of a dicarboxylic acid and a diol; cellulosic polymers, for example methylcellulose, carboxymethylcellulose, hydroxyethyloxy cellulose, or other alkyl or alkylalkoxy celluloses; solvents such as 1,2-propanediol, monoethanolamine; diethylene glycol, ethanol, and any mixture thereof; hydrotropes such as sodium cumene sulfonate, sodium xylene sulfonate, sodium toluene sulfonate, and any mixture; organic acids and their salts such as citric acid / citrate; and any combination thereof.The composition can 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.

[0038] The detergent composition preferably comprises one or more additional enzymes. Thus, a preferred composition comprises: (a) an alginate lyase, and (b) one or more additional enzymes selected from the group consisting of aminopeptidases, amylases, carbohydrases, carboxypeptidases, catalases, cellulases, chitinases, cutinases, cyclodextrin glycosyltransferases, deoxyribonucleases, esterases, alpha-galactosidases, beta-galactosidases, glucoamylases, alpha-glucosidases, beta-glucosidases, haloperoxidases, invertases, laccases, lipases, mannanases, mannosidases, oxidases, pectinases, peptidoglutamineases, peroxidases, phytases, polyphenoloxidases, proteolytic enzymes, ribonucleases, transglutaminases, xylanases, xanthan lyases, xanthanases, endo-beta-1,3-glucanases, and mixtures thereof. Preferably, the cleaning composition comprises an additional enzyme selected from the group consisting of amylases, nucleases such as DNases and RNases and mixtures thereof, hexosaminidases, mannanases, xanthan lyases, xanthanases, amylases, and mixtures thereof.

[0039] Preferably, the composition comprises an additional enzyme selected from the group consisting of xanthan lyases, xanthanases, mannanases, and mixtures thereof. Especially preferred is a mannanase.

[0040] One or more additional enzymes can be produced, for example, by a microorganism belonging to the genus Aspergillus, such as Aspergillus aculeatus, Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger, or Aspergillus oryzae; by a microorganism belonging to the genus Fusarium, such as Fusarium bactridioides, Fusarium cerealis, Fusarium crookwellense, Fusarium culmorum, Fusarium graminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negundi, Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusarium sambucinum, Fusarium sarcochroum, Fusarium sulphureum, Fusarium toruloseum, Fusarium trichothecioides, or Fusarium venenatum; by a microorganism belonging to the genus Humicola, such as Humicola insolens or Humicola lanuginosa; or by a microorganism belonging to the genus Trichoderma, such as Trichoderma harzianum, Trichoderma koningii, Trichoderma longibrachiatum, Trichoderma reesei, or Trichoderma viride.

[0041] Preferably, the composition comprises a protease or a mixture of more than one protease, a lipase or a mixture of more than one lipase, a peroxidase or a mixture of more than one peroxidase, one or more amylolytic enzymes, e.g., alpha-amylase, glucoamylase, maltogenic amylase, and / or cellulase or a mixture thereof.

[0042] In general, the properties of the selected enzymes will be generally compatible with the selected detergent, i.e., pH optimum, compatibility with other enzymatic or non-enzymatic ingredients, etc., and the enzyme(s) should be present in effective amounts. Preferably, the products of the present application comprise at least 0.01 mg, preferably from about 0.05 mg to about 10 mg, more preferably from about 0.1 mg to about 6 mg, especially from about 0.2 mg to about 5 mg of additional active enzyme per gram of composition.

[0043] Protease: The compositions of the present application preferably comprise a protease. Mixtures of two or more proteases can help enhance 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 subtilisins (EC 3.4.21.62). Suitable proteases include those of animal, vegetable or microbial origin. In one aspect, such suitable proteases can be of microbial origin. Suitable proteases include chemically or genetically modified mutants of the foregoing suitable proteases. In one aspect, suitable proteases can be serine proteases such as alkaline microbial proteases or / and trypsin-type proteases. Examples of suitable neutral or alkaline proteases include:

[0044] Subtilisin (EC 3.4.21.62), in particular those derived from Bacillus (such as Bacillus subtilis, B. lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, B. pumilus, B. gibsonii and B. akibaii) as described in WO2004067737, WO2015091989, WO2015091990, WO2015024739, WO2015143360, US 6,312,936 Bl, US 5,679,630, US 4,760,025, DE 102006022216 Al, DE 102006022224 Al, WO2015089447, WO2015089441, WO2016066756, WO2016066757, WO2016069557, WO2016069563, WO2016069569 and WO2016174234. In particular the mutants S9R, A15T, V66A, A188P, V199I, Q239R, N255D (savinase numbering system).

[0045] Trypsin-type or chymotrypsin-type proteases, such as trypsin (e.g. porcine or bovine trypsin), including fusarin protease as described in WO 89 / 06270 and chymotrypsin derived from Cellumonas as described in WO 05 / 052161 and WO 05 / 052146.

[0046] Metalloproteases, in particular those derived from Bacillus amyloliquefaciens as described in WO07 / 044993A2, Bacillus as described in WO2014194032, WO2014194054 and WO2014194117, Thermoactinomyces, Geobacillus, Paenibacillus, Lysinibacillus or Streptomyces spp. as described in WO2015193488 derived from Kribella alluminosa and Lysobacter as described in WO2016075078 derived from Streptomyces and Lysobacter.

[0047] Proteases having at least 90% identity to the subtilase from Bacillus sp. TY145, NCIMB 40339 as described in WO92 / 17577 (Novozymes A / S), including variants of this Bacillus sp. TY145 subtilase as described in WO2015024739 and WO2016066757.

[0048] A particularly preferred protease for use in the cleaning compositions of the present application is a polypeptide having at least 90%, preferably at least 95%, more preferably at least 98%, even more preferably at least 99%, in particular 100% identity to the wild-type enzyme from Bacillus lentus, comprising a mutation at one or more, preferably two or more, more preferably three or more of the following positions: S9R, A15T, V68A, N76D, N87S, S99D, S99SD, S99A, S101G, S101M, S103A, V104N / I, G118V, G118R, S128L, P129Q, S130A, Y167A, R170S, A194P, V205I, Q206L / D / E, Y209W, M222S, Q245R and / or M222S, using the BPN' numbering system and amino acid abbreviations as shown in WO00 / 37627 (incorporated herein by reference).

[0049] Most preferably, the protease is selected from the group comprising the following mutations (BPN' numbering system) relative to the PB92 wild-type (SEQ ID NO: 2 in WO 08 / 010925) or the subtilisin 309 wild-type (sequence according to the PB92 backbone, except that it comprises the natural variation N87S).

[0050] (i) G118V + S128L + P129Q + S130A

[0051] (ii) S101M + G118V + S128L + P129Q + S130A

[0052] (iii) N76D + N87R + G118R + S128L + P129Q + S130A + S188D + N248R

[0053] (iv) N76D + N87R + G118R + S128L + P129Q + S130A + S188D + V244R

[0054] (v) N76D + N87R + G118R + S128L + P129Q + S130A

[0055] (vi) V68A + N87S + S101G + V104N

[0056] (vii) S99AD

[0057] (viii) S9R + A15T + V68A + N218D + Q245R

[0058] Suitable commercially available proteases include those sold under the trade names Liquanase Savinase Blaze and those sold by Novozymes A / S (Denmark); under the tradename Purafect Purafect Ovozyme®, and Purafect those sold by Dupont; under the tradename and those sold under the tradename Savinase® by Novozymes, those sold under the tradename Purafect® by Genencor, those sold under the tradename Properase® by Genencor, those sold under the tradename Kannase® by DuPont, those sold under the tradename BLAP by Solvay Enzymes, and those available from Henkel / Kemira, i.e. BLAP (the sequence is shown in Figure 29 of US US 5,352,604 with the following mutations S99D + S101 R + 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 mutations A230V + S256G + S259N).

[0059] Especially preferred for use herein are commercial proteases selected from the group consisting of: BLAP and BLAP variants.

[0060] A preferred level of protease in the products of the present application includes from about 0.05 mg to about 10 mg, more preferably from about 0.5 mg to about 7 mg and especially from about 1 mg to about 6 mg of active protease per gram of composition.

[0061] Lipase: The composition preferably comprises a lipase. The presence of oil and / or fat can further increase the resilience of stains comprising mannan and other polysaccharides. Thus, the presence of a lipase in the enzyme package can further improve the removal of such stains. Suitable lipases include those derived from bacteria or fungi or synthetic. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from the genus Humicola (synonym Thermomyces), e.g., from H. lanuginosa (T. lanuginosus) or from H. lanuginosa, Pseudomonas lipases, e.g., from P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. stutzeri, P. fluorescens, Pseudomonas sp. strain SD705, P. wisconsinensis, Bacillus lipases, e.g., from B. subtilis (Dartois et al. (1993) Biochemica et Biophysica Acta 1131:253-360), B. stearothermophilus, or B. pumilus.

[0062] The lipase can be a "first cycle lipase", such as those described in U.S. Patent 6,939,702 Bl and U.S. Patent 2009 / 0217464. In one aspect, the lipase is a first wash lipase, preferably a variant of the wild-type lipase from H. lanuginosa comprising T231 R and N233R mutations. The wild-type sequence is 269 amino acids (amino acids 23-291) of Swissprot accession number Swiss-Prot 059952 (derived from H. lanuginosa). Preferred lipases include those sold under the trade name Lipex®. and Lipex®.

[0063] Other suitable lipases include: Liprl 139, e.g. as described in WO2013 / 171241; TfuLip2, e.g. as described in WO2011 / 084412 and WO2013 / 033318; Pseudomonas stutzeri lipase, e.g. as described in WO2018228880; Microbulbifer thermotolerans lipase, e.g. as described in WO2018228881; Sulfobacillus acidocaldarius lipase, e.g. as described in EP3299457; LIP062 lipase, e.g. as described in WO2018209026; PinLip lipase, e.g. as described in WO2017036901, and Absidia sp. lipase, as described in WO2017005798.

[0064] A suitable lipase is a variant of SEQ ID NO: 5 comprising:

[0065] (a) the substitution T231R

[0066] and

[0067] (b) the substitution N233R or N233C

[0068] and

[0069] (c) at least three further 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;

[0070] wherein the positions correspond to the positions of SEQ ID NO: 5, and wherein the lipase variant has at least 90% but less than 100% sequence identity to the polypeptide having the amino acid sequence of SEQ ID NO: 5, and wherein the variant has lipase activity.

[0071] A preferred lipase is a variant of SEQ ID NO: 5 comprising the substitutions T231R, N233R, D27R, G38A, D96E, D111A, G163K, D254S and P256T.

[0072] A preferred lipase is a variant of SEQ ID NO: 5 comprising the substitutions T231R, N233R, N33Q, G91Q, E210Q, I255A.

[0073] Suitable lipases are commercially available from Novozymes, for example under the trade name Lipex Evity 100L, Lipex Evity 200L (both liquid feedstocks) and Lipex Evity 105T (granulate). These lipases have a different structure compared to the products Lipex 100L, Lipex 100T and Lipex Evity 100T which are outside the scope of the present application.

[0074] Cellulases: Suitable cellulases include those derived from bacteria or fungi. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., fungal cellulases produced by Humicola insolens, Myceliopthora thermophila, and Fusarium oxysporum, disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757, and US 5,691,178.

[0075] In one aspect, preferred enzymes include endoglucanases derived from microorganisms that exhibit endo-beta-1,4-glucanase activity (E.C. 3.2.1.4), preferably selected from the group consisting of:

[0076] (a) an endogenous bacterial polypeptide of a Bacillus member having a sequence of at least 90%, 94%, 97%, and even 99% identity to the amino acid sequence of SEQ ID NO: 2 in US 7,141,403 B2, preferred substitutions comprise one or more of positions corresponding to positions 292, 274, 266, 265, 255, 246, 237, 224, and 221 of the mature polypeptide of SEQ ID NO: 2, and the variant has cellulase activity;

[0077] (b) a glycosyl hydrolase having enzyme activity on xyloglucan and amorphous cellulose substrates, wherein the glycosyl hydrolase is selected from the GH 5, 7, 12, 16, 44, or 74 families;

[0078] (c) a glycosyl hydrolase having a sequence of at least 90%, 94%, 97%, and even 99% identity to the amino acid sequence of SEQ ID NO: 3 in WO09 / 148983;

[0079] (d) variants exhibiting at least 70% identity to SEQ ID NO: 5 in WO2017106676. Preferred substitutions comprise one or more of the 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;

[0080] (e) and mixtures thereof.

[0081] Suitable endoglucanases are sold under the tradenames Celluclean® and (Genencor International Inc.), Carezyme® (Novozymes A / S, Bagsvaerd, Denmark). Examples include 5000L, Classic 400L, Classic 700T, 4500T, 1.5T, 2.0L.

[0082] Other commercially available cellulases include Premium (Novozymes A / S), Puradax 1000, 2000 (Genencor International Inc.), (Kao Corporation), FCL, DCL, DCC, NCD, FCC, FLX1 (AB Enzymes).

[0083] Suitable glucanases include endo-beta-1,3-glucanases, preferably from the class E.C. 3.2.1.39, preferably obtained from a microorganism of the genus Paenibacillus, Xanthobacter squalenes, Thermotoga neapolitana, or Trichoderma, preferably Paenibacillus or Xanthobacter squalenes, most preferably Paenibacillus.

[0084] Amylase: Preferably, the composition of the present application comprises an amylase. Suitable alpha-amylases include those derived from bacteria or fungi. Mutants (variants) including chemically modified or genetically modified are included. Preferred alkaline alpha-amylases are derived from strains of Bacillus, such as Bacillus licheniformis, B. amyloliquefaciens, B. stearothermophilus, B. subtilis or other Bacillus sp., such as Bacillus sp. NCBI 12289, NCBI 12512, NCBI 12513, DSM 9375 (USP 7,153,818), DSM 12368, DSMZ 12649, KSM AP1378 (WO 97 / 00324), KSM K36 or KSM K38 (EP 1,022,334). Preferred amylases include:

[0085] (a) variants described in USP 5,856,164 and WO99 / 23211, WO 96 / 23873, WO00 / 60060, WO06 / 002643 and WO2017 / 192657, in particular variants having one or more substitutions in the following positions relative to the AA560 enzyme set out 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, which variants preferably further comprise the deletions of D183* and G184*.

[0086] (b) variants exhibiting at least 85%, preferably 90% identity with SEQ ID No. 4 in WO06 / 002643, wild-type enzyme from Bacillus sp. SP722, in particular variants with deletions at positions 183 and 184, and variants described in WO 00 / 60060, WO201 1 / 100410 and WO2013 / 003659, especially those with one or more substitutions in the following positions relative to SEQ ID NO. 4 of WO06 / 002643: 51, 52, 54, 109, 304, 140, 189, 134, 195, 206, 243, 260, 262, 284, 347, 439, 469, 476 and 477.

[0087] (c) variants exhibiting at least 90% identity with the wild-type enzyme from Bacillus 707 (SEQ ID NO: 7 in US 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. Especially preferred are those comprising the M202L or M202T mutations. Further relevant mutations / deletions based on the SP707 backbone include W48, A51, V103, V104, A1 13, R1 18, N125, V131, T132, E134, T136, E138, R142, S154, V165, R182, G182, H183, E190, D192, T193, I206, M208, D209, E212, V213, V214, N214, L217, R218, N219, 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.

[0088] (d) variants described in WO 09 / 149130, preferably those exhibiting at least 90% identity to SEQ ID NO: 1 or SEQ ID NO: 2 in WO 09 / 149130 (wild-type enzyme from Geobacillus Stearophermophilus or a truncated version thereof).

[0089] (e) variants described in WO10 / 115021, in particular those exhibiting at least 75%, or at least 85%, or at least 90%, or at least 95% to SEQ ID NO: 2 in WO10 / 115021 (alpha-amylase derived from Bacillus sp. TS-23).

[0090] (f) variants exhibiting at least 89% identity to SEQ ID NO: 1 in WO2016091688, in particular those comprising a deletion at positions H183+G184 and further comprising one or more mutations at positions 405, 421, 422 and / or 428.

[0091] (g) variants described in WO2014099523, in particular those exhibiting at least 60% amino acid sequence identity to the “PcuAmyl alpha-amylase” from Paenibacillus curdlanolyticus YK9 (SEQ ID NO: 3 in WO2014099523).

[0092] (h) variants described in WO2014099523, in particular those exhibiting at least 60% amino acid sequence identity to the “CspAmy2 amylase” from Cytophaga sp. (SEQ ID NO: 1 and 6 in WO2014164777). In particular those 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.

[0093] (i) variants exhibiting at least 85% identity to AmyE from Bacillus subtilis (SEQ ID NO: 1 in WO2009149271).

[0094] (j) variants exhibiting at least 90% identity to wild-type amylase from Bacillus sp. KSM-K38 (Accession No. AB051102).

[0095] (k) variants described in WO2016180748, in particular those exhibiting at least 80% identity to the mature amino acid sequence of AAI10 from Bacillus sp. in SEQ ID NO: 7 in WO2016180748; those exhibiting at least 80% identity to the mature amino acid sequence of Alicyclobacillus sp amylase in SEQ ID NO: 8 in WO2016180748, and those exhibiting at least 80% identity to the mature amino acid sequence of SEQ ID NO: 13 in WO2016180748, in particular those comprising one or more of the following mutations: H*, N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G184T, N195F, V206L, K391A, P473R, G476K.

[0096] (l) variants described in WO2018060216, in particular those exhibiting at least 70% identity to the mature amino acid sequence of SEQ ID NO: 4 in WO2018060216 (a fusion molecule of B. amyloliquefaciens and B. licheniformis). In particular those comprising 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.

[0097] A preferred amylase is an engineered enzyme in which one or more of the amino acids susceptible to bleaching oxidation have been substituted with amino acids that are less susceptible to oxidation. In particular, it is preferred that methionine residues are substituted with any other amino acid. In particular, it is preferred that the most susceptible to oxidation methionine is substituted. Preferably, the methionine at the position equivalent to 202 in SEQ ID NO: 11 is substituted. Preferably, the methionine at this position is substituted with threonine or leucine, preferably leucine.

[0098] Suitable commercially available alpha-amylases include TERMAMYL STAINZYME ACHIEVE PRIME, and (Novozymes A / S, Bagsvaerd, Denmark), AT 9000 Biozym Biotech Trading GmbH Wehlistrasse 27b A-1200 Wien Austria, OPTISIZE HT PREFERENZ series (including PREFERENZ and PREFERENZ ), PURASTAR (DuPont., Palo Alto, California) and (Kao, 14-10 Nihonbashi Kayabacho, 1-chome, Chuo-ku Tokyo 103-8210, Japan).

[0099] Preferably, the composition comprises at least 0.01 mg, preferably from about 0.05 mg to about 10 mg, more preferably from about 0.1 mg to about 6 mg, in particular from about 0.2 mg to about 5 mg of active amylase per gram of composition.

[0100] Peroxidase / oxidase: Suitable peroxidases / oxidases include those derived from plants, bacteria or fungi. Chemically modified or protein engineered mutant peroxidases are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus and variants thereof as described in WO 93 / 24618, WO 95 / 10602 and WO 98 / 15257.

[0101] Commercially available peroxidases include (Novozymes A / S).

[0102] Pectate lyase: Suitable pectate lyases include those sold under the tradename (both from Novozymes A / S, Bagsvaerd, Denmark), Those sold by F1000 (DuPont Industrial Biosciences).

[0103] Mannanase. The composition preferably comprises one or more mannanases. As used herein, the term "mannanase" or "galactomannanase" refers to a mannanase that is defined as a mannan endo-1,4-β-mannosidase according to what is known in the art and has the aliases β-mannanase and endo-1,4-mannanase and catalyzes the hydrolysis of 1,4-β-D-mannosidic bonds in mannans, galactomannans, glucomannans and galactoglucomannans. Mannanases are classified according to enzyme nomenclature as EC 3.2.1.78 and belong 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 names (Novozymes A / S) such as 200L and Mannaway Evity 4.0T. Other commercially available mannanases include M1000, 375, PreferenzM100 and (all from DuPont Industrial Biosciences) and Biotouch M7 (AB Enzymes). Other suitable mannanases belong to glycosyl hydrolase family 26, including those described in WO2018191135, WO2015040159, WO2017021515, WO2017021516, WO2017021517 and WO2019081515. Suitable mixtures of mannanases include a combination of glycosyl hydrolase family 5 and glycosyl hydrolase family 26 mannanases described in WO2019081515.

[0104] Xanthan-degrading enzymes: The composition can comprise one or more xanthan-degrading enzymes. Suitable enzymes for degrading xanthan-based stains include xanthan endo-glucanases, optionally in combination with xanthan lyases. As used herein, the term "xanthan endo-glucanase" denotes an enzyme exhibiting endo-beta-1,4-glucanase activity, which enzyme is capable of catalysing the hydrolysis of the 1,4-linked beta-D-glucose polymer backbone of xanthan, optionally in combination with a suitable xanthan lyase. Suitable xanthan endo-glucanases are described in WO2013167581, WO2015181299, WO2015181292, WO2017046232, WO2017046260, WO201837062, WO201837065, WO2019038059 and WO2019162000. As used herein, the term "xanthan lyase" denotes an enzyme that cleaves the beta-D-mannosyl-beta-D-1,4-glucuronide bond of xanthan. Such enzymes belong to E.C. 4.2.2.12. Suitable xanthan lyases are described in WO2015001017, WO2018037061, WO201837064, WO2019038060, WO2019162000 and WO2019038057.

[0105] Nucleases: Preferably, the composition comprises a nuclease, such as an RNase or a DNase or mixtures thereof. Nucleases are enzymes that are capable of cleaving the phosphodiester bonds between the nucleotide subunits of nucleic acids. The nucleases herein are preferably deoxyribonucleases or ribonucleases or functional fragments thereof. By functional fragment or portion is meant a portion of the nuclease that catalyses the cleavage of the phosphodiester bonds in the DNA backbone and is thus a region of the nuclease protein that retains catalytic activity. It thus includes truncated but functional forms of the enzyme and / or variants and / or derivatives and / or homologues in which the function is maintained.

[0106] Preferably, the nuclease is a deoxyribonuclease, preferably selected from any one of the following classes: E.C. 3.1.21.x, wherein x = 1, 2, 3, 4, 5, 6, 7, 8 or 9, E.C. 3.1.22.y, wherein y = 1, 2, 4 or 5, E.C. 3.1.30.z, wherein z = 1 or 2, E.C. 3.1.31.1 and mixtures thereof.

[0107] DNase: Suitable DNases include wild-type and variants of DNases defined by SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, and 9 in WO2017162836 (Novozymes) and 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, 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 in WO2018108865, and variants of Bacillus cibi DNase including those described in WO2018011277 (Novozymes), incorporated herein by reference. Preferred DNases are as described in co-pending European patent application EP18202967.

[0108] RNase: 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 in WO2018178061 (Novozymes) and SEQ ID NOs: 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, and 104 in WO2020074499 (Novozymes), incorporated herein by reference.

[0109] Amino hexosidase: The composition can comprise one or more amino hexosidases. The term amino hexosidase includes the "dispersin" and the abbreviation "Dsp" which refers to a polypeptide having amino hexosidase activity, EC 3.2.1.- which catalyzes the hydrolytic cleavage of beta-1,6-glucosidic bonds of N-acetyl-glucosamine polymers present in microbial- sourced stains. The term amino hexosidase includes polypeptides having N-acetylglucosaminidase activity and beta-N-acetylglucosaminidase activity. Amino hexosidase activity can be determined according to Assay II described in WO2018184873. Suitable amino hexosidases include those disclosed in WO2017186936, WO2017186937, WO2017186943, WO2017207770, WO2018184873, WO2019086520, WO2019086528, WO2019086530, WO2019086532, WO2019086521, WO2019086526, WO2020002604, WO2020002608, WO2020007863, WO2020007875, WO2020008024, WO2020070063, WO2020070249, WO2020088957, WO2020088958 and WO2020207944. Variants of Geobacillus stearothermophilus amino hexosidase defined by SEQ ID NO: 1 of WO2020207944 can be preferred, in particular variants disclosed in this publication having improved thermostability.

[0110] Galactanase: Preferably, the composition comprises a galactanase, i.e. an extracellular polymeric substance degrading enzyme comprising an endo-beta-1,6-galactanase. 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 from glycoside hydrolase family 30 (EC 3.2.1.164) catalyzing the hydrolytic cleavage of 1,6-beta-D-galacto-oligosaccharides with a degree of polymerization (DP) higher than 3, as well as their acidic derivatives having a 4-0-methylglucuronic acid or glucuronate group at the non-reducing end. For the purpose of the present disclosure, endo-beta-1,6-galactanase activity is determined according to the procedure described in Assay I in WO2015185689. Suitable examples from EC 3.2.1.164 are described in WO2015185689, such as the mature polypeptide SEQ ID NO: 2.

[0111] Additional enzymes can be included in the detergent composition by the addition of separate enzyme additives comprising additional enzymes or a combined enzyme additive comprising two or several or all of these additional enzymes. Such enzyme additives can be in the form of granulates, liquids or slurries, preferably additionally comprising enzyme stabilizers.

[0112] Preferably, the or each additional enzyme will be present in the composition in an amount of at least 0.0001 wt% to about 0.1 wt% pure active enzyme protein, such as from about 0.0001% to about 0.01%, from about 0.001% to about 0.01%, or from about 0.001% to about 0.01%, by weight based on the weight of the composition.

[0113] Fabric hueing agents. The composition can comprise a fabric hueing agent (sometimes referred to as shading agents, bluing agents, or whitening agents / dyes). Hueing agents generally provide a blue or violet shade to fabric. Hueing agents can be used alone or in combination to create a particular shade of hueing and / or to shade different fabric types. This can be provided, for example, by mixing a red and a blue-green dye to yield a blue or violet shade. The hueing agent can be selected from any known chemical class of dye, including but not limited to acridine, anthraquinone (including polycyclic quinones), azine, azo (e.g., monoazo, disazo, trisazo, tetrakisazo, polyazo), including premetallized azo, benzodifurane and benzodifuranone, carotenoid, coumarin, cyanine, diazahemicyanine, diphenylmethane, formazan, hemicyanine, indigoids, methane, naphthalimide, naphthoquinone, nitro and nitroso, oxazone, phthalocyanine, pyrazole, stilbene, styryl, triarylmethane, triphenylmethane, xanthene, and mixtures thereof. Preferred are azo dyes, especially mono or disazo dyes, triarylmethane dyes and anthraquinone dyes.

[0114] 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 falling into the Colour Index (C.I.) classifications of Direct Dyes, Basic Dyes, Reactive Dyes or Hydrolysed Reactive Dyes, Solvent Dyes or Disperse Dyes. Examples of suitable small molecule dyes include, for example, small molecule dyes selected from the group consisting of Colour Index (Society of Dyers and Colourists, Bradford, UK) numbers: Direct Violet dyes such as 9, 35, 48, 51, 66 and 99, Direct Blue dyes such as 1, 71, 80 and 279, Acid Red dyes such as 17, 73, 52, 88 and 150, Acid Violet dyes such as 15, 17, 24, 43, 49, 50 and 51, Acid Blue dyes such as 15, 17, 25, 29, 40, 45, 75, 80, 83, 90 and 113, Acid Black dyes such as 1, Basic Violet dyes such as 1, 3, 4, 10 and 35, Basic Blue dyes such as 3, 16, 22, 47, 66, 75 and 159, Disperse or Solvent dyes such as described in EP1794275 or EP1794276, or dyes as disclosed in US 7,208,459 B2, and mixtures thereof.

[0115] Preferred polymeric dyes include polymeric dyes selected from the group consisting of polymers containing covalently bound (sometimes referred to as conjugated) chromophores (dye-polymer conjugates) (for example polymers with co-polymerised into the backbone of the polymer) and mixtures thereof. Polymeric dyes include those described in WO2011 / 98355, WO2011 / 47987, US2012 / 090102, WO2010 / 145887, WO2006 / 055787 and WO2010 / 142503.

[0116] Preferred polymeric dyes include alkoxylated, preferably ethoxylated, azo, anthraquinone or triarylmethane dyes. Particularly preferred are ethoxylated thienyl nitrogen containing dyes, for example polymeric dyes selected from the group consisting of: (Milliken, Spartanburg, South Carolina, USA) fabric direct colorants, dye-polymer conjugates formed from at least one reactive dye, and polymers selected from the group consisting of polymers comprising a moiety selected from the group consisting of: a hydroxyl moiety, a primary amine moiety, a secondary amine moiety, a thiol moiety, and mixtures thereof. Suitable polymeric dyes include polymeric dyes selected from the group consisting of: Violet CT, carboxymethylcellulose (CMC) covalently bound to a reactive blue, reactive violet or reactive red dye, such as CMC conjugated with C.I. Reactive Blue 19 sold by Megazyme, Wicklow, Ireland under the product name AZO-CM-CELLULOSE, product code S-ACMC, alkoxylated triphenyl-methane polymeric colorants, alkoxylated thiophene polymeric colorants, and mixtures thereof.

[0117] Preferred shading dyes include the alkoxylated thiophene azo whitening agents present in US 2008 / 0177090, which can optionally be anionic, such as those selected from Examples 1 to 42 in Table 5 of WO 2011 / 011799. Other preferred dyes are disclosed in US 8138222.

[0118] Suitable pigments include pigments selected from the group consisting of ultramarine blue (C.I. Pigment Blue 29), ultramarine violet (C.I. Pigment Violet 15), and mixtures thereof. Pigments and / or dyes can also be added for aesthetic reasons to add color. Preferred are organic blue, violet and / or green pigments.

[0119] Builders: The detergent composition can also comprise a builder, such as a carbonate, bicarbonate or silicate based builder, the silicate builder can be a zeolite, such as zeolite A, zeolite MAP (high alumina type P). Zeolites useful for laundry are preferably of the formula Na 12 (AlO2) 12 (SiO2) 12 • 27H2O and zeolite A typically has a particle size between 1 and 10 μιη, zeolite MAP typically has a particle size between 0.7 and 2 μιη. Other builders are sodium metasilicate (Na2SiO3.nH2O or Na2Si2O5.n H2O) strong alkali and are preferably used in dishwashing. In preferred embodiments, the amount of detergent builder can be higher than 5%, higher than 10%, higher than 20%, higher than 30%, higher than 40% or higher than 50% and can be lower than 80%, 65%. In dishwashing detergents, the content of builder is typically 40% to 65%, especially 50% to 65% or even 75% to 90%.

[0120] Encapsulates: The composition can comprise an encapsulated benefit agent comprising a core and a shell having an inner surface and an outer surface, the shell encapsulating the core. The core can comprise a material selected from the group consisting of: a perfume; a whitening agent; a dye; an insect repellent; a silicone; a wax; a flavor; a vitamin; a fabric softening agent; a skin care agent, in one aspect, a paraffin; an enzyme; an antibacterial agent; a bleaching agent; a sensate; and mixtures thereof. The shell can comprise a material selected from the group consisting of: polyethylene; polyamide; polystyrene; polyisoprene; polycarbonate; polyester; polyacrylate; an aminoplast, in one aspect the aminoplast can comprise a polyurea, a polyurethane, and / or a polyureaurethane, in one aspect the polyurea can comprise a polyoxymethyleneurea and / or a melamine formaldehyde resin; a polyolefin; a polysaccharide, in one aspect the polysaccharide can comprise an alginate and / or a chitosan; a gelatin; a shellac; an epoxy resin; a vinyl polymer; a water-insoluble inorganic; a silicone; and mixtures thereof. Preferred encapsulates comprise a core comprising a perfume. Such encapsulates are perfume microcapsules.

[0121] Enzyme Stabilizers: The composition can comprise an enzyme stabilizer. Suitable enzyme stabilizers can 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) mass effective reversible protease inhibitors selected from the group consisting of: benzoic acids and derivatives thereof, e.g. aromatic boronic esters, or benzoic acid derivatives such as 4-formylbenzoic acid, or peptide aldehydes such as di-, tri- or tetrapeptide aldehydes or aldehyde analogues (one of the forms B1-B0-R, wherein R is H, CH3, CX3, CHX2 or CH2X (X = halogen), B0 is a single amino acid residue (preferably with an optionally substituted aliphatic or aromatic side chain); and B1 consists of one or more amino acid residues (preferably one, two or three), optionally comprising an N-terminal protecting group, or as described in WO09118375, WO98 / 13459); and (d) reversible protease inhibitors such as boron containing compounds; (e) polyols such as propylene glycol or glycerol 1-2 propylene glycol; (f) calcium and / or sodium formate; (g) protein type protease inhibitors such as RASI, BASI, WASI (rice, barley and wheat bifunctional alpha-amylase / subtilisin inhibitors) or CI2 or SSI, and (h) any combination thereof.

[0122] Structurants: In one aspect, the composition can comprise a structurant selected from the group consisting of: diglycerides and triglycerides, ethylene glycol distearate, microcrystalline cellulose, cellulose based materials, microfibrous cellulose, biopolymers, xanthan gum, gellan gum, and mixtures thereof.

[0123] Polymer: The composition preferably comprises one or more polymers. Preferred examples are carboxymethylcellulose, poly(vinylpyrrolidone), poly(ethylene glycol), poly(vinyl alcohol), poly(vinylpyridine-N-oxide), poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic / acrylic acid copolymers and lauryl methacrylate / acrylic acid copolymers and amphiphilic polymers and mixtures thereof.

[0124] Amphiphilic cleansing polymer: Preferably, the amphiphilic cleansing polymer is a compound having the general structure: bis((C2H5O)(C2H4O)n)(CH3)-N + -C x H 2x -N + -(CH3)-bis((C2H5O)(C2H4O)n), wherein n = 20 to 30 and x = 3 to 8, or sulfated or sulfonated variants thereof.

[0125] The amphiphilic alkoxylated grease cleansing polymers of the present invention refer to any alkoxylated polymer having a balanced hydrophilic and hydrophobic character, such that they are able to remove grease particles from fabrics and surfaces. Specific embodiments of the amphiphilic alkoxylated grease cleansing polymers of the present invention comprise a core structure and a plurality of alkoxylate groups attached to the core structure. These can include alkoxylated polyalkyleneimines, preferably having internal polyethylene oxide blocks and external polypropylene oxide blocks.

[0126] The core structure can comprise a polyalkyleneimine structure comprising repeat units of formula (I), (II), (III) and (IV) in condensed form:

[0127]

[0128] wherein in each case # denotes one half of a bond between a nitrogen atom of two adjacent repeat units of formula (I), (II), (III) or (IV) and a free binding site of group A 1 ; in each case * denotes one half of a bond to one of the alkoxylate groups; and A 1 is independently selected from linear or branched C2-C6-alkylene; wherein the polyalkyleneimine structure consists of 1 repeat unit of formula (I), x repeat units of formula (II), y repeat units of formula (III) and y+1 repeat units of formula (IV), wherein in each case x and y have a value in the range of from 0 to about 150; wherein the average weight average molecular weight Mw of the polyalkyleneimine core structure is in the range of values from about 60 g / mol to about 10,000 g / mol.

[0129] The core structure can alternatively comprise a polyalkanolamine structure of a condensation product of at least one compound selected from N-(hydroxyalkyl)amines of the formula (I.a) and / or (I.b),

[0130]

[0131] 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 are independently selected from hydrogen, alkyl, cycloalkyl or aryl, wherein the last three mentioned radicals can optionally be substituted; and R 6 is selected from hydrogen, alkyl, cycloalkyl or aryl, wherein the last three mentioned radicals can optionally be substituted.

[0132] The plurality of alkyleneoxy groups attached to the core structure is independently selected from alkyleneoxy units of the formula (V)

[0133]

[0134] wherein in each case * denotes one half of a bond to a nitrogen atom of a repeating unit of the formula (I), (II) or (IV); in each case A 2 is independently selected from 1,2-propylene, 1,2-butylene and 1,2-isobutylene; A 3 is 1,2-propylene; in each case R is independently selected from hydrogen and C1-C4-alkyl; m has an average value in the range of 0 to about 2; n has an average value in the range of about 20 to about 50; and p has an average value in the range of about 10 to about 50.

[0135] Carboxylate polymer: The composition also preferably comprises one or more carboxylate polymers, such as a maleate / acrylate random copolymer or a polyacrylate homopolymer. In one aspect, 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.

[0136] Soil release polymer: The composition also preferably comprises one or more soil release polymers having a structure defined by one of the following structures (I), (II) or (III):

[0137] (I) - [OCHR 1 -CHR2 a -O-OC-Ar-CO- d

[0138] (II)-[(OCHR 3 -CHR 4 b -O-OC-sAr-CO- e

[0139] (III)-[(OCHR 5 -CHR 6 c -OR 7 f

[0140] wherein:

[0141] a, b and c are from 1 to 200;

[0142] d, e and f are from 1 to 50;

[0143] Ar is a 1,4-substituted phenylene;

[0144] sAr is a 1,3-substituted phenylene substituted in position 5 by SO3Me;

[0145] Me is Li, K, Mg / 2, Ca / 2, Al / 3, ammonium, mono-, di-, tri- or tetraalkylammonium, wherein alkyl is C1-C 18 alkyl or C2-C 10 hydroxyalkyl or mixtures thereof;

[0146] R 1 , R 2 , R 3 , R 4 , R 5 and R 6 are independently selected from H or C1-C 18 n-alkyl or isoalkyl; and

[0147] R 2 is a linear or branched C1-C 18 alkyl, or a linear or branched C2-C 30 alkenyl, or a cycloalkyl group having from 5 to 9 carbon atoms, or a C8-C 30 aryl group, or a C6-C 30 aralkyl group.

[0148] ​​​​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.

[0149] Cellulosic polymer: The composition also preferably comprises one or more cellulosic polymers, including those selected from the group consisting of alkyl cellulose, alkyl alkoxy alkyl cellulose, carboxyalkyl cellulose, alkyl carboxyalkyl cellulose. In one aspect, the cellulosic polymer is selected from the group consisting of carboxymethyl cellulose, methyl cellulose, methylhydroxyethyl cellulose, methyl carboxymethyl cellulose, and mixtures thereof. In one aspect, the carboxymethyl cellulose has a carboxymethyl substitution of 0.5 to 0.9 and a molecular weight of 100,000 Da to 300,000 Da.

[0150] Bleach system: The composition can contain a bleach system, for example, comprising a source of H2O2 such as perborate or percarbonate, which can be combined with a bleach activator such as tetraacetylethylenediamine or nonanoyloxybenzenesulfonate that forms a peracid. Alternatively, the bleach system can comprise a peroxyacid (e.g., amide, imide, or sulfone-based peroxyacid). Generally, when a bleach is used, the compositions of the present application can comprise 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.

[0151] Chelant: The composition preferably comprises a chelant, preferably in an amount of from 0.005% to about 15% or even from about 3.0% to about 10% by weight of the composition. Suitable chelants include copper, iron and / or manganese chelants, and mixtures thereof. Preferred chelants (complexing agents) include: DTPA (diethylene triamine pentaacetic acid), HEDP (hydroxyethane diphosphonic acid), DTPMP (cyclobutane triamine penta(methylene phosphonic acid)), 1,2-dihydroxybenzene-3,5-disulfonic acid disodium salt hydrate, ethylenediamine, cyclobutane triamine, ethylenediamine disuccinic acid (EDDS), N-hydroxyethyl ethylenediamine triacetic acid (HEDTA), triethylenetetramine hexaacetic acid (TTHA), N-hydroxyethyliminodiacetic acid (HEIDA), dihydroxyethylglycine (DHEG), ethylenediaminetetrappropionic acid (EDTP), methylglycine- diacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), iminodisuccinic acid (IDS), carboxymethylcellulose; and their salt derivatives and mixtures thereof. Preferred chelants are selected from methylglycine diacetic acid (MGDA) and salts and derivatives thereof, glutamic acid diacetic acid tetrasodium (GLDA) and salts and derivatives thereof, iminodisuccinic acid tetrasodium (IDS) and salts and derivatives thereof, carboxymethylcellulose and salts and derivatives thereof, and mixtures thereof. Particularly preferred is MGDA and salts thereof, especially the trisodium salt comprising MGDA.

[0152] The composition can also comprise other conventional detergent ingredients (such as fabric conditioners), including clays, foam boosters, suds suppressors, anti-corrosion agents, soil suspending agents, anti-soil redeposition agents, dyes, bactericides, optical brighteners, hydrotropes, tarnish inhibitors, organic solvents (such as ethanol), or perfumes.

[0153] Method of use

[0154] The present application also provides a method for treating a fabric, the method comprising contacting the fabric in a contacting step with an aqueous wash liquor comprising an alginate lyase as described above, preferably in an amount of from 0.01 ppm to 10 ppm, preferably from 0.1 ppm to 1 ppm; and an anionic surfactant, preferably in an amount of from 0.05 g / l to 50 g / l, more preferably from 0.2 g / l to 5 g / l or from 0.5 g / l to 3 g / l, wherein the alginate lyase is from the polysaccharide lyase family 7.

[0155] The aqueous wash liquor can be formed by adding the composition as described above to water, for example in a laundry washing process or a hand washing process. Alternatively, the aqueous wash liquor can be formed by adding the alginate lyase and the anionic surfactant as separate components to water to form the wash liquor. The fabric can then be optionally washed and / or rinsed and / or dried.

[0156] The alginate lyase and any additional enzymes can be present in the wash liquor in an amount corresponding to 0.001 mg to 100 mg of active enzyme protein per liter of wash liquor, preferably 0.005 mg to 5 mg of active enzyme protein per liter of wash liquor, more preferably 0.01 mg to 1 mg of active enzyme protein per liter of wash liquor, and in particular 0.1 mg to 1 mg of active enzyme protein per liter of wash liquor.

[0157] In the contacting step, or in a subsequent step, mechanical agitation can be preferably used to facilitate cleaning and removal of the decomposition soil by-products from the fabric. The wash liquor preferably has a pH of about 7 or 8 to about 10.5. The composition can be employed typically 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 °C to 35 °C or 30 °C. The ratio of water to fabric is typically about 1 : 1 to about 30: 1.

[0158] Testing

[0159] Enzyme activity on beta-D-mannuronate blocks (poly M activity) and alpha-L-guluronate blocks (poly G activity) Examples

[0160] Alginate lyase activity was measured using Mannuronate block oligosaccharides DP20-DP35 (product code: ALG601) and Guluronate oligosaccharides DP2-DP45 (product code: ALG610) from Eclicityl, France as substrates. Mannuronate block oligosaccharides DP20-DP35 were used to measure polyM activity, while Guluronate oligosaccharides DP2-DP45 were used to measure polyG activity.

[0161] 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 at 25 °C for 60 minutes.

[0162] When the enzymes were contacted with each of the substrates, the activity on each of the substrates was given as delta absorption at 235 nm in a spectrophotometer relative to a zero enzyme sample. These values were then used to assess the activity of the respective enzyme on beta-D-mannuronate blocks (polyM) and / or alpha-L-guluronate blocks (polyG). Enzymes having activity on poly(beta-D-mannuronate) (polyM activity) preferably provide a delta absorption of at least 0.1 absorption units, more preferably at least 0.15 absorption units, and more preferably at least 0.2 absorption units relative to zero enzyme. Enzymes having activity on poly(alpha-L-guluronate) (polyG activity) preferably provide a delta absorption of at least 0.3 absorption units, preferably at least 0.4 or even 0.5 or 0.6 absorption units relative to zero enzyme.

[0163] Example 1 : Liquid detergent composition comprising alginate lyase from the polysaccharide lyase (PL) 7 family

[0164] Detergency performance of liquid detergent compositions comprising alginate lyases from other PL families Detergent examples

[0165] The wash performance of alginate lyase enzymes on the removal of soiled collars and cuffs was determined as follows in the context of laundry detergent:

[0166] A Talboys Professional Incubating Microplate Shaker (Equipment No. 080513002) supplied by Cole-Parmer Instrument Co Ltd, UK was used for the removal tests. The soiled collar and cuff stains were cut into 2 cm x 2 cm pieces and added to each receptacle of a 6-well plate (VWR International Ltd, Leicester, UK).

[0167] In each receptacle, 6 mL of a solution containing 1.5 g / L of Ariel unit dose liquid (without enzyme) was added. The stains were added and incubated with the respective alginate lyase of interest and the enzyme-free unit dose liquid solution at 35 °C for 45 minutes at a stirring speed of 600 rpm.

[0168] Alginate lyases from PL7 and different PL families were tested at a wash concentration of 2 ppm active alginate lyase for each of the enzymes. During the test, the temperature was kept at 35 °C. After 40 minutes, the wash water was drained and the fabric was rinsed in cold tap water (19 grains per US gallon) and then the washed stain samples were laid flat on a rack to dry under ambient conditions.

[0169] This procedure was repeated three more times, resulting in a total of four washes of the stains per treatment, i.e. four external replicates, each comprising one stain.

[0170] Pre- and post-wash analysis of the stains was done using image analysis (Illuminant D65 / 10) to calculate the difference in stain removal between the test and reference formulations.

[0171] The Stain Removal Index (SRI) was calculated using the following formula, where ΔE AB is the color difference between the stain-free area of the fabric before washing and the stain area before washing, ΔE AD is the color difference between the stain-free area of the fabric before washing and the stain area after washing.

[0172] SRI = 100 * (ΔE AB - ΔE AD ) / ΔE AB ,

[0173] The average test results are shown in the table below. They show that the addition of the PL7 family alginate lyase results in a large improvement in stain removal of 76.9 SRI units for the soiled collar and cuffs. This improvement is statistically significant, i.e. with a confidence level of greater than 99.9% (20.4 SRI units) relative to no alginate lyase addition according to the Student's T test (P < 0.001). In contrast, the addition of the alginate lyase from the PL5 family results in 25.3 SRI units of stain removal, which is not statistically significant from the zero enzyme control. The addition of the alginate lyase from the PL6 family results in 28.0 SRI units of stain removal on the soiled collar and cuffs, which is also not statistically significant from the zero enzyme control, i.e. with a confidence level of less than 90% according to the Student's T test (P > 0.1).

[0174]

[0175] Examples 14-21 : Heavy duty liquid laundry detergent compositions

[0176] Examples 1-6: Granular laundry detergent compositions designed for hand washing or top loading washing machines.

[0177]

[0178]

[0179] Examples 7-13: Granular laundry detergent compositions designed for front loading automatic washing machines.

[0180]

[0181]

[0182] * Deoxyribonuclease is shown as active enzyme milligrams per 100 g of detergent.

[0183] Examples 22-28: Unit dose laundry detergent compositions. Such unit dose formulations can include one or more

[0184]

[0185]

[0186]

[0187] Compartment Example 29: Multi-compartment unit dose compositions .

[0188]

[0189]

[0190] Multi-compartment formulations

[0191] The following provides multi-compartment unit dose laundry detergent formulations of the present application. In these examples, the unit dose has three compartments, but similar compositions can be made with two, four, or five compartments. The film used to enclose the compartments is polyvinyl alcohol.

[0192]

[0193] Raw materials and instructions for composition examples 1 to 29

[0194]

[0195] ​

[0196] Linear alkylbenzene sulfonate with C11-C18 average fatty carbon chain length,

[0197] C12-18 dimethyl hydroxyethylammonium chloride

[0198] AE3S is C12-15 alkyl ethoxy (3) sulfate

[0199] AE7 is C12-15 alcohol ethoxylate with an average degree of ethoxylation of 7

[0200] AE9 is C12-16 alcohol ethoxylate with an average degree of ethoxylation of 9

[0201] HSAS is a mid-branched primary alkyl sulfate with a carbon chain length of about 16-17 as disclosed in US 6,020,303 and US 6,060,443

[0202] Polyacrylate MW 4500 is carboxymethylcellulose supplied by BASF V

[0203] CHEC is a cationically modified hydroxyethylcellulose polymer.

[0204] Phosphonate chelants are, for example, diethylenetriaminepentaacetic acid (DTPA) hydroxyethane diphosphonate (HEDP)

[0205] Celluclean™, and are products of Novozymes (Bagsvaerd, Denmark).

[0206] Purafect is a product of Genencor International, Palo Alto, California, USA

[0207] Optical Brightener 1 is AMS, Optical Brightener 2 is CBS-X, Direct Violet 9 is Violet BN-Z NOBS is sodium nonanoyloxybenzenesulfonate

[0208] TAED is tetraacetylethylenediamine

[0209] S-ACMC is carboxymethylcellulose conjugated with C.I. Reactive Blue 19 product name AZO-CM-CELLULOSE

[0210] Detergent is PF

[0211] The molecular weight of the acrylic / maleic copolymer is 70,000 with a ratio of acrylic to maleic of 70:30

[0212] EDDS is the sodium salt of ethylenediamine-N,N'-disuccinic acid, the (S,S) isomer of an antifoam suppressor is HSAS is a mid-branched alkyl sulfate supplied by Dow Corning, Midland, Michigan, USA

[0213] Violet CT polymeric shading dye is supplied by Milliken, Spartanburg, South Carolina, USA

[0214] Polyethoxylated azothiophene dye is Violet DDTM Polymer hueing dye, supplied by Milliken, Spartanburg, South Carolina, USA

[0215] 1 Random graft copolymer is a polyvinyl acetate grafted polyethylene oxide copolymer having a polyethylene oxide backbone and a plurality of polyvinyl acetate side chains. The polyethylene oxide backbone has a molecular weight of about 6000 and the weight ratio of polyethylene oxide to polyvinyl acetate is about 40 to 60 and has no more than 1 graft point per 50 ethylene oxide units.

[0216] 2 Polyethyleneimine (MW = 600) with 20 ethoxylate groups per -NH.

[0217] 3 Amphiphilic alkoxylated polymer is a polyethyleneimine (molecular weight = 600) prepared from a polymer derivatized to contain 24 ethoxylate groups per -NH and 16 propoxylate groups per -NH.

[0218] 4 Protease is shown as milligrams of active enzyme per 100 g of detergent.

[0219] 5 DNase is shown as milligrams of active enzyme per 100 g of detergent in all these examples. The DNase can contain trace amounts of superoxide dismutase impurities.

[0220] 6 Alginate lyase from PL7 (shown as milligrams of active enzyme per 100 g of detergent in all examples).

[0221] a Proxel GXL, 20% aqueous dipropylene glycol solution of 1,2-benzisothiazolin-3-one, supplied by Lonza.

[0222] b N,N-bis(hydroxyethyl)-N,N-dimethylammonium chloride fatty acid ester. The iodine value of the parent fatty acid of this material is between 18 and 22. The material from Evonik contains impurities in the form of free fatty acids, impurities in the form of monoester forms of N,N-bis(hydroxyethyl)-N,N-dimethylammonium chloride fatty acid ester, and impurities in the form of fatty acid esters of N,N-bis(hydroxyethyl)-N-methylamine.

[0223] c Supplied by Dow Corning, 8% active

[0224] d As described in US 8,765,659, expressed as 100% encapsulated perfume oil

[0225] e CDE, cationic polymeric thickener supplied by BASF

[0226] f N,N-dimethyl octanamide and N,N-dimethyl decanamide, in a weight ratio of about 55:45, under the trade name M-8-10 from Stepan Company

[0227] The dimensions and values disclosed herein are not to 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." SEQUENCE LISTING <110> The Procter & Gamble Company <120> Cleaning compositions comprising alginate lyase <130> CM05273M <160> 7 <170> PatentIn version 3.5 <210> 1 <211> 288 <212> PRT <213> Flavobacterium sp. <400> 1 Met Ser lie Gin Phe Ser Lys lie Leu Leu Leu Thr Val Leu Ala Thr 1 5 10 15 Ala Thr lie Ser Asn Ala Gin Asp Lys Lys Ser Lys Ser Lys Thr Ala 20 25 30 Lys lie Asp Trp Ser His Trp Thr Val Thr Val Pro Glu Glu Asn Pro 35 40 45 Asp Lys Pro Gly Lys Pro Tyr Ser Leu Gly Tyr Pro Glu lie Leu Asn 50 55 60 Tyr Ala Glu Asp Lys lie Ala Ser Lys Tyr Met Tyr Asp Asp Pro Lys 65 70 75 80 Asp Lys Ser Val Val Phe Tyr Ala Phe Pro Ser Gly Val Thr Thr Ala 85 90 95 Asn Thr His Tyr Ser Arg Ser Glu Leu Arg Glu Thr Met Glu Thr Gly 100 105 110 Ser Asn Lys Val Asn Trp Thr Phe Ala Lys Gly Gly Lys Met Arg Gly 115 120 125 Thr Tyr Ala Ile Asp Asp Ile Ser Lys Glu Pro Asp Gly Lys Tyr Ser 130 135 140 Arg Val Ile Ile Ala Gln Ile His Gly Val Leu Thr Asp Glu Gln Arg 145 150 155 160 Asp Leu Ile Gly Gln Lys Asp Asn Asn Ala Pro Pro Ile Leu Lys Val 165 170 175 Tyr Trp Asp Lys Gly Lys Ile Arg Val Lys Thr Lys Val Leu Lys Asp 180 185 190 Leu Asn Ala Pro Tyr Lys Glu Met Leu Leu Glu His Ala Trp Gly Asp 195 200 205 Asp Glu Gly Arg Asn Phe Lys Glu Lys Ile Asp Leu Asn Thr Arg Phe 210 215 220 Thr Leu Glu Val Lys Val Ser Asp Gly Arg Met Glu Val Ile Leu Asn 225 230 235 240 Asp Thr Glu Ser Leu Val Tyr Asp Asp Ile His Met Lys Lys Trp Gly 245 250 255 Ile Phe Glu Asn Tyr Phe Lys Ala Gly Asn Tyr Phe Gln Ser Lys Thr 260 265 270 Pro Gly Thr Phe Ala Lys Val Lys Ile Tyr Ser Leu Gln Val Thr His 275 280 285 <210> 2 <211> 446 <212> PRT <213> Zobellia galactanivorans <400> 2 Met Lys Lys Asn Val Phe Thr Thr Leu Arg Thr Val Val Asn Gly Asp 1 5 10 15 Ile Met Trp Lys Leu Ile Pro Val Phe Phe Leu Ala Leu Cys Leu Gly 20 25 30 Ser Cys Ser Glu Glu Pro Val Asp Pro Glu Glu Glu Ala Val Leu Thr 35 40 45 Lys Leu Ser Ala Asn Ser Thr Ala Ile Gly Ile Ser Ser Val Ser Ala 50 55 60 Ser Thr Ser Gln Ser Pro Asn Val Ala Ser Asn Thr Leu Asp Gly Ser 65 70 75 80 Thr Ser Thr Arg Trp Ser Gly Tyr Gly Asp Gly Ala Ser Ile Thr Tyr 85 90 95 Asp Leu Gly Ser Ser Ala Asn Ile Asp Tyr Val Lys Ile Ala Phe Tyr 100 105 110 Lys Gly Asp Ser Arg Lys Thr Lys Tyr Glu Val Trp Val Gly Asn Ser 115 120 125 Thr Ser Ser Leu Thr Lys Ile Lys Ser Lys Thr Ser Ser Gly Ser Thr 130 135 140 Ser Asp Tyr Glu Thr Ile Asp Leu Pro Asn Ser Thr Ala Arg Tyr Ile 145 150 155 160 Arg Ile Val Gly Lys Gly Tyr Val Leu Asn Ser Gly Gly Ser Thr Val 165 170 175 Leu Trp Asn Ser Ile Thr Lys Phe Gln Ala Trp Gly Ser Gly Gly Ser 180 185 190 Ser Thr Leu Pro Ile Ser Gly Asn Ser Pro Ala Ser Val Leu Gly Ile 195 200 205 Thr Ala Asn Thr Trp Lys Ile Asn Ser Phe Ile Gly Ser Pro Gly Ser 210 215 220 Ser Ala Thr Tyr Tyr Asp Asp Ile Thr Asp Ala Ser Gly Ile Ser Tyr 225 230 235 240 Asn Thr Tyr Ser Asp Asp Asn Tyr Phe Tyr Thr Asp Gly Glu Trp Val 245 250 255 Tyr Phe Lys Cys Tyr Arg Gly Leu Gly Gly Ser Ala Asn Ser Gln Asn 260 265 270 Pro Arg Val Glu Leu Arg Glu Met Asp Asn Gly Asn Leu Ala Ser Trp 275 280 285 Thr Gly Asp Ser Gly Thr His Thr Met Glu Trp Thr Val Gln Val Asn 290 295 300 Gln Leu Pro Gln Asp Thr Asp Gly Asp Gly Gly Val Leu Cys Phe Gly 305 310 315 320 Gln Ile His Gly Pro Ser Lys Asn Ser Asp Gly Val Glu Val Asp Asp 325 330 335 Val Val Arg Val Gln Phe Ile Gly Glu Glu Asn Gln Ser Ser Gly Ser 340 345 350 Val Lys Leu Lys Ile Ser Gly Tyr Val Thr Glu Glu Gln Gly Gly Ser 355 360 365 Gln Thr Phe Ser Gly Tyr Ser Leu Asp Thr Thr Tyr Asn Cys Lys Leu 370 375 380 Val Tyr Ser Gly Gly Tyr Val Glu Leu Phe Met Asn Gly Ser Ser Val 385 390 395 400 Phe Arg Lys Lys Met Glu Val Asp Asp Leu Ser Glu Asn Tyr Phe Lys 405 410 415 Val Gly Asn Tyr Leu Gln Ser Val Lys Gly Ala Ser Tyr Thr Gly Ser 420 425 430 Tyr Gly Leu Val Arg Ile Lys Asn Leu Ser Val Thr His Asn 435 440 445 <210> 3 <211> 611 <212> PRT <213> Glycophagus destructor degradation product <400> 3 Met Thr Phe Ile Lys Ile Met Gly Ala Gly Ala Leu Ile Ala Ser Ala 1 5 10 15 Ser Leu Ala Asn Ala Ala Thr Phe Val Leu Glu Lys Val Asn Thr Gly 20 25 30 Phe Ser Val Asp Gly Gly Asn Gly Ala Val Glu Ala Arg Gln Val Tyr 35 40 45 Leu Trp Glu Thr Asn Thr Asn Asn Val Asn Gln Asn Trp Val Gln Ile 50 55 60 Ser His Gly Gly Gly Tyr Tyr Ser Tyr Lys Lys Gln Asn Thr Asn Leu 65 70 75 80 Cys Leu Asp Gly Gly Ser Gly Gly Ala Arg Leu Gln Pro Val Thr Leu 85 90 95 Glu Val Cys Asp Ser Ser Asn Tyr Asp Gln His Trp Asn Lys Val Lys 100 105 110 Val Tyr Thr Gly Thr Glu Ile Tyr Arg Met Glu Lys Arg Asn Ala Pro 115 120 125 Gly Phe Ser Ile Asp Gly Asn Gly Gly Ala Ala Ala Arg Gln Ala Ile 130 135 140 Tyr Leu Trp Asn Ser Asn Ser Asn Asn Val Asn Gln Gln Trp Glu Phe 145 150 155 160 Ile Arg Thr Asp Glu Asp Thr Gly Asp Gly Lys Leu Ala Ile Ala Thr 165 170 175 Ala Phe Asp Asp Gly Ser Ser His Ser Ser Tyr Pro Ala Ser Lys Ala 180 185 190 Ile Asp Gly Asn Thr Ala Trp Ala Ser Arg Trp Ala Ala Ser Gly Ser 195 200 205 Pro Val Asn Leu Thr Ile Gln Leu Glu Gln Thr Ser Arg Val Thr Glu 210 215 220 Val Gly Ile Ala Trp Gly Gln Gly Gly Ser Arg Ala Tyr Thr Phe Glu 225 230 235 240 Ile Tyr Ala Arg Pro Gly Thr Ser Gly Ser Trp Thr Lys Val Phe Asp 245 250 255 Asp Val Ser Ser Gly Ser Thr Ala Gly lie Glu Val Phe Asp lie Thr 260 265 270 Asp lie Asp Ala Gin Gin lie Arg Val Lys Thr Phe Glu Asn Thr Ala 275 280 285 Gly Thr Thr Trp Thr Asn lie Thr Glu Val Glu lie Tyr Gly Ala Asp 290 295 300 Gly Gly Ser Ser Ser Ser Ser Ser Ser Ser Ser Ser Thr Ser Ser Thr 305 310 315 320 Ser Ser Thr Ser Ser Thr Ser Ser Ser Ser Gly Gly Phe Asn Leu Asn 325 330 335 Pro Asn Ala Pro Pro Ser Ser Asn Phe Asn Leu Ser Gin Trp Tyr Leu 340 345 350 Ser Val Pro Thr Asp Thr Asp Gly Ser Gly Thr Ala Asp Ser lie Lys 355 360 365 Glu Gly Glu Leu Asn Ser Gly Tyr Glu Asn Asn Ser Tyr Phe Tyr Thr 370 375 380 Gly Ser Asp Gly Gly Met Val Phe Lys Cys Pro lie Ser Gly Tyr Lys 385 390 395 400 Thr Ser Thr Gly Thr Ser Tyr Thr Arg Thr Glu Leu Arg Glu Met Leu 405 410 415 Arg Ala Gly Asn Thr Ser Ile Ala Thr Ser Gly Val Asn Lys Asn Asn 420 425 430 Trp Val Phe Gly Ser Ala Pro Ser Ser Ala Gln Ala Ala Ala Gly Gly 435 440 445 Val Asp Gly Asn Met Lys Ala Thr Leu Ala Val Asn Tyr Val Thr Thr 450 455 460 Thr Gly Asp Ser Ser Gln Val Gly Arg Val Ile Ile Gly Gln Ile His 465 470 475 480 Ala Glu Lys Asn Glu Pro Ile Arg Leu Tyr Tyr Arg Lys Leu Pro Gly 485 490 495 Asn Ser Lys Gly Gly Ile Tyr Tyr Ala His Glu Asp Ala Asp Gly Gly 500 505 510 Glu Val Trp Val Asp Met Ile Gly Ser Arg Ser Ser Ser Ala Ser Asn 515 520 525 Pro Ser Asp Gly Ile Ala Leu Asn Glu Val Phe Ser Tyr Glu Ile Asp 530 535 540 Val Thr Asn Asn Met Leu Thr Val Lys Ile Tyr Arg Asp Gly Lys Ser 545 550 555 560 Thr Val Thr Ser Gin Tyr Asn Met Val Asn Ser Gly Tyr Asp Asp Ser 565 570 575 Asp Asp Trp Met Tyr Phe Lys Ala Gly Val Tyr Asn Gin Asn Asn Thr 580 585 590 Gly Asn Gly Ser Asp Tyr Val Gin Ala Thr Phe Tyr Ser Leu Thr His 595 600 605 Thr His Asp 610 <210> 4 <211> 307 <212> PRT <213> Klebsiella pneumoniae <400> 4 Met Leu Lys Ser Gly Val Met Val Ala Ser Leu Cys Leu Phe Ser Val 1 5 10 15 Pro Ser Arg Ala Ala Val Pro Ala Pro Gly Asp Lys Phe Glu Leu Ser 20 25 30 Gly Trp Ser Leu Ser Val Pro Val Asp Ser Asp Asn Asp Gly Lys Ala 35 40 45 Asp Gin Ile Lys Glu Lys Thr Leu Ala Ala Gly Tyr Arg Asn Ser Asp 50 55 60 Phe Phe Thr Leu Ser Asp Ala Gly Gly Met Val Phe Lys Ala Pro Ile 65 70 75 80 Ser Gly Ala Lys Thr Ser Lys Asn Thr Thr Tyr Thr Arg Ser Glu Leu 85 90 95 Arg Glu Met Leu Arg Lys Gly Asp Thr Ser Ile Ala Thr Gln Gly Val 100 105 110 Ser Arg Asn Asn Trp Val Leu Ser Ser Ala Pro Leu Ser Glu Cys Lys 115 120 125 Lys Ala Gly Gly Val Asp Gly Thr Leu Glu Ala Thr Leu Ser Val Asp 130 135 140 His Val Thr Thr Thr Gly Val Asn Trp Gln Val Gly Arg Val Ile Ile 145 150 155 160 Gly Gln Ile His Ala Asn Asn Asp Glu Pro Ile Arg Leu Tyr Tyr Arg 165 170 175 Lys Leu Pro His His Gln Lys Gly Ser Val Tyr Phe Ala His Glu Pro 180 185 190 Arg Lys Gly Phe Gly Asp Glu Cys Trp Tyr Glu Met Ile Gly Thr Leu 195 200 205 Gln Pro Ser His Gly Asn Gln Thr Ala Ala Pro Thr Glu Pro Glu Ala 210 215 220 Gly Ile Ala Leu Gly Glu Thr Phe Ser Tyr Arg Ile Asp Ala Thr Gly 225 230 235 240 Asn Lys Leu Thr Val Thr Leu Met Arg Glu Gly Arg Pro Asp Val Val 245 250 255 Lys Thr Val Asp Met Ser Lys Ser Gly Tyr Ser Glu Ala Gly Gln Tyr 260 265 270 Leu Tyr Phe Lys Ala Gly Val Tyr Asn Gln Asn Lys Thr Gly Lys Pro 275 280 285 Asp Asp Tyr Val Gln Ala Thr Phe Tyr Arg Leu Lys Ala Thr His Gly 290 295 300 Ala Gln Arg 305 <210> 5 <211> 248 <212> PRT <213> Zobellia galactanivorans <400> 5 Gly Asn Ser Pro Ala Ser Val Leu Gly Ile Thr Ala Asn Thr Trp Lys 1 5 10 15 Ile Asn Ser Phe Ile Gly Ser Pro Gly Ser Ser Ala Thr Tyr Tyr Asp 20 25 30 Asp Ile Thr Asp Ala Ser Gly Ile Ser Tyr Asn Thr Tyr Ser Asp Asp 35 40 45 Asn Tyr Phe Tyr Thr Asp Gly Glu Trp Val Tyr Phe Lys Cys Tyr Arg 50 55 60 Gly Leu Gly Gly Ser Ala Asn Ser Gin Asn Pro Arg Val Glu Leu Arg 65 70 75 80 Glu Met Asp Asn Gly Asn Leu Ala Ser Trp Thr Gly Asp Ser Gly Thr 85 90 95 His Thr Met Glu Trp Thr Val Gin Val Asn Gin Leu Pro Gin Asp Thr 100 105 110 Asp Gly Asp Gly Gly Val Leu Cys Phe Gly Gin He His Gly Pro Ser 115 120 125 Lys Asn Ser Asp Gly Val Glu Val Asp Asp Val Val Arg Val Gin Phe 130 135 140 He Gly Glu Glu Asn Gin Ser Ser Gly Ser Val Lys Leu Lys He Ser 145 150 155 160 Gly Tyr Val Thr Glu Glu Gin Gly Gly Ser Gin Thr Phe Ser Gly Tyr 165 170 175 Ser Leu Asp Thr Thr Tyr Asn Cys Lys Leu Val Tyr Ser Gly Gly Tyr 180 185 190 Val Glu Leu Phe Met Asn Gly Ser Ser Val Phe Arg Lys Lys Met Glu 195 200 205 Val Asp Asp Leu Ser Glu Asn Tyr Phe Lys Val Gly Asn Tyr Leu Gin 210 215 220 Ser Val Lys Gly Ala Ser Tyr Thr Gly Ser Tyr Gly Leu Val Arg Ile 225 230 235 240 Lys Asn Leu Ser Val Thr His Asn 245 <210> 6 <211> 260 <212> PRT <213> Flavobacterium sp. <400> 6 Arg Asn Gly Ala Asn Ile Asp Leu Ser His Trp Thr Leu Thr Thr Pro 1 5 10 15 Ala Glu Asp Pro Lys Lys Pro Gly Lys Thr Phe Asp Leu Asn Tyr Pro 20 25 30 Glu Ile Phe Asp Phe Ala Ser Asn Asp Ile Ala Lys Lys Tyr Met Tyr 35 40 45 Glu Asp Pro Lys Asp Lys Ser Ile Val Phe Tyr Ala Tyr Pro Ser Gly 50 55 60 Thr Ser Thr Ala Asn Ser His Phe Ser Arg Ser Glu Leu Arg Glu Thr 65 70 75 80 Met Glu Ile Gly Ser Lys Asn Val Asn Trp Thr Phe Ala Gln Gly Gly 85 90 95 Tyr Phe Lys Gly Thr Tyr Ala Ile Glu Asp Val Ser Lys Glu Ala Asp 100 105 110 Gly Lys Tyr Ser Arg Val lie lie Ala Gin lie His Gly lie Leu Thr 115 120 125 Asp Ser Gin Gin Ala Leu lie Gly Gin Lys Asp Lys Asn Ala Ala Pro 130 135 140 lie Leu Lys lie Phe Trp Asp Gin Gly Lys lie Arg Val Lys Thr Lys 145 150 155 160 Val Leu Lys Asn Gin Asn Ala Ser Leu Lys Glu Met Leu Pro Ala Asp 165 170 175 Ala Trp Thr Asp Asp Lys Gly Arg Asp Phe Lys Glu Lys lie Asp Phe 180 185 190 Asn Thr Lys Phe Thr Leu Glu lie Lys Val Ser Asp Gly Arg Leu Glu 195 200 205 Val lie Met Asn Gly Thr Glu Ser Phe Val Tyr Glu Asp lie Asn lie 210 215 220 Lys Lys Trp Gly Val Phe Glu Asn Tyr Phe Lys Ala Gly Asn Tyr Phe 225 230 235 240 Gln Ser Thr Asn Pro Asn Thr Phe Ala Lys Val Lys lie Tyr Asp Leu 245 250 255 Gln Val Ser His 260 <210> 7 <211> 391 <212> PRT <213> Flavobacterium sp. <400> 7 Lys Leu Val Thr Thr Lys Leu Thr Pro Ala Ser Val Ser Asp Asn Gly 1 5 10 15 Asn Asp Gly Asn Val Ala Ala Asn Thr Leu Asp Gly Asn Leu Ser Thr 20 25 30 Arg Trp Ser Ser Asp Gly Ser Thr Gly Lys Tyr Ile Thr Tyr Asp Leu 35 40 45 Gly Ser Ser Lys Ser Ile Ser Ser Leu Lys Ile Ala Trp His Gln Gly 50 55 60 Asp Gln Arg Lys Ser Tyr Phe Gln Ile Arg Val Gly Asp Ser Thr Gly 65 70 75 80 Ser Leu Thr Thr Val Tyr Asp Ala Lys Thr Thr Gly Ser Ser Gly Thr 85 90 95 Thr Thr Ala Leu Glu Thr Tyr Thr Leu Ser Ser Pro Val Thr Ala Arg 100 105 110 Tyr Val Arg Ile Ser Cys Phe Gly Asn Ser Leu Thr Thr Trp Asn Ser 115 120 125 Ile Ala Glu Thr Glu Ile Tyr Ser Thr Val Asp Asp Gly Leu Pro Asp 130 135 140 Thr Tyr Pro Thr Ser Val lie Gly lie Thr Ala Asn Thr Trp Lys lie 145 150 155 160 Asn Ser Phe Thr Gly Thr Pro Gly Ser Ser Ala Val Tyr Tyr Asp Asp 165 170 175 Ile Thr Thr Ala Ser Gly Val Ser Tyr Asn Thr Tyr Asn Asp Pro Asn 180 185 190 Tyr Phe Tyr Thr Asp Gly Thr Trp Thr Tyr Phe Lys Cys Tyr Arg Gly 195 200 205 Leu Gly Thr Ser Ser Asn Ser Ser Asn Pro Arg Val Glu Leu Arg Glu 210 215 220 Leu Asn Asn Gly Ser Ser Ala Ser Trp Asp Gly Ser Val Gly Thr His 225 230 235 240 Thr Met Thr Trp Thr Val Lys Val Asp Lys Leu Pro Lys Gly Glu Asn 245 250 255 Gly Thr Thr Gly Val Leu Cys Phe Gly Gin lie His Gly Pro Ser Thr 260 265 270 Asn Ser Ser Gly Val Ala Val Asp Asp lie lie Arg Val Gin Phe Asp 275 280 285 Gly Ala Ala Asn Gin Ser Thr Gly Thr Val Lys Leu Lys lie Ser Gly 290 295 300 Tyr Ile Thr Glu Lys Val Leu Gly Gly Ser Lys Ser Phe Thr Gly Tyr 305 310 315 320 Ser Leu Gly Thr Ser Tyr Thr Phe Thr Ile Lys Tyr Thr Gly Gly Lys 325 330 335 Val Tyr Leu Tyr Asn Gly Ser Thr Leu Val Phe Ser Gln Gln Met Asp 340 345 350 Thr Ser Thr Glu Gly Asn Tyr Phe Lys Ala Gly Asn Tyr Leu Gln Ser 355 360 365 Val Lys Asn Val Ser Tyr Asp Gly Ser Tyr Gly Leu Val Gly Ile Ser 370 375 380 Ser Leu Thr Val Ser His Gln 385 390

Claims

1. A laundry detergent composition comprising 0.00005 wt% to 5 wt% alginate lyase and 1 wt% to 60 wt% anionic surfactant, wherein the alginate lyase is selected from the alginate lyases set forth in SEQ ID NOs: 1, 2, 3, 4, 5, 6, and 7 or mixtures thereof.

2. The detergent composition of claim 1, wherein the alginate lyase is of microbial origin.

3. The detergent composition of claim 1, wherein the alginate lyase is of bacterial or algal origin.

4. The detergent composition of claim 1, wherein the alginate lyase is of bacterial origin.

5. The detergent composition of any one of claims 1-4, wherein the alginate lyase is obtained from Flavobacterium sp, Sphingomonas sp, Zobellia galactanivorans.

6. The detergent composition of any one of claims 1-4, wherein the alginate lyase is obtained from Flavobacterium sp.

7. The detergent composition of any one of claims 1-4, wherein the anionic surfactant is present in an amount such that the weight ratio of surfactant to active alginate lyase protein is at least 500:

1.

8. The detergent composition of any one of claims 1-4, wherein the anionic surfactant is present in an amount such that the weight ratio of surfactant to active alginate lyase protein is at least 1000:

1.

9. The laundry detergent composition of claim 1, wherein the alginate lyase provides activity on poly(β-D-mannuronic acid) and activity on poly(α-L-guluronic acid).

10. The detergent composition of any one of claims 1-4, wherein the alginate lyase comprises two or more alginate lyases.

11. The detergent composition of any one of claims 1-4, wherein the composition additionally comprises a nonionic surfactant.

12. The detergent composition of claim 11, wherein the composition additionally comprises a nonionic surfactant in an amount of 1 wt% to 30 wt% of the composition.

13. The detergent composition of claim 11, wherein the surfactant comprises an anionic surfactant and a nonionic surfactant in a weight ratio of anionic surfactant to nonionic surfactant of 30: 1 to 1:

2.

14. The detergent composition of claim 11, wherein the surfactant comprises an anionic surfactant and a nonionic surfactant in a weight ratio of anionic surfactant to nonionic surfactant of 20: 1 to 2:

3.

15. The detergent composition of claim 11, wherein the surfactant comprises anionic surfactant and nonionic surfactant in a weight ratio of 20: 1 to 1 : 1 of anionic surfactant to nonionic surfactant.

16. The detergent composition of any one of claims 1-4, wherein the anionic surfactant comprises alkyl benzene sulfonate and / or ethoxylated alkyl sulfate.

17. The detergent composition of claim 16, wherein the ethoxylated alkyl sulfate has an ethoxylated degree of 0 to 7.

18. The detergent composition of claim 16, wherein the ethoxylated alkyl sulfate has an ethoxylated degree of 0.5 to 3.

19. The detergent composition of any one of claims 1-4, wherein the anionic surfactant comprises alkyl benzene sulfonate surfactant.

20. The detergent composition of any one of claims 1-4, comprising an additional enzyme selected from amylase, nuclease, hexosaminidase, mannanase, xanthanase, and mixtures thereof.

21. The detergent composition of claim 20, wherein the nuclease is a DNase or an RNase.

22. The detergent composition of claim 20, wherein the xanthanase is a xanthan lyase.

23. The detergent composition of any one of claims 1-4, comprising a mannanase.

24. A method of treating a fabric, the method comprising contacting a fabric with an aqueous wash liquid comprising (i) an alginate lyase; (ii) an anionic surfactant; and (iii) optionally a cleaning adjunct, wherein the alginate lyase is selected from the alginate lyases set forth in SEQ ID NOs: 1, 2, 3, 4, 5, 6, and 7 or mixtures thereof.

25. Use of a composition or method according to any one of claims 1 to 24 to improve stain removal from a fabric.

26. The use of claim 25, wherein the use is for improving cleaning of a collar or cuff.

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