Machine cleaning compositions containing enzymes

Abstract

A cleaning composition for a washing machine, comprising: (a) at least two enzymes selected from (i) an alginate lyase enzyme, (ii) a Pel-ase enzyme, (iii) a Psl-ase enzyme, (iv) a β-1,3-glucanase enzyme, and (v) a β-1,3(4)-glucanase enzyme; and (b) a cleaning adjunct.

Description

[Technical Field]

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

[0002] FIELD OF THE INVENTION The present invention relates to a machine cleaning composition that is particularly suitable for use in a dishwasher or washing machine, especially a washing machine. The present invention also relates to the use of a machine cleaner for cleaning a dishwasher or washing machine, especially a washing machine. [Background technology]

[0003] Over time, dirt accumulates within the washing machine, particularly in areas where dirt may be trapped, such as the machine's interior surfaces, filters, seals, drain area, and / or on the washing machine drum, especially on its exterior surfaces. These dirt can reduce cleaning effectiveness and produce foul odors. This problem is exacerbated by today's trend toward faster, cooler washes to address environmental concerns and the reduction in cleaning chemicals such as bleach. Under these conditions, dirt can accumulate and even lead to microbial growth. The resulting accumulated dirt, particularly dirt produced by microorganisms, can be sticky and typically contain extracellular polymeric substances (EPS), which are polymeric aggregates generally composed of, for example, extracellular DNA, proteins, and polysaccharides. These dirt can be particularly difficult to remove and can cause problems with wash and rinse water circulation, leading to poor cleaning results, including increased soil redeposition on the items being washed and on the machine's interior surfaces, as well as increased foul odors.

[0004] The use of enzymes in compositions for cleaning dishwashers is well known in the art, for example as disclosed in WO 98 / 39402. [Prior art documents] [Patent documents]

[0005] [Patent Document 1] International Publication No. 98 / 39402 Summary of the Invention [Problem to be solved by the invention]

[0006] However, there remains a need for improved means for ameliorating soil buildup within cleaning machines such as dishwashers and washing machines, particularly washing machines, and for providing cleaning to such machines. [Means for solving the problem]

[0007] The present invention provides a machine cleaning composition comprising: (a) at least two enzymes selected from (i) an alginate lyase enzyme, (ii) a Pel-ase enzyme, (iii) a Psl-ase enzyme, (iv) an endo-β-1,3-glucanase enzyme, and (v) an endo-β-1,3(4)-glucanase enzyme; and (b) a cleaning adjunct. Preferably, the composition contains 0.00005 to 5% by weight of alginate lyase enzyme (active enzyme protein), and / or 0.00005 to 5% by weight of Pel-ase (active enzyme protein), and / or 0.00005 to 5% by weight of Psl-ase (active enzyme protein), and / or 0.00005 to 5% by weight of endo-β-1,3-glucanase enzyme (active enzyme protein), and / or 0.00005 to 5% by weight of endo-β-1,3(4)-glucanase enzyme (active enzyme protein). Preferably, the composition also contains a surfactant, preferably in an amount of 1 to 60% by weight.

[0008] The present invention also provides a method of treating the interior of an automatic dishwasher and / or washing machine to prevent or remove soil buildup, the method comprising dispensing a machine cleaning composition into the interior of the machine during at least one wash cycle or at least one rinse cycle of the dishwasher or washing machine. Specifically, the method is for treating the interior of a washing machine when soil buildup and soiling properties are particularly problematic by combining cooler wash temperatures with milder detergent compositions including more neutral pH conditions to minimize fabric damage from the laundering process.

[0009] The present invention also provides a method for disintegrating soils on the interior surfaces of an automatic dishwasher or washing machine, the method comprising providing a machine cleaning composition during at least one or more wash cycles or one or more rinse cycles of the automatic dishwasher or washing machine, wherein the machine cleaning composition is present in the wash water or rinse water (aqueous wash liquor).

[0010] The present invention also provides the use of the machine cleaning composition for cleaning a washing machine, such as a washing machine and / or dishwasher, either domestic or commercial / institutional, in particular for cleaning a washing machine.

[0011] The washing machine may be at least partially loaded with items during at least one wash cycle or at least one rinse cycle. The machine cleaning composition may be used over two or more successive wash and / or rinse cycles of the washing machine.

[0012] The compositions, methods and uses of the present invention may also produce a biofilm disrupting effect and / or an anti-fouling redeposition effect. DETAILED DESCRIPTION OF THE INVENTION

[0013] definition Parent or Parent Enzyme: The term "parent" or "parent enzyme" refers to an enzyme that is modified to produce an enzyme variant. The parent may be a naturally occurring (wild-type) polypeptide or a variant thereof.

[0014] Sequence identity: The relatedness between two amino acid sequences or two nucleotide sequences is expressed by the parameter "sequence identity." For the purposes of the present invention, the degree of sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48:443-453), as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16:276-277), preferably version 3.0.0 or later. Optionally, the parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and an EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled "longest identity" (obtained using the -nobrief option) is used as the percentage identity, which is calculated as follows: (Identical residues × 100) / (length of alignment − total number of gaps in the alignment)

[0015] Alternatively, optional parameters used can be a gap opening penalty of 10, a gap extension penalty of 0.5, and an EDNAFULL (the EMBOSS version of NCBI NUC4.4) substitution matrix. The Needle output labeled "Longest Identity" (obtained using the -nobrief option) is used as the percent identity, which is calculated as follows: (identical deoxyribonucleotides × 100) / (length of alignment − total number of gaps in alignment)

[0016] Variant: The term "variant" refers to a polypeptide having enzymatic activity, which includes modifications / mutations, i.e., substitutions, insertions, and / or deletions, at one or more (e.g., several) positions relative to the parent. A substitution refers to the replacement of an amino acid occupying a position with a different amino acid, a deletion refers to the removal of an amino acid occupying a position, and an insertion refers to the addition of 1 to 3 amino acids immediately adjacent to and following the amino acid occupying a position.

[0017] Wild-type enzyme: The term "wild-type" enzyme refers to an enzyme expressed by a naturally occurring microorganism, such as a bacterium, algae, yeast, or filamentous fungus, as found in nature.

[0018] Cleaning composition for washing machines The machine cleaning composition may be in the form of a liquid or a solid. It may be in the form of a liquid or gel, or a powder or tablet, or a solid such as a liquid and / or powder enclosed in a unit dose form, for example, a water-soluble film or a water-soluble sheet (woven or non-woven fibrous sheet (unit dose pouch)). When the machine cleaning composition is in the form of a unit dose pouch, the pouch may contain single or multiple compartments, or may be divided among pouches such that the ingredients of the composition are added by adding two or more pouches, the total of the pouches used together in the washing machine adding all of the ingredients of the machine cleaning composition to the washing machine.

[0019] The machine cleaning composition comprises: (a) at least two enzymes selected from the group consisting of (i) an alginate lyase enzyme, (ii) a Pel-ase enzyme, (iii) a Psl-ase enzyme, (iv) an endo-β-1,3-glucanase enzyme, and (v) an endo-β-1,3(4)-glucanase enzyme; and (b) a cleaning adjuvant.

[0020] Alginate lyase enzyme The alginate lyase is preferably of microbial origin, preferably of bacterial or algal origin (eg, from brown seaweeds (Phaeophyceae) such as Ascophyllum, Laminara, Macrocystis), most preferably of bacterial origin. The alginate lyase enzyme can be obtained from Aeromonas sp., Azotobacter sp., Bacillus sp., Flavobacterium sp., Klebsiella sp., Pseudomonas sp., Sphingomonas sp., Vibrio sp., Zobellia galactanivorans, and most preferably Flavobacterium sp.

[0021] Preferably, the alginate lyase enzyme has at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 1; or at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, to SEQ ID NO: 2. or an alginate lyase having at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity; or having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:3. an alginate lyase having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:4; or at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90% to SEQ ID NO:5 or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:6; or an alginate lyase having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:6;The alginate lyase includes an alginate lyase having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 7; or a mixture thereof. Preferred alginate lyase enzymes include alginate lyase enzymes corresponding to the wild-type or preferably wild-type variant of any one of SEQ ID NOs: 1, 2, 3, 4, 5, 6, or 7 described herein, or a mixture thereof. SEQ ID NOs: 6, 7, and variants thereof, and mixtures thereof are particularly preferred.

[0022] Where the alginate lyase enzyme is a variant of a parent amino acid sequence, the parent alginate lyase enzyme preferably has at least 50%, or at least 60%, or at least 70%, or at least 80%, such as at least 85%, at least 90%, 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 one or more polypeptides of SEQ ID NOs: 1, 2, 3, 4, 5, 6, or 7, and has alginate lyase enzymatic activity. It may be preferred that the variant amino acid sequence differs from the parent alginate lyase by no more than 15, or no more than 10 amino acids, or no more than 5, or 4, or 3, or 2, or 1 amino acid from one or more polypeptides of SEQ ID NOs: 1, 2, 3, 4, 5, 6, or 7.

[0023] When the alginate lyase enzyme is a variant of a parent amino acid sequence, the parent can be obtained from any genus of microorganism. For purposes of the present invention, the term "obtained from," when used herein in reference to a given source, means that the parent encoded by the polynucleotide is produced by that source or by a cell into which a polynucleotide from that source has been inserted. In one aspect, the parent is secreted extracellularly. Variants can be prepared using any mutagenesis technique known in the art, such as site-directed mutagenesis, synthetic gene construction, semi-synthetic gene construction, random mutagenesis, shuffling, etc.

[0024] The alginate lyase can be from any polysaccharide lyase (PL) family, including PL5, PL6, PL7, PL14, PL15, PL17, PL18, PL32, PL34, and PL36. Preferably, the alginate lyase is from PL family 7.

[0025] Preferably, the alginate lyase enzyme has activity toward poly(beta-D-mannuronate) (poly M activity) and activity toward poly(alpha-L-guluronate) (poly G activity). The alginate lyase enzyme may comprise a single alginate lyase enzyme to provide poly M activity and poly G activity, or may comprise two or more alginate lyase enzymes that, in combination, provide poly M and poly G activity. Preferably, the alginate lyase comprises an enzyme having both poly M activity and poly G activity. Preferably, the poly M activity, as defined by Test Method 1 in the Testing 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 poly G activity, as defined by Test Method 1 in the Testing section herein, is at least 0.3 absorbance units, preferably at least 0.4 absorbance units, or at least 0.5 or even at least 0.6 absorbance units. The alginate lyase enzyme can be incorporated into the cleaning compositions and methods of the present invention in the form of a substantially pure enzyme. Alternatively, particularly where the enzyme is a variant of a wild-type enzyme, the variant is not recovered, but rather a host cell expressing the enzyme is used as the source of the alginate lyase enzyme.

[0026] The alginate lyase enzyme may be in the form of a liquid or dry composition. For example, the composition may be in the form of particles or microparticles. The alginate lyase enzyme may be stabilized according to methods known in the art, including by encapsulation.

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

[0028] Preferably, the alginate lyase enzyme is present in the aqueous cleaning liquor in an amount of from 0.01 ppm to 1000 ppm, or from 0.05 or 0.1 ppm to 750 or 500 ppm of enzyme.

[0029] Pel-ase enzyme The Pel-ase enzyme exhibits glycoside hydrolase activity on the Pel polysaccharide and preferably belongs to the endo-alpha-1,4-polygalactosminidase class of enzymes (EC 3.2.1.109) and preferably has at least 60% or 65%, or more preferably at least 70% or at least 75% or at least 80% or at least 85% or at least 90% or at least 95%, up to 100% identity to one or more of SEQ ID NOs: 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40.

[0030] Preferably, the Pel-ase glycoside hydrolase is an isolated glycoside hydrolase.

[0031] Preferably, the Pel-ase glycoside hydrolase enzyme is present in the machine cleaning composition in an amount of 0.001 to 1 wt % based on the active protein in the composition, or 0.005 to 0.5 wt % or 0.01 to 0.25 wt % based on the weight of the composition.

[0032] Preferably, the glycoside hydrolase enzyme is present in the aqueous wash liquor in an amount of from 0.01 ppm to 1000 ppm enzyme, or from 0.05 or 0.1 ppm to 750 or 500 ppm based on active protein.

[0033] The Pel-ase described herein may also produce a biofilm disrupting effect or an anti-fouling redeposition effect.

[0034] Psl-ase enzyme The Psl-ase enzyme exhibits glycoside hydrolase activity on Psl polysaccharides. Psl-ase preferably has at least 60% or 65%, or more preferably at least 70%, 75%, 80%, 85%, 90%, or 95%, up to 100%, identity to one or more of SEQ ID NOs: 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, or 52.

[0035] Preferably, the glycoside hydrolase is an isolated glycoside hydrolase.

[0036] Preferably, the Psl-ase glycoside hydrolase enzyme is present in the cleaning composition in an amount of 0.001 to 1 wt %, or 0.005 to 0.5 wt %, or 0.01 to 0.25 wt %, based on active protein.

[0037] Preferably, the Psl-ase glycoside hydrolase enzyme is present in the wash aqueous liquor in an amount of from 0.01 ppm to 1000 ppm enzyme, or from 0.05 or 0.1 ppm to 750 or 500 ppm based on active protein.

[0038] Compositions comprising the Psl-ase glycoside hydrolases described herein may also produce or be useful in biofilm disruption or soil redeposition prevention effects.

[0039] Endo-beta-1,3(4)-glucanase enzyme Endo-beta-1,3(4)-glucanase enzymes exhibit significant endo-beta-1,3-glucanase activity toward polysaccharides with an endo-beta-1,3-glucan backbone (e.g., curdlan, pachyman, laminarin, scleroglucan, schizophyllan) and toward so-called "mixed linkage" glucan polysaccharides containing both beta-1,3 and beta-1,4 linkages (e.g., those found in cereals such as oats and barley). Activity toward both of these substrates can be confirmed using Test Method 2. Endo-beta-1,3(4)-glucanase enzymes preferably belong to class EC 3.2.1.6. The endo-beta-1,3(4)-glucanase preferably has at least 60% or 65%, or more preferably at least 70% or at least 75% or at least 80% or at least 85% or at least 90% or at least 95%, up to 100%, identity to one or more of SEQ ID NOs: 53, 54, 55, 56, 57 or 58.

[0040] Endo-beta-1,3-glucanase enzyme The endo-beta-1,3-glucanase enzyme exhibits significant endo-beta-1,3-glucanase activity toward polysaccharides having an endo-beta-1,3-glucan backbone (e.g., curdlan, pachyman, laminarin, scleroglucan, schizophyllan), but has little or no activity toward so-called "mixed linkage" glucan polysaccharides containing both beta-1,3 and beta-1,4 linkages, such as those found in cereals such as oats and barley. Activity toward both of these substrates can be determined using Test Method 2. The endo-beta-1,3-glucanase enzyme preferably belongs to class EC 3.2.1.39. The endo-beta-1,3-glucanase preferably has at least 60% or 65%, or more preferably at least 70% or at least 75% or at least 80% or at least 85% or at least 90% or at least 95%, up to 100%, identity to one or more of SEQ ID NOs: 59, 60, 61, 62, 63, 64 or 65.

[0041] The machine cleaning compositions of the present invention may comprise at least an alginate lyase enzyme and a Pel-ase enzyme, and optionally additionally a Psl-ase enzyme, an endo-β-1,3-glucanase enzyme, and / or an endo-β-1,3(4)-glucanase enzyme.

[0042] The machine cleaning compositions of the present invention may comprise at least an alginate-lytic enzyme and a Psl-ase enzyme, and optionally additionally a Pel-ase enzyme, an endo-β-1,3-glucanase enzyme, and / or an endo-β-1,3(4)-glucanase enzyme.

[0043] The machine cleaning compositions of the present invention may comprise at least an alginate lyase enzyme and an endo-β-1,3-glucanase enzyme, and optionally additionally a Pel-ase enzyme, a Psl-ase enzyme, and / or an endo-β-1,3(4)-glucanase enzyme.

[0044] The machine cleaning compositions of the present invention may comprise at least an alginate lyase enzyme and an endo-β-1,3(4)-glucanase enzyme, and optionally additionally a Pel-ase enzyme, a Psl-ase enzyme, and / or an endo-β-1,3-glucanase enzyme.

[0045] The machine cleaning compositions of the present invention may comprise at least Pel-ase and Psl-ase enzymes, and optionally additionally alginate lyase enzymes, endo-β-1,3-glucanase enzymes, and / or endo-β-1,3(4)-glucanase enzymes.

[0046] The machine cleaning compositions of the present invention may comprise at least Pel-ase and endo-β-1,3-glucanase enzymes, and optionally additionally alginate lyase enzyme, Psl-ase enzyme, and / or endo-β-1,3(4)-glucanase enzyme.

[0047] The machine cleaning compositions of the present invention may comprise at least Pel-ase and endo-β-1,3(4) glucanase enzymes, and optionally additionally Psl-ase, endo-β-1,3-glucanase, and / or alginate lyase enzymes.

[0048] The machine cleaning compositions of the present invention may comprise at least a Psl-ase enzyme and an endo-β-1,3-glucanase enzyme, and optionally additionally a Pel-ase enzyme, an alginate lyase enzyme, and / or an endo-β-1,3(4)-glucanase enzyme.

[0049] The machine cleaning compositions of the present invention may comprise at least Psl-ase and endo-β-1,3(4)-glucanase enzymes, and optionally additionally Pel-ase, endo-β-1,3-glucanase, and / or alginate lyase enzymes.

[0050] The machine cleaning compositions of the present invention may comprise at least an endo-β-1,3-glucanase enzyme and an endo-β-1,3(4)-glucanase enzyme, and optionally additionally a Pel-ase enzyme, a Psl-ase enzyme, and / or an alginate lyase enzyme.

[0051] The machine cleaning composition includes a cleaning adjunct. Typically, the cleaning adjunct is present in the composition in an amount of 1 to 98.9% by weight, more typically 5 to 90% by weight of the cleaning adjunct. Suitable cleaning adjuncts include surfactants, builders, bleaching agents, colorants, chelating agents, dispersants, additional enzymes and enzyme stabilizers, catalytic materials, preformed peracids, polymeric dispersants, mud stain removers / anti-redeposition agents, filler salts, hydrotropes, suds suppressors, structure extenders, preservatives, antioxidants, bactericides, mildew inhibitors, anti-tarnish agents, corrosion inhibitors, alkalinity sources, solubilizers, carriers, processing aids, pigments, dyes, fragrances, and pH adjusters, encapsulating agents, polymers, and mixtures thereof.For example, these include bleaching agents such as bleach activators, bleach accelerators such as imine bleach accelerators, bleach catalysts, hydrogen peroxide, hydrogen peroxide sources such as percarbonates and / or perborates, especially percarbonates coated with materials such as carbonates and / or sulfates, silicates, borosilicates, and any mixtures thereof, preformed peracids, including encapsulated preformed peracids, transition metal catalysts; foam suppressors or foam suppressor systems, for example, silicone-based foam suppressors and / or fatty acid-based foam suppressors; flocculating agents such as polyethylene oxide; soil dispersants and soil anti-redeposition aids such as alkoxylated polyamines and ethoxylated ethyleneimine polymers; anti-redeposition components such as polyesters; carboxylate polymers, for example, maleic acid polymers or copolymers of maleic acid and acrylic acid; fragrances, for example, fragrance microcapsules, starch-encapsulated accords, fragrance propellants; cosmetic particles; aesthetic The composition may include dyes; fillers such as sodium sulfate and / or citrus fibers (although it may be preferable for the composition to be substantially filler-free); silicates such as sodium silicate, including 1.6R and 2.0R sodium silicate, or sodium metasilicate; copolyesters of dicarboxylic acids and diols; cellulosic polymers such as methylcellulose, carboxymethylcellulose, hydroxyethoxycellulose, or other alkyl or alkylalkoxycelluloses; solvents such as 1,2 propanediol, monoethanolamine; diethylene glycol, ethanol, and any mixtures thereof; hydrotropes such as sodium cumene sulfonate, sodium xylene sulfonate, sodium toluene sulfonate, and any mixtures thereof; organic acids and their salts, such as citric acid / citrates; and any combinations thereof. The composition may be such that the cleaning adjunct preferably comprises one or more selected from the group consisting of (i) surfactants, (ii) additional enzymes, (iii) suds suppressors, (iv) enzyme stabilizers, (v) solvents, and (vi) mixtures thereof. The composition may also contain a bleaching agent component.

[0052] The inventors have found that while enzyme combinations provide good soil degradation, the presence of a surfactant can improve removal of the substrate and the soil degradation products it contains. Therefore, the machine cleaning composition preferably contains a surfactant, which may be selected from anionic, nonionic, zwitterionic, amphoteric, and cationic surfactants, preferably anionic surfactants, nonionic surfactants, and mixtures thereof, preferably in an amount of 1 to 60% by weight. Nonionic surfactants are particularly preferred. The composition may be substantially free of anionic surfactants.

[0053] Preferably, the weight ratio of surfactant to either total active enzyme protein or active enzyme protein of each of the at least two enzymes is at least 500:1, preferably at least 1000:1, or at least 1500:1, or at least 2000:1, preferably not more than 500,000:1, preferably not more than 400,000:1, or not more than 200,000:1, or at most 150,000:1, or 100,000:1, or 50,000:1, or 10,000:1. Preferably, the weight ratio of surfactant to active enzyme protein is at least 500:1, preferably at least 1000:1 or at least 1500:1 or at least 2000:1, preferably not more than 500,000:1, preferably not more than 400,000:1, or not more than 200,000:1, or up to 150,000:1, or 100,000:1, or 50,000:1, or 10,000:1.

[0054] Preferred anionic surfactants are sulfonate and sulfate surfactants, preferably alkylbenzene sulfonates and / or (optionally alkoxylated) alkyl sulfates. Particularly preferred anionic surfactants include linear alkylbenzene sulfonates (LAS). Preferred alkyl sulfates include alkyl ether sulfates, particularly C9-15 alcohol ether sulfates, especially those having an average degree of ethoxylation of 0.5-7, preferably 1-5; C8-C16 ester sulfates; and C10-C14 ester sulfates, such as monododecyl ester sulfate. In preferred compositions, the anionic surfactant comprises an alkylbenzene sulfonate and, optionally, an ethoxylated alkyl sulfate, preferably having an ethoxylation degree of 0-7, more preferably 0.5-3.Isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefinsulfonates, alkenesulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS), such as sodium dodecyl sulfate (SDS), fatty alcohol sulfate (FAS), primary alcohol sulfate (PAS), alcohol ether sulfate (primary alcohol sulfate, AES or alcohol ethoxy sulfate, AEOS or fatty alcohol ether sulfate, FES, also known as alcohol ethoxy sulfate or fatty alcohol ether sulfate), secondary alkanesulfonates (SAS), paraffin sulfonates, Also suitable anionic surfactants are sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid methyl esters (alpha-SFMe or SES) (including methyl ester sulfonates (MES)), alkyl- or alkenyl succinic acids, dodecenyl / tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfosuccinic acid, or salts of fatty acids (soaps), and combinations thereof.

[0055] When present, anionic surfactants are preferably added to machine cleaning compositions in the form of their salts. Preferred cations are alkali metal ions, such as sodium and potassium. However, salt forms of anionic surfactants may also be formed in situ by neutralizing the acid form of the surfactant with an alkali, such as sodium hydroxide, or an amine, such as mono-, di-, or triethanolamine. The compositions may contain 1 to 60%, or 1 to 50%, or 2, or 5 to 40% by weight of the composition of anionic surfactant. The surfactant preferably comprises a surfactant system comprising an anionic surfactant and one or more additional surfactants, which may be nonionic, including semi-polar and / or cationic and / or zwitterionic and / or amphoteric and / or semi-polar nonionic and / or mixtures thereof.

[0056] The present invention also provides a machine cleaning composition comprising 0.00005 to 5% by weight (active enzyme protein) of each of at least two enzymes and a surfactant, the surfactant comprising an anionic surfactant and a nonionic surfactant, preferably in a weight ratio of anionic to nonionic of 30:1 to 1:2, preferably 20:1 to 2:3 or 1:1.

[0057] Suitable nonionic 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, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (FAD ... Examples of suitable nonionic surfactant cleaners include N-acyl N-alkyl derivatives of polyhydroxyalkyl fatty acid amides or glucosamine (glucamide, GA, or fatty acid glucamide, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof. Alcohol ethoxylates are particularly preferred, preferably having C9-18 or preferably C12-15 alkyl chains, and preferably having an average degree of ethoxylation of 3-9, more preferably 3-7. Commercially available nonionic surfactant cleaners include Plurafac™, Lutensol™, and Pluronic™ from BASF, the Dehypon™ series from Cognis, and the Genapol™ series from Clariant.

[0058] The machine cleaning composition preferably comprises from 0.5% to about 40% by weight of a nonionic surfactant, preferably from 1 to 30% by weight of the composition.

[0059] The machine cleaning composition preferably comprises one or more additional enzymes. Thus, preferred compositions comprise one or more additional enzymes selected from the group consisting of aminopeptidases, amylases, carbohydrases, carboxypeptidases, catalases, cellulases, chitinases, cutinases, cyclodextrin glycosyltransferases, esterases, alpha-galactosidases, beta-galactosidases, glucoamylases, alpha-glucosidases, beta-glucosidases, haloperoxidases, hexosaminidases, invertases, laccases, lipases, mannanases, mannosidases, nucleases, oxidases, pectinolytic enzymes, peptidoglutaminases, peroxidases, phytases, polyphenol oxidases, proteolytic enzymes, transglutaminases, xylanases, xanthan lyases, xanthanases, and mixtures thereof. Preferably, the cleaning composition comprises an additional enzyme selected from a nuclease such as a DNase or an RNase, a mannanase, a xanthan lyase, a xanthanase, an amylase, and mixtures thereof.

[0060] The composition preferably comprises an additional enzyme selected from xanthan lyase, xanthanase, mannanase, and mixtures thereof, with mannanase being particularly preferred.

[0061] The additional enzyme may be derived from, for example, Aspergillus species, such as Aspergillus aculetus, Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger, or Aspergillus oryzae; Fusarium species, such as Fusarium bactridioides, Fusarium cerealis, Fusarium cloacaelensis, or Fusarium culmorum. Fusarium, Fusarium graminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negunji, Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusarium sambusinum, Fusarium sarcochromium, Fusarium sulphureum, Fusarium torulosum, Fusarium trichothesioides, or Fusarium bennitum; Humicola, for example Humicola insolens insolens, or Humicola lanuginosa; or Trichoderma, for example, Trichoderma harzianum, Trichoderma koningii, Trichoderma longibrachiatum, Trichoderma reesei, or Trichoderma viride.

[0062] Preferably, the composition comprises a protease or a mixture of two or more proteases, a lipase or a mixture of two or more lipases, a peroxidase or a mixture of two or more peroxidases, one or more starch-degrading enzymes, such as alpha-amylase, glucoamylase, maltogenic amylase, and / or cellulase or a mixture thereof.

[0063] Generally, the properties of the selected enzyme should be compatible with the selected detergent (i.e., pH optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme should be present in an effective amount. Preferably, the products of the present invention contain at least 0.01 mg, preferably from about 0.05 to about 10 mg, more preferably from about 0.1 to about 6 mg, and especially from about 0.2 to about 5 mg of additional active enzyme per gram of composition.

[0064] Protease: The compositions of the present invention preferably include a protease. A mixture of two or more proteases can contribute to improved cleaning over a wider temperature, cycle duration, and / or substrate range. Suitable proteases include metalloproteases and serine proteases, including, for example, neutral or alkaline microbial serine proteases such as subtilisin (EC 3.4.21.62). Suitable proteases include those of animal, vegetable, or microbial origin. In one aspect, such suitable proteases may be of microbial origin. Suitable proteases include chemically or genetically modified variants of the aforementioned suitable proteases. In one aspect, suitable proteases may be serine proteases, such as alkaline microbial proteases and / or trypsin-type proteases. Examples of suitable neutral or alkaline proteases include:

[0065] Subtilisins (EC3.4.21.62), in particular those described in International Publication Nos. 2004067737, 2015091989, 2015091990, 2015024739, and 2015143360, U.S. Patent Nos. 6,312,936(B1), 5,679,630, and 4,760,025, and German Patent Application Publication No. 102006022216(B1), Bacillus species described in International Publication Nos. 2015089447, 2015089441, 2016066756, 2016066757, 2016069557, 2016069563, 2016069569, and 2016174234. Those derived from the genus Bacillus, such as Bacillus sp., B. lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, B. pumilus, B. gibsonii, and B. akibaii, specifically those with the mutations S9R, A15T, V66A, A188P, V199I, Q239R, and N255D (savinase numbering system).

[0066] Trypsin- or chymotrypsin-type proteases such as trypsin (e.g., of porcine or bovine origin), including the Fusarium proteases described in WO 89 / 06270, and the chymotrypsin proteases from Cellulomonas described in WO 05 / 052161 and WO 05 / 052146.

[0067] Metalloproteases, in particular those from Bacillus amyloliquefaciens as described in WO 07 / 044993(A2), those from Bacillus, Brevibacillus, Thermoactinomyces, Geobacillus, Paenibacillus, Lysinibacillus or Streptomyces spp. as described in WO 2014194032, WO 2014194054 and WO 2014194117, those from Kribella aluminosa as described in WO 2015193488, alluminosa, and those derived from the genera Streptomyces and Lysobacter as described in WO 2016075078.

[0068] A protease having at least 90% identity to the subtilase from Bacillus sp. TY145, NCIMB40339, described in WO 92 / 17577 (Novozymes A / S), including variants of the Bacillus sp. TY145 subtilase described in WO 2015024739 and WO 2016066757.

[0069] Particularly preferred proteases for the cleaning compositions of the present invention have at least 90%, preferably at least 95%, more preferably at least 98%, even more preferably at least 99%, especially 100% identity to the wild-type enzyme from Bacillus lentus and have the following positions: S9R, A15T, V68A, N76D, N87S, S99D, S99SD, S99A, S101G, S101M, S103A, V104N / I, G118V, G and / or M222S (using the BPN' numbering system and amino acid abbreviations exemplified in WO 00 / 37627, incorporated herein by reference).

[0070] Most preferably, the protease is selected from the group of proteases comprising the following mutations (BPN numbering system) relative to either PB92 wild type (SEQ ID NO: 2 of WO 08 / 010925) or subtilisin 309 wild type (sequence according to the PB92 backbone but containing the natural mutation N87S): (i) G118V + S128L + P129Q + S130A (ii)S101M+G118V+S128L+P129Q+S130A (iii)N76D+N87R+G118R+S128L+P129Q+S130A+S188D+N248R (iv)N76D+N87R+G118R+S128L+P129Q+S130A+S188D+V244R (v)N76D+N87R+G118R+S128L+P129Q+S130A (vi) V68A+N87S+S101G+V104N (vii)S99AD (viii)S9R+A15T+V68A+N218D+Q245R

[0071] Suitable commercially available protease enzymes include those sold by Novozymes A / S (Denmark) under the trade names Alcalase®, Savinase®, Primase®, Durazym®, Polarzyme®, Kannase®, Liquanase®, Liquanase Ultra®, Savinase Ultra®, Ovozyme®, Neutrase®, Everlase®, Coronase®, Blaze®, Blaze Ultra® and Esperase®; and those sold under the trade names Maxatase®, Maxacal®, Maxapem®, Properase®, Purafect®, Purafect Prime®, Purafect Ox®, FN3®, FN4®, Excellase®, Ultimase® and Purafect those sold by DuPont under the trade names Opticlean® and Optimase® by Solvay Enzymes; and those available from Henkel / Kemira, namely, BLAP (the sequence of which is shown in Figure 29 of U.S. Pat. No. 5,352,604 and which has the mutations S99D+S101R+S103A+V104I+G159S, hereinafter referred to as BLAP), BLAP R (BLAP with S3T+V4I+V199M+V205I+L217D), BLAP X (BLAP with S3T+V4I+V205I) and BLAP F49 (BLAP with S3T+V4I+A194P+V199M+V205I+L217D); and KAP (Bacillus alkalophilus subtilisin with the mutations A230V+S256G+S259N) from Kao.

[0072] Commercially available proteases selected from the group consisting of Properase®, Blaze®, Ultimase®, Everlase®, Savinase®, Excellase®, Blaze Ultra®, BLAP and BLAP variants are particularly preferred for use herein.

[0073] Preferred concentrations of protease in the products of the present invention include about 0.05 to about 10, more preferably about 0.5 to about 7, and especially about 1 to about 6 mg of active protease per gram of composition.

[0074] Lipase: The composition preferably comprises a lipase. The presence of oils and / or fats can further increase the recovery of stains containing mannans and other polysaccharides. Therefore, the presence of lipase in the enzyme package can further improve the removal of such stains. Suitable lipases include those of bacterial, fungal or synthetic origin, including chemically modified or genetically engineered variants of the protein. Examples of useful lipases include lipases from the genus Humicola (also known as Thermomyces), such as H. lanuginosa (T. lanuginosus) or H. insolens; lipases from the genus Pseudomonas, such as P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. stutzeri, P. fluorescens, Pseudomonas sp. SD705, and P. wisconsinensis; lipases from B. subtilis (Dartois et al. (1993), Biochemica et Biophysica Acta, 1131, 253-360), B. stearothermophilus, or B. pumilus.

[0075] The lipase may be a "first cycle lipase" as described in U.S. Patent No. 6,939,702 (B1) and U.S. Patent Application Publication No. 2009 / 0217464. In one aspect, the lipase is a first wash lipase, preferably a variant of the wild-type lipase from Thermomyces lanuginosus, containing the T231R and N233R mutations. The wild-type sequence is Swiss-Prot Accession No. Swiss-Prot O59952 (269 amino acids (amino acids 23-291) from Thermomyces lanuginosus (Humicola lanuginosa)). Preferred lipases include those sold under the tradenames Lipex®, Lipolex®, and Lipoclean®.

[0076] Other suitable lipases include Liprl139, as described, for example, in WO 2013 / 171241; TfuLip2, as described, for example, in WO 2011 / 084412 and WO 2013 / 033318; Pseudomonas stutzeri lipase, as described, for example, in WO 2018228880; Microbulbifer thermotolerans lipase, as described, for example, in WO 2018228881; Sulfobacillus acidocaldarius lipase, as described, for example, in EP 3299457; acidocaldarius lipases, such as LIP062 lipase as described in WO2018209026, PinLip lipase as described in WO2017036901, and Absidia species lipases as described in WO2017005798.

[0077] Suitable lipases are (a) Substitution T231R (b) Substitution N233R or N233C (c) a variant of SEQ ID NO: 5 comprising at least three additional substitutions selected from E1C, D27R, N33Q, G38A, F51V, G91Q, D96E, K98L, K98I, D111A, G163K, H198S, E210Q, Y220F, D254S, I255A, and P256T; wherein the positions correspond to those of SEQ ID NO: 5, the lipase variant has at least 90% but less than 100% sequence identity with a polypeptide having the amino acid sequence of SEQ ID NO: 5, and the variant has lipase activity.

[0078] One preferred lipase is a variant of SEQ ID NO:5 containing the following substitutions: T231R, N233R, D27R, G38A, D96E, D111A, G163K, D254S, and P256T.

[0079] One preferred lipase is a variant of SEQ ID NO:5 containing the following substitutions: T231R, N233R, N33Q, G91Q, E210Q, I255A.

[0080] Suitable lipases are commercially available from Novozymes, for example as Lipex Evity 100L, Lipex Evity 200L (both liquid ingredients) and Lipex Evity 105T (granules), which have a different structure to the products Lipex 100L, Lipex 100T and Lipex Evity 100T, which are outside the scope of the present invention.

[0081] Cellulase: Suitable cellulases include cellulases of bacterial or fungal origin, including chemically modified or genetically engineered variants of proteins. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, such as fungal cellulases produced by Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum, as disclosed in U.S. Patent Nos. 4,435,307, 5,648,263, 5,691,178, 5,776,757, and 5,691,178.

[0082] In one aspect, preferred enzymes include endoglucanases derived from microorganisms that exhibit endo-beta-1,4-glucanase activity (EC 3.2.1.4), preferably selected from the group comprising: (a) a bacterial polypeptide endogenous to a member of the genus Bacillus having a sequence that is at least 90%, 94%, 97%, or even 99% identical to the amino acid sequence of SEQ ID NO:2 in U.S. Patent No. 7,141,403(B2), with preferred substitutions including one or more positions corresponding to positions 292, 274, 266, 265, 255, 246, 237, 224, and 221 of the mature polypeptide of SEQ ID NO:2, wherein the variant has cellulase activity; (b) a glycosyl hydrolase having enzymatic activity on both xyloglucan and amorphous cellulose substrates, the glycosyl hydrolase being selected from GH family 5, 7, 12, 16, 44, or 74; (c) glycosyl hydrolases having a sequence that is at least 90%, 94%, 97%, and even 99% identical to the amino acid sequence of SEQ ID NO: 3 of WO 09 / 148983; (d) A variant exhibiting at least 70% identity to SEQ ID NO: 5 in WO2017106676. Preferred substitutions include one or more positions corresponding to positions 4, 20, 23, 29, 32, 36, 44, 51, 77, 80, 87, 90, 97, 98, 99, 102, 112, 116, 135, 136, 142, 153, 154, 157, 161, 163, 192, 194, 204, 208, 210, 212, 216, 217, 221, 222, 225, 227, and 232; (e) and mixtures thereof.

[0083] Suitable endoglucanases are sold under the trade names Celluclean® and Whitezyme® (Novozymes A / S, Bagsvaerd, Denmark). Examples include Celluclean® 5000L, Celluclean® Classic 400L, Celluclean® Classic 700T, Celluclean® 4500T, Whitezyme® 1.5T, and Whitezyme® 2.0L.

[0084] Other commercially available cellulases include Celluzyme®, Carezyme®, Carezyme® Premium (Novozymes A / S), Clazinase®, Puradax HA®, Revitalenz® 1000, Revitalenz® 2000 (Genencor International Inc.), KAC-500® (Kao Corporation), Biotouch® FCL, Biotouch® DCL, Biotouch® DCC, Biotouch® NCD, Biotouch® FCC, Biotouch® FLX1 (AB Enzymes).

[0085] Suitable glucanases include endo-β-1,3-glucanases, preferably from EC class 3.2.1.39, preferably obtained from microorganisms of the genus Paenibacillus, Zobellia galactanivorans, Thermotoga petrophila, or Trichoderma, preferably Paenibacillus or Zobellia galactanivorans, most preferably Paenibacillus.

[0086] Amylase: Preferably, the compositions of the present invention comprise an amylase. Suitable alpha-amylases include those of bacterial or fungal origin, including chemically or genetically modified variants. Preferred alkaline alpha-amylases are derived from Bacillus species, such as Bacillus licheniformis, Bacillus amyloliquefaciens, Bacillus stearothermophilus, Bacillus subtilis, or other Bacillus species, such as Bacillus species NCBI 12289, NCBI 12512, NCBI 12513, DSM 9375 (U.S. Pat. No. 7,153,818), DSM 12368, DSM Z No. 12649, KSM AP1378 (WO 97 / 00324), KSM K36, or KSM K38 (EP 1,022,334). Preferred amylases include: (a) Variants described in U.S. Pat. No. 5,856,164 and WO 99 / 23211, WO 96 / 23873, WO 00 / 60060, WO 06 / 002643, and WO 2017 / 192657, in particular the following positions relative to the AA560 enzyme described as SEQ ID NO: 12 in WO 06 / 002643: and one or more substitutions at positions 26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193, 202, 214, 231, 246, 256, 257, 258, 269, 270, 272, 283, 295, 296, 298, 299, 303, 304, 305, 311, 314, 315, 318, 319, 339, 345, 361, 378, 383, 419, 421, 437, 441, 444, 445, 446, 447, 450, 461, 471, 482, 484, preferably D183. * and G184 * Variants that also contain deletions. (b) variants exhibiting at least 85%, preferably 90%, identity with SEQ ID NO: 4 in WO 06 / 002643, the wild-type enzyme from Bacillus sp. SP722, in particular variants in which positions 183 and 184 are deleted, and variants described in WO 00 / 60060, WO 2011 / 100410 and WO 2013 / 003659, in particular the following positions relative to SEQ ID NO: 4 in WO 06 / 002643, which are incorporated herein by reference: those with one or more substitutions at positions 51, 52, 54, 109, 304, 140, 189, 134, 195, 206, 243, 260, 262, 284, 347, 439, 469, 476, and 477. (c) Variants exhibiting at least 90% identity to the wild-type enzyme from Bacillus sp. 707 (SEQ ID NO: 7 in U.S. Pat. No. 6,093,562), particularly those containing one or more of the following mutations: M202, M208, S255, R172, and / or M261. Preferably, the amylase contains one or more of M202L, M202V, M202S, M202T, M202I, M202Q, M202W, S255N, and / or R172Q. Particularly preferred are those containing the M202L or M202T mutation. Additional relevant mutations / deletions based on the SP707 backbone are W48, A51, V103, V104, A113, R118, N125, V131, T132, E134, T136, E138, R142, S154, V165, R182, G182, H183, E190, D192, T193, I206, M208, D209, E212, V213, V214, N215, L217, R218, N219 Includes 9, V222, T225, T227, G229, I235, K242, Y243, S244, F245, T246, I250, S255, A256, H286, V291, T316, V317, V318, N417, T418, A419, H420, P421, I428, M429, F440, R443, N444, K445, Q448, S451, A465, N470, S472. (d) a variant described in WO 09 / 149130, preferably SEQ ID NO: 1 or SEQ ID NO: 2 in WO 09 / 149130, which shows at least 90% identity to the wild-type enzyme from Geobacillus Stearophermophilus, or a truncated version thereof. (e) a variant described in WO 10 / 115021, in particular SEQ ID NO: 2 in WO 10 / 115021, which exhibits at least 75%, or at least 85%, or at least 90%, or at least 95% identity with the alpha-amylase from Bacillus sp. TS-23. (f) Variants exhibiting at least 89% identity to SEQ ID NO: 1 in WO2016091688, in particular those containing a deletion at positions H183+G184 and further containing one or more mutations at positions 405, 421, 422, and / or 428. (g) Variants described in WO2014099523, in particular those exhibiting at least 60% amino acid sequence identity with "PcuAmyl α-amylase" from Paenibacillus curdlanolyticus YK9 (SEQ ID NO: 3 in WO2014099523). (h) Variants described in WO2014099523, in particular "CspAmy2 amylase" from Cytophaga species (showing at least 60% amino acid sequence identity with SEQ ID NOs: 1 and 6 in WO2014164777, in particular those containing one or more of the following deletions and / or mutations based on SEQ ID NO: 1 in WO2014164777: R178 * , G179 * , T38N, N88H, N126Y, T129I, N134M, F153W, L171R, T180D, E187P, I203Y, G476K, G477E, Y303D. (i) A variant showing at least 85% identity with Bacillus subtilis (SEQ ID NO: 1 in WO 2009149271). (j) A variant showing at least 90% identity with the wild-type amylase derived from Bacillus sp. KSM-K38 under accession number AB051102. (k) variants described in WO2016180748, in particular those exhibiting at least 80% identity with the mature amino acid sequence of AAI10 from Bacillus species as set forth in SEQ ID NO: 7 in WO2016180748; those exhibiting at least 80% identity with the mature amino acid sequence of amylase from Alicyclobacillus species as set forth in SEQ ID NO: 8 in WO2016180748, and those exhibiting at least 80% identity with the mature amino acid sequence of SEQ ID NO: 13 in WO2016180748, in particular those having the following mutations: * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G184T, N195F, V206L, K391A, P473R, G476K. (l) Variants described in WO2018060216, in particular variants exhibiting at least 70% identity to the mature amino acid sequence of SEQ ID NO: 4 in WO2018060216, fusion molecules of Bacillus amyloliquefaciens and Bacillus licheniformis. In particular, those containing one or more substitutions at positions H1, N54, V56, K72, G109, F113, R116, T134, W140, W159, W167, Q169, Q172, L173, A174, R181, G182, D183, G184, W189, E194, N195, V206, G255, N260, F262, A265, W284, F289, S304, G305, W347, K391, Q395, W439, W469, R444, F473, G476, and G477.

[0087] A preferred amylase is a genetically engineered enzyme in which one or more amino acids susceptible to bleaching oxidation are replaced with amino acids less susceptible to oxidation. Specifically, methionine residues are preferably replaced with any other amino acid. Specifically, the methionine most susceptible to oxidation is preferably replaced. Preferably, the methionine at position 202 in SEQ ID NO: 11 is replaced. Preferably, the methionine at this position is replaced with threonine or leucine, preferably leucine.

[0088] Suitable commercially available alpha-amylases include DURAMYL®, LIQUEZYME®, TERMAMYL®, TERMAMYL ULTRA®, NATALASE®, SUPRAMYL®, STAINZYME®, STAINZYME PLUS®, FUNGAMYL®, ATLANTIC®, ACHIEVE ALPHA®, AMPLIFY® PRIME, INTENSA®, and BAN® (Novozymes A / S, Bagsvaerd, Denmark), KEMZYM® AT9000 (Biozym Biotech Trading GmbH, Wehlistrasse 27b A-1200 Wien, Austria), RAPIDASE®, PURASTAR®, ENZYSIZE®, OPTISIZE HT PLUS®, POWERASE®, and PREFERENZ. Examples include the S (registered trademark) series (including PREFERENZ S1000 (registered trademark) and PREFERENZ S2000 (registered trademark)), PURASTAR OXAM (registered trademark) (DuPont, Palo Alto, California), and KAM (registered trademark) (Kao, 14-10 Nihonbashi Kayabacho, 1-chome, Chuo-ku, Tokyo 103-8210, Japan).

[0089] Preferably, the composition contains at least 0.01 mg, preferably about 0.05 to about 10, more preferably about 0.1 to about 6, especially about 0.2 to about 5 mg of active amylase per gram of composition.

[0090] Peroxidases / Oxidases: Suitable peroxidases / oxidases include those of plant, bacterial, or fungal origin, including chemically modified or genetically engineered variants of the protein. Examples of useful peroxidases include peroxidases from the genus Coprinus, such as those from C. cinereus and variants thereof, as described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257.

[0091] Commercially available peroxidases include GUARDZYME® (Novozymes A / S).

[0092] Pectate lyases: Suitable pectate lyases include those sold under the trade names Pectawash®, Pectaway®, X-Pect® (all Novozymes A / S, Bagsvaerd, Denmark) and Preferenz® F1000 (DuPont Industrial Biosciences).

[0093] Mannanase. The composition preferably contains one or more additional mannanase enzymes. As used herein, the term "mannanase" or "galactomannanase" refers to a mannanase enzyme, defined in accordance with what is known in the art as mannan endo-1,4-beta-mannosidase, also known as beta-mannanase and endo-1,4-mannanase, that catalyzes the hydrolysis of 1,4-beta-D-mannosidic linkages in mannans, galactomannans, glucomannans, and galactoglucomannans. Mannanases are classified as EC 3.2.1.78 according to enzyme nomenclature and belong to glycosyl hydrolase families 5, 26, and 113. Many suitable mannanases belong to glycosyl hydrolase family 5. Commercially available mannanases include those sold under the trade name Mannaway® (Novozymes A / S), such as Mannaway® 200L and Mannaway Evity 4.0T. Other commercially available mannanases include Effectenz® M1000, Mannastar® 375, Preferenz M100, and Purabrite® (all from DuPont Industrial Biosciences) and Biotouch M7 (AB Enzymes). Other suitable mannanases belong to glycosyl hydrolase family 26, such as those described in WO 2018191135, WO 2015040159, WO 2017021515, WO 2017021516, WO 2017021517, and WO 2019081515. Suitable mixtures of mannanases include the combination of glycosyl hydrolase family 5 mannanase and glycosyl hydrolase family 26 mannanase described in WO 2019081515.

[0094] Nuclease: Preferably, the composition comprises a nuclease enzyme, such as RNase or DNase, or a mixture thereof. A nuclease enzyme is an enzyme capable of cleaving phosphodiester bonds between nucleotide subunits of nucleic acids. The nuclease enzyme herein is preferably a deoxyribonuclease or ribonuclease enzyme, or a functional fragment thereof. A functional fragment or portion refers to a portion of a nuclease enzyme that catalyzes the cleavage of phosphodiester bonds in the DNA backbone, and thus is a region of the nuclease protein that retains catalytic activity. It therefore includes truncated but functional versions of the enzyme and / or variants and / or derivatives and / or homologs in which functionality is maintained.

[0095] Preferably, the nuclease enzyme is a deoxyribonuclease preferably selected from any of the following classes: EC 3.1.21.x (wherein x=1, 2, 3, 4, 5, 6, 7, 8 or 9), EC 3.1.22.y (wherein y=1, 2, 4 or 5), EC 3.1.30.z (wherein z=1 or 2), EC 3.1.31.1, and mixtures thereof.

[0096] DNases: Suitable DNases include those set forth in SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, and 9 of WO 2017162836 (Novozymes) and SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 of WO 2018108865, DNase wild-type and mutant forms defined by 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, and 54, as well as mutant forms of Bacillus cibi DNase, including those described in International Publication No. 2018011277 (Novozymes), which are incorporated herein by reference. Preferred DNases are as claimed in European Patent No. 3476935(A).

[0097] RNases: Suitable RNases include wild-type and variants of DNases defined by SEQ ID NOs: 3, 6, 9, 12, 15, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 72 and 73 of WO2018178061 (Novozymes), and SEQ ID NOs: 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103 and 104 of WO2020074499 (Novozymes), which are incorporated herein by reference.

[0098] Hexosaminidase: The present compositions preferably additionally comprise one or more hexosaminidase enzymes. The term hexosaminidase includes "dispersant" and the abbreviation "Dsp" and refers to a polypeptide having hexosaminidase activity. Suitable enzymes are found in EC 3.2.1., which catalyze the hydrolysis of β-1,6-glycosidic bonds in N-acetyl-glucosamine polymers found in microbial soils. The term "hexosaminidase" includes polypeptides having N-acetylglucosaminidase activity and β-N-acetylglucosaminidase activity. Hexosaminidase activity can be determined according to Assay II described in WO2018184873. Suitable hexosaminidases include those described in International Publication Nos. 2017186936, 2017186937, 2017186943, 2017207770, 2018184873, 2019086520, 2019086528, 2019086530, 2019086532, 2019086521, and 2019 Examples of suitable hexosaminidases include those disclosed in WO 2020207944, WO 2020002604, WO 2020002608, WO 2020007863, WO 2020007875, WO 2020008024, WO 2020070063, WO 2020070249, WO 2020088957, WO 2020088958, and WO 2020207944. Variants of the Terribacillus saccharophilus hexosaminidase defined by SEQ ID NO: 1 in WO 2020207944 are preferred, particularly the variants with improved thermostability disclosed therein.

[0099] Particularly preferred hexosaminidase enzymes are those having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 66, and those having at least 60%, or at least 70%, or at least 75%, or at least 80%, or at least 85%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 67 herein, and mixtures thereof.

[0100] Xanthan gum-degrading enzymes: The compositions may contain one or more xanthan gum-degrading enzymes. Enzymes suitable for degrading xanthan gum-based stains include xanthan endoglucanases, optionally in combination with xanthan lyases. As used herein, the term "xanthan endoglucanases" refers to enzymes that exhibit endo-β-1,4-glucanase activity, optionally in combination with a suitable xanthan lyase enzyme, capable of catalyzing the hydrolysis of the 1,4-linked β-D-glucose polymer backbone of xanthan gum. Suitable xanthan endoglucanases are described in WO 2013167581, WO 2015181299, WO 2015181292, WO 2017046232, WO 2017046260, WO 201837062, WO 201837065, WO 2019038059, and WO 2019162000. As used herein, the term "xanthan lyase" refers to an enzyme that cleaves the β-D-mannosyl-β-D-1,4-glucuronosyl bond in xanthan gum. Such enzymes belong to the EC 4.2.2.12 enzyme class. Suitable xanthan gelases are described in WO 2015001017, WO 2018037061, WO 201837064, WO 2019038060, WO 2019162000, and WO 2019038057.

[0101] Galactanase: Preferably, the composition comprises a galactanase, i.e., an extracellular polymer-degrading enzyme, including an endo-beta-1,6-galactanase enzyme. The term "endo-beta-1,6-galactanase" or "polypeptide with endo-beta-1,6-galactanase activity" refers to endo-beta-1,6-galactanase activity (EC 3.2.1.164) from glycoside hydrolase family 30 that catalyzes the hydrolytic cleavage of 1,6-3-D-galactooligosaccharides with a degree of polymerization (DP) greater than 3 and their acidic derivatives bearing a 4-O-methyl glucosyluronate or glucosyluronate group at the non-reducing end. For purposes of this disclosure, endo-beta-1,6-galactanase activity is determined in Assay I according to the procedure described in WO2015185689. Suitable examples from classification EC3.2.1.164 are described in WO2015185689, e.g., mature polypeptide SEQ ID NO:2.

[0102] The additional enzymes may be included in the machine cleaning composition by adding a separate enzyme additive containing the additional enzymes or a mixed enzyme additive containing two, some or all of the additional enzymes. Such enzyme additives may be in the form of granules, liquids or slurries, and preferably further comprise an enzyme stabilizer.

[0103] Preferably, the or each additional enzyme is present in an amount of at least 0.0001% to about 0.1% by weight of pure active enzyme protein, such as from about 0.0001% to about 0.01%, 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.

[0104] Builders: The machine cleaning compositions may further contain builders, such as builders based on carbonates, bicarbonates, or silicates, which may be zeolites such as Zeolite A or Zeolite MAP (Maximum Aluminum type P). Zeolites suitable for laundry use preferably have the formula Na12(AlO2)12(SiO2)12·27H2O, with particle sizes typically ranging from 1 to 10 μm for Zeolite A and 0.7 to 2 μm for Zeolite MAP. Another builder is sodium metasilicate (Na2SiO3·nH2O or Na2SiO5·nH2O), which is strongly alkaline and is preferably used in dishwashing. In preferred embodiments, the amount of detergent builder may be greater than 5%, 10%, 20%, 30%, 40%, or 50%, or less than 80% or 65%. In dishwashing detergents, the builder concentration is typically 40-65%, especially 50-65%, or even 75-90%.

[0105] Encapsulating Agent: The composition may include 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 may include a material selected from the group consisting of a fragrance, an enzyme, an antimicrobial agent, a bleaching agent, and mixtures thereof. The shell may include a material selected from the group consisting of polyethylene, polyamide, polystyrene, polyisoprene, polycarbonate, polyester, polyacrylate, aminoplast (in one aspect, the aminoplast may include polyurea, polyurethane, and / or polyureaurethane; in one aspect, the polyurea may include polyoxymethylene urea and / or melamine formaldehyde), polyolefin, polysaccharide (in one aspect, the polysaccharide may include alginate and / or chitosan), gelatin, shellac, epoxy resin, vinyl polymer, water-insoluble inorganic material, silicone, and mixtures thereof.

[0106] Enzyme Stabilizer: The composition preferably comprises an enzyme stabilizer. Suitable enzyme stabilizers may be selected from the group consisting of: (a) inorganic salts selected from the group consisting of calcium salts, magnesium salts, and mixtures thereof; (b) carbohydrates selected from the group consisting of oligosaccharides, polysaccharides, and mixtures thereof, and sugars or sugar alcohols; (c) phenylboronic acid and derivatives thereof, such as aromatic borate esters, or phenylboronic acid derivatives, such as 4-formylphenylboronic acid, or peptide aldehydes, such as di-, tri-, or tetrapeptide aldehydes or aldehyde analogs (any of the forms B1-B0-R, where R is H, CH3, CX3, CHX2, or CH2X (X = halogen), and B0 is a single amino acid residue (preferably an optionally substituted aliphatic or aromatic side chain); B1 consists of one or more amino acid residues (preferably 1, 2 or 3), optionally including an N-terminal protecting group], or as described in WO 09118375, WO 98 / 13459); (d) mass-efficient reversible protease inhibitors selected from the group consisting of reversible protease inhibitors, such as boron-containing compounds; (e) polyols, such as propylene glycol or glycerol 1-2 propanediol; (f) calcium formate and / or sodium formate; (g) protein-type protease inhibitors, such as RASI, BASI, WASI (rice, barley and wheat bifunctional alpha-amylase / subtilisin inhibitor) or CI2 or SSI, and (h) any combination thereof.

[0107] Structuring Agents: The composition may include a structuring agent selected from the group consisting of, for example, diglycerides and triglycerides, ethylene glycol distearate, microcrystalline cellulose, cellulose-based materials, microfiber cellulose, biopolymers, xanthan gum, gellan gum, and mixtures thereof.

[0108] Polymers: The composition may contain one or more polymers. Preferred examples include carboxymethylcellulose, poly(ethylene glycol), poly(vinyl alcohol), poly(vinylpyridine-N-oxide), poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic acid / acrylic acid copolymers and lauryl methacrylate / acrylic acid copolymers, and amphiphilic polymers, and mixtures thereof.

[0109] Amphiphilic cleaning polymers: Preferably, the amphiphilic cleaning polymers have the following general structure: bis((C2H5O)(C2H4O)n)(CH3)-N + -C x H 2x -N + Compounds having the formula -(CH3)-bis((C2H5O)(C2H4O)n) where n=20-30 and x=3-8, or sulfated or sulfonated variants thereof.

[0110] Amphiphilic alkoxylated grease cleaning polymer refers to any alkoxylated polymer that has a balance of hydrophilic and hydrophobic properties to remove grease particles from fabrics and surfaces. Specific embodiments of the amphiphilic alkoxylated grease cleaning polymer of the present invention comprise a core structure and a plurality of alkoxylate groups attached to the core structure. These may comprise alkoxylated polyalkyleneimines, preferably having an inner polyethylene oxide block and an outer polypropylene oxide block.

[0111] The core structure may comprise a polyalkyleneimine structure comprising repeat units of formulae (I), (II), (III), and (IV) in condensed form:

[0112] [ka] where # in each case indicates a link between a nitrogen atom and a group A of two adjacent repeating units of formula (I), (II), (III) or (IV). 1 indicates half of the binding between the free binding sites of *indicates in each case half of a bond with one of the alkoxylate groups, and A 1 are independently selected from straight-chain or branched C2-C6-alkylene; the polyalkyleneimine structure consists of 1 repeat units of formula (I), x repeat units of formula (II), y repeat units of formula (III), and y+1 repeat units of formula (IV), where x and y in each instance have values ​​ranging from 0 to about 150; and the average weight average molecular weight Mw of the polyalkyleneimine core structure has a value ranging from about 60 to about 10,000 g / mol.

[0113] Alternatively, the core structure may comprise a polyalkanolamine structure that is a condensation product of at least one compound selected from N-(hydroxyalkyl)amines of formula (Ia) and / or (Ib):

[0114] [ka] wherein A is independently selected from C1-C6-alkylene; 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, where the alkyl, cycloalkyl, or aryl radicals may be optionally substituted; R 6 is selected from hydrogen, alkyl, cycloalkyl, or aryl, where the alkyl, cycloalkyl, or aryl of said radicals may be optionally substituted.

[0115] The multiple alkyleneoxy groups attached to the core structure are independently selected from alkyleneoxy units of formula (V):

[0116] [ka] During the ceremony, *represents in each case half of the bond to the nitrogen atom of a repeating unit of formula (I), (II), or (IV), and A 2 is in each occurrence independently selected from 1,2-propylene, 1,2-butylene, and 1,2-isobutylene; A 3 is 1,2-propylene; R in each occurrence is independently selected from hydrogen and C1-C4-alkyl; m has an average value ranging from 0 to about 2; n has an average value ranging from about 20 to about 50; and p has an average value ranging from about 10 to about 50.

[0117] Carboxylate polymers: The present compositions can also include one or more carboxylate polymers, such as maleate / acrylate random copolymers or polyacrylate homopolymers. In one embodiment, the carboxylate polymer is a polyacrylate homopolymer having a molecular weight of 4,000 Da to 9,000 Da or 6,000 Da to 9,000 Da.

[0118] Soil Release Polymers: The composition preferably also includes one or more soil release polymers having a structure defined by one of the following structures (I), (II), or (III): (I)-[(OCHR 1 -CHR 2 ) a -O-OC-Ar-CO-] d (II)-[(OCHR 3 -CHR 4 ) b -O-OC-sAr-CO-] e (III)-[(OCHR 5 -CHR 6 ) c -OR 7 ] f During the ceremony, a, b, and c are 1 to 200; d, e, and f are 1 to 50; Ar is 1,4-substituted phenylene; sAr is 1,3-substituted phenylene substituted at the 5-position with SO3Me; Me is Li, K, Mg / 2, Ca / 2, Al / 3, ammonium, mono-, di-, tri-, or tetra-alkylammonium (the alkyl groups are C1-C 18 Alkyl or C2-C 10 hydroxyalkyl), or mixtures thereof; R 1 , R 2 , R 3 , R 4 , R 5 , and R 6 are independently H or C1 to C 18 n- or iso-alkyl; R 7 is a straight chain or branched chain C1 to C 18 Alkyl, or straight or branched C2-C 30 Alkenyl or cycloalkyl groups having 5 to 9 carbon atoms, or C8 to C 30 Aryl group or C6-C 30 It is an arylalkyl group.

[0119] 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.

[0120] Cellulosic polymer: The composition may include one or more cellulosic polymers, preferably selected from alkyl celluloses, alkyl alkoxyalkyl celluloses, carboxyalkyl celluloses, and alkyl carboxyalkyl celluloses. In one embodiment, the cellulosic polymer is selected from the group consisting of carboxymethyl cellulose, methyl cellulose, methylhydroxyethyl cellulose, methylcarboxymethyl cellulose, and mixtures thereof. In one embodiment, the carboxymethyl cellulose has a degree of carboxymethyl substitution of 0.5 to 0.9 and a molecular weight of 100,000 Da to 300,000 Da.

[0121] Bleaching System: The compositions may contain a bleaching system comprising a source of HO, such as a perborate or percarbonate, which may be combined with a peracid-forming bleach activator, such as tetraacetylethylenediamine or nonanoyloxybenzenesulfonate. Alternatively, the bleaching system may comprise, for example, an amide, imide, or sulfone-type peroxyacid. Generally, when a bleaching agent is used, the compositions of the present invention may comprise from about 0.1% to about 30%, or even from about 0.1% to about 25%, by weight of the subject cleaning composition, of bleaching agent.

[0122] Chelating Agents: The compositions preferably include a chelating agent, preferably in an amount of from 0.005% to about 15%, or even from about 3.0% to about 10% chelating agent by weight of the composition. Suitable chelating agents include copper, iron, and / or manganese chelating agents, and mixtures thereof. Preferred chelating agents (complexing agents) include DTPA (Diethylene triamine pentaacetic acid), HEDP (Hydroxyethane diphosphonic acid), DTPMP (Diethylene triamine penta(methylene phosphonic acid), 1,2-dihydroxybenzene-3,5-disulfonic acid disodium salt hydrate, ethylenediamine, diethylenetriamine, ethylenediaminedisuccinic acid (EDDS), N-hydroxyethylethylenediaminetri-acetic acid (HEDTA), triethylenetetraaminehexaacetic acid (TTHA), N-hydroxyethyliminodiacetic acid (HEIDA), dihydroxyethylglycine (DHEG), ethylenediaminetetrapropionic acid (ETPA), and the like. acid (EDTP), methyl-glycine-diacetic acid (MGDA), glutamic-N,N-diacetic acid (GLDA), iminodisuccinic acid (IDS), carboxymethyl inulin, and salts, derivatives, and mixtures thereof.Preferred chelating agents are selected from the group consisting of methyl-glycine-diacetic acid (MGDA), its salts and derivatives, glutamic acid-N,N-diacetic acid (GLDA), its salts and derivatives, iminodisuccinic acid (IDS), its salts and derivatives, carboxymethyl inulin, its salts and derivatives, and mixtures thereof. MGDA and its salts are particularly preferred, especially the trisodium salt of MGDA.

[0123] How to use The present invention also provides a method of treating the interior of a cleaning machine, such as a dishwasher or washing machine, to prevent or remove soil buildup, the method comprising the step of supplying a machine cleaning composition to the interior of the machine during at least one wash cycle or at least one rinse cycle of the dishwasher or washing machine, wherein the machine cleaning composition is present in the wash water or rinse water (aqueous wash liquor).

[0124] In particular, the method is for treating the interior of a washing machine.

[0125] The present invention also provides a method for dissolving soils on the interior surfaces of a washing machine, such as a dishwasher or a washing machine, comprising providing a machine cleaning composition during at least one or more wash cycles or one or more rinse cycles of the washing machine, wherein the machine cleaning composition is present in the wash water or rinse water (aqueous wash liquor).

[0126] The present invention also provides the use of the machine cleaning composition for cleaning a cleaning machine, such as a washing machine or a dishwasher. The compositions and methods of the present invention are suitable for cleaning either domestic or commercial / institutional cleaning machines.

[0127] The machine cleaning composition may be provided to the washing machine either via a dispensing mechanism integrated into the machine, such as a drawer or other dispenser, or via a cartridge which is dispensed into the machine, or by being placed directly inside the machine, for example, in the case of a washing machine, directly into the drum.

[0128] The washing machine may be at least partially loaded with items during at least one wash cycle or at least one rinse cycle. The machine cleaning composition may be used over two or more successive wash or rinse cycles of the washing machine.

[0129] It may be preferred that the machine is empty during at least one wash cycle or at least one rinse cycle so that the machine cleaning composition of the present invention has better access to all areas of the washing machine. This is particularly the case for washing machines, and therefore in a preferred method for cleaning a washing machine, at least one wash cycle or at least one rinse cycle is carried out in an empty washing machine.

[0130] In a preferred embodiment of the present invention, the machine cleaning composition is used in more than one operation of a washing machine, for example, in two or more of the pre-wash, wash, and rinse steps in the same washing program, or in a continuous washing program. These operations are preferably sequential. The washing operation may include a pre-wash (optional), a wash cycle, and a rinse cycle, or may include either a wash-only cycle or a rinse-only cycle. The rinse-only cycle may be either a pre-wash cycle or a post-wash cycle. Using the composition of the present invention in only the wash cycle or only the rinse cycle can be achieved by loading the composition into the washing machine and then running only that type of cycle in the presence of the composition. Alternatively, the composition may be formulated with a suitable release mechanism, for example, accelerated or delayed release, so that the cleaning composition is released at the desired part of the washing operation. When a polymer is used to achieve accelerated or delayed release of the composition of the present invention, suitable polymers for achieving this effect are well known in the art.

[0131] The washer may be operated in either a wash program and / or a rinse program during the method, which includes both. Typically, the wash and rinse cycles may last up to 2 hours, the wash-only cycle lasts up to 1.5 hours, and the rinse-only cycle lasts up to 0.5 hours.

[0132] The compositions of the present invention are preferably in contact with the stain to be removed for at least 10 minutes, preferably at least 15 minutes, for example at least 20 minutes, regardless of whether the composition is applied to the stain during the wash cycle or the rinse cycle.

[0133] During the wash / rinse cycle, the composition is distributed throughout the cavity of the washer, which brings it into contact with the interior surfaces of the machine, such as pipes, filter drums, etc. Additionally, the aqueous cleaning solution containing the composition of the present invention must be drained through the filter and piping, thereby providing additional opportunities for soil removal from the filter and piping.

[0134] In the aqueous cleaning liquor the or each enzyme is preferably present in an amount of from 0.01 ppm to 10 ppm, preferably from 0.1 ppm to 1 ppm. If present, the surfactant is preferably present in an amount of from 0.05 to 5 g / L, or up to 2 g / L, or up to 1 g / L, or up to 0.75 g / L, or up to 0.5 g / L.

[0135] The or each enzyme may be present in the wash solution in an amount corresponding to 0.001 to 100 mg of active enzyme protein per liter of wash solution, preferably 0.005 to 5 mg of active enzyme protein per liter of wash solution, more preferably 0.01 to 1 mg of enzyme protein per liter of wash solution, and especially 0.1 to 1 mg of enzyme protein per liter of wash solution.

[0136] The washing solution preferably has a pH of about 5 or 10.5, more preferably 6 to 8, or 7.5. The washing solution preferably has a temperature of about 5°C to about 40°C, or preferably 10 to 35°C, or 30°C, or 25°C.

[0137] Test Method Test Method 1 Enzyme activity towards β-D-mannuronic acid block (poly M activity) and α-L-guluronic acid block (poly G activity) Alginate lyase activity was measured using mannuronic block oligosaccharide DP20-DP35 (product code: ALG601) and guluronate oligosaccharide DP2-DP45 (product code: ALG610) manufactured by Elicityl France as substrates. Mannuronic block oligosaccharide DP20-DP35 was used to measure poly M activity, and guluronate oligosaccharide DP2-DP45 was used to measure poly G activity.

[0138] A 2.5% solution of each substrate was suspended in Tris buffer, pH 8.3, and incubated with 3 ppm of each alginate lyase of interest in a 96-well plate for 60 minutes at 25°C.

[0139] Activity for each substrate is given as the delta absorbance at 235 nm in a spectrophotometer relative to a sample without enzyme when the enzyme is contacted with each substrate. These values ​​are then used to evaluate the activity of each enzyme toward β-D-mannuronic acid blocks (poly M) and / or α-L-guluronic acid blocks (poly G). Enzymes with activity toward poly(beta-D-mannuronate) (poly M activity) preferably provide a delta absorbance relative to the absence of enzyme of at least 0.1 absorbance units, more preferably at least 0.15 absorbance units, and more preferably at least 0.2 absorbance units. Enzymes with activity toward poly(alpha-L-guluronate) (poly G activity) preferably provide a delta absorbance relative to the absence of enzyme of at least 0.3 absorbance units, preferably at least 0.4 or even 0.5 or 0.6 absorbance units.

[0140] Test Method 2 Measurement of activity against beta-1,3-glucan and beta-1,3(4)-glucan Activity towards beta-1,3-glucan and beta-1,3(4)-glucan was measured using the red variant of the discovery kit provided by GlycoSpot A / S (Soborg, Denmark), which allows for the simultaneous assay of 16 different activities of a given enzyme. The assay protocol is shown below. If a given enzyme exhibits greater than 0.3 absorbance units towards curdlan (CPH0009) and barley-derived beta-glucan (CPH0003), the enzyme is considered to be active towards both beta-1,3-glucan and beta-1,3(4)-glucan, i.e., classified as an endo-beta-1,3(4)-glucanase. An enzyme is considered to be an endo-β-1,3-glucanase if it exhibits greater than 0.3 absorbance units against curdlan (CPH0009) but less than or equal to 0.3 absorbance units against barley-derived beta-glucan (CPH0003). 1. Add 200 μL of activation solution to each well of a 96-well plate. 2. Incubate at room temperature for 10 minutes without agitation. 3. Remove remaining solution by centrifugation (2700 xg for 10 minutes or vacuum). 4. Wash twice with 100 μL of water to completely remove the stabilizer. 5. Add a sample and a control to each well of a 96-well plate. The control is 150 μL of 1 M tris(hydroxymethyl)aminomethane hydrochloride (Tris-HCl) buffer (pH 8). The sample is 1 mg of active enzyme protein dissolved in 150 μL of the same Tris-HCl buffer. 6. Place the "product plate" under the substrate plate. 7. Incubate the reaction at 30°C for 30 hours. 8. Transfer the reaction products to the product plate by centrifugation (2700 xg for 10 minutes or vacuum). 9. Ensure that the volume in each well is equal. 10. Detect absorbance (517 nm). [Example]

[0141] Machine Cleaning Composition Examples Examples 1-3 Machine Cleaning Gel:

[0142] [Table 1]

[0143] Examples 4-6 Machine Cleaning Powder

[0144] [Table 2]

[0145] Examples 7-9 Machine Cleaning Tablets

[0146] [Table 3]

[0147] Dimensions and values ​​disclosed herein should not be understood as being strictly limited to the exact numerical values ​​recited. Instead, unless otherwise specified, each such dimension is intended to mean both the recited value and a functionally equivalent range surrounding that value. For example, a dimension disclosed as "40 mm" is intended to mean "about 40 mm." The inventions disclosed in this specification are as follows. [1] (a) A machine cleaning composition comprising at least two enzymes selected from (i) an alginate lyase enzyme, (ii) a Pel-ase enzyme, (iii) a Psl-ase enzyme, (iv) an endo-β-1,3-glucanase enzyme, and (v) an endo-β-1,3(4)-glucanase enzyme; and (b) a cleaning adjuvant. [2] The cleaning composition for a washing machine according to [1], further comprising a surfactant. [3] The cleaning composition for a washing machine according to [1] or [2], wherein the alginate lyase enzyme is derived from a microorganism, preferably from a bacterium or an alga, most preferably from a bacterium, preferably from Flavobacterium sp., Sphingomonas sp., Zobellia galactanivorans, preferably from Flavobacterium sp. [4] The alginate lyase enzyme has at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to one or more of SEQ ID NO: 1; or at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 99% sequence identity to SEQ ID NO: 2. an alginate lyase having 7%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:3; an alginate lyase having at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:4; an alginate lyase having at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least alginate lyases having at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:5; alginate lyases having at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:6; %, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 7; alginate lyases having at least 60%, or at least 70%, or at least 80%, or at least 90%, or at least 95%, or at least 96%, or at least 97%, or at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 7;and mixtures thereof, preferably an alginate lyase selected from SEQ ID NO: 1, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7, or mixtures thereof, and most preferably the alginate lyase enzyme comprises an alginate lyase selected from alginate lyases having at least 60% sequence identity to one or more of SEQ ID NO: 6 and SEQ ID NO: 7, and mixtures thereof; [5] The machine cleaning composition according to any one of [1] to [4], further comprising a nuclease enzyme and / or a hexosaminidase enzyme in an amount of 0.00005 to 5% by weight of active enzyme protein. [6] The cleaning composition for a washing machine according to any one of [1] to [5], further comprising a nonionic surfactant, preferably in an amount of 0.5 to 30% by weight of the composition. [7] The cleaning composition for a washing machine according to any one of [1] to [6], further comprising an additional enzyme, preferably selected from amylase, nuclease, mannanase, xanthan lyase, xanthanase, and mixtures thereof. [8] A method for treating the interior of a cleaning machine, such as a dishwasher or a washing machine, to prevent or remove dirt buildup, the method comprising the step of supplying the machine cleaning composition according to any one of [1] to [7] to the interior of the machine during at least one wash cycle or at least one rinse cycle of the dishwasher or washing machine. [9] The method according to [8] for treating the inside of a washing machine.

[10] A method for breaking down soils on the internal surfaces of a dishwasher or washing machine, the method comprising the step of providing a machine cleaning composition according to any one of [1] to [7] during at least one wash cycle or one rinse cycle of an automatic dishwasher or washing machine, wherein the machine cleaning composition is present in the wash water or rinse water (aqueous cleaning liquid).

[11] The method according to any one of [8] to

[10] , wherein the washing machine can at least partially load items during the at least one washing cycle or the at least one rinsing cycle.

[12] The method according to any one of [8] to

[11] , wherein the machine cleaning composition is provided in two or more consecutive wash and / or rinse cycles of the washing machine.

[13] Use of the machine cleaning composition according to any one of [1] to [7] for cleaning a washing machine such as a washing machine or dishwasher, either domestic or commercial / institutional.

Claims

1. 1. A machine cleaning composition comprising: (a) an alginate lyase enzyme; (ii) at least one enzyme selected from a Pel-ase enzyme and a Psl-ase enzyme; and (iv) an endo-β-1,3(4)-glucanase enzyme; and (b) a cleaning adjunct.

2. 10. The machine cleaning composition of claim 1, further comprising a surfactant.

3. 10. The machine cleaning composition of claim 1, wherein the alginate lyase enzyme is of microbial origin.

4. 2. The machine cleaning composition of claim 1, wherein the alginate lyase enzyme comprises an alginate lyase selected from an alginate lyase having at least 90% sequence identity to SEQ ID NO:1; an alginate lyase having at least 90% sequence identity to SEQ ID NO:2; an alginate lyase having at least 90% sequence identity to SEQ ID NO:3; an alginate lyase having at least 90% sequence identity to SEQ ID NO:4; an alginate lyase having at least 90% sequence identity to SEQ ID NO:5; an alginate lyase having at least 90% sequence identity to SEQ ID NO:6; an alginate lyase having at least 90% sequence identity to SEQ ID NO:7; and mixtures thereof.

5. 10. The machine cleaning composition of claim 1 further comprising a nuclease enzyme and / or a hexosaminidase enzyme in an amount of 0.00005 to 5% by weight of active enzyme protein.

6. 10. The machine cleaning composition of claim 1, wherein the composition further comprises a nonionic surfactant.

7. 10. The machine cleaning composition of claim 1, comprising an additional enzyme.

8. 10. A method of treating the interior of a cleaning machine such as a dishwasher or washing machine to prevent or remove soil build-up, said method comprising the step of supplying a machine cleaning composition according to any one of claims 1 to 7 to the interior of the machine during at least one wash cycle or at least one rinse cycle of the dishwasher or washing machine.

9. 9. The method of claim 8 for treating the interior of a washing machine.

10. 10. A method for disintegrating soils on the internal surfaces of a dishwasher or washing machine, the method comprising the step of providing a machine cleaning composition according to any one of claims 1 to 7 during at least one or more wash cycles or one or more rinse cycles of an automatic dishwasher or washing machine, wherein the machine cleaning composition is present in the wash water or rinse water (aqueous wash liquor).

11. 9. The method of claim 8, wherein the washing machine can be at least partially loaded with items during the at least one wash cycle or the at least one rinse cycle.

12. 10. The method of claim 8, wherein the machine cleaning composition is provided in two or more successive wash and / or rinse cycles of the washing machine.

13. Use of a machine cleaning composition according to any one of claims 1 to 7 for cleaning a washing machine such as a washing machine or dishwasher, either domestic or commercial / institutional.

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