Water-soluble unit dose articles containing metalloproteinases

Abstract

A novel fabric cleaning composition is provided that has a reduced concentration of ethoxylated alkyl sulfate and provides good dirt and stain removal. [Solution] A water-soluble unit-dose detergent article comprising a water-soluble film and a liquid laundry detergent composition, wherein the detergent composition is a non-soap surfactant system comprising an anionic non-soap surfactant and a nonionic surfactant, wherein the anionic non-soap surfactant comprises an anionic non-soap surfactant selected from the group consisting of alkyl sulfates, alkoxylated alkyl sulfates, and mixtures thereof, in an amount of more than 0% to less than 20% by weight of the anionic non-soap surfactant, a metalloproteinase, and water up to 15% by weight of the composition.

Description

[Technical Field]

[0001] A water-soluble unit-dose article comprising a detergent composition containing a surfactant and a metalloproteinase. [Background technology]

[0002] Water-soluble unit-dose detergent articles are popular with consumers because they are convenient and efficient to use. Such water-soluble unit-dose articles contain a detergent composition encased in a water-soluble film. When a water-soluble unit-dose detergent article is added to water, the film dissolves / disintegrates, releasing the detergent into the surrounding water and creating a cleaning solution.

[0003] This invention addresses the challenge of reducing reliance on ethoxylated alkyl sulfates while achieving effective fabric cleaning performance. Ethoxylated alkyl sulfates are commonly used surfactants that help remove dirt, stains, and oily grime. This invention seeks alternative compositions containing lower concentrations of ethoxylated alkyl sulfates. [Overview of the Initiative] [Problems that the invention aims to solve]

[0004] Therefore, an object of the present invention is to provide a novel fabric cleaning composition having a reduced concentration of ethoxylated alkyl sulfate that provides good dirt and stain removal. [Means for solving the problem]

[0005] A water-soluble unit-dose detergent article comprising a water-soluble film and a liquid detergent composition, wherein the detergent composition is A non-soap surfactant system, wherein the surfactant system comprises an anionic non-soap surfactant and a nonionic surfactant (the anionic non-soap surfactant comprises an anionic non-soap surfactant selected from the group consisting of alkyl sulfates, alkoxylated alkyl sulfates, and mixtures thereof, in an amount of more than 0% to less than 20% by weight of the anionic non-soap surfactant), Up to 15% by weight of water in the composition, A water-soluble, unit-dose detergent article containing metalloproteinase.

[0006] The water-soluble unit-dose detergent article of the present invention includes a cleaning composition that significantly reduces the amount of ethoxylated alkyl sulfate used while maintaining a high cleaning effect. [Modes for carrying out the invention]

[0007] Water-soluble unit quantity article This invention discloses a water-soluble unit-dose article comprising a water-soluble film and a liquid detergent composition, preferably a liquid laundry detergent composition. The water-soluble film and detergent composition will be described in more detail below.

[0008] A water-soluble unit-dose detergent article includes a water-soluble film molded such that the unit-dose article contains at least one internal compartment surrounded by a water-soluble film. The unit-dose article may comprise a first water-soluble film and a second water-soluble film sealed together to define the internal compartment. The water-soluble unit-dose article is configured to prevent the detergent composition from leaking out of the compartment during storage. However, when the water-soluble unit-dose article is added to water, the water-soluble film dissolves, releasing the contents of the internal compartment into the cleaning solution.

[0009] A compartment should be understood as a sealed internal space within a unit-dose article that holds the detergent composition. During manufacturing, the first water-soluble film may be shaped to include an opening compartment into which the detergent composition is added. Next, the first film is covered with a second water-soluble film in an orientation that closes the opening of the compartment. The first and second films are then sealed together along the sealing region.

[0010] A unit dose article may contain more than one compartment, more than two compartments, more than three compartments, or more than four compartments. The compartments may be arranged in an overlapping orientation, that is, one positioned on top of the other. In such an orientation, the unit dose article contains at least three films, one or more in the top, one in the middle, and one in the bottom. Alternatively, the compartments may be positioned in a side-by-side orientation, that is, one adjacent to the other. The compartments may also be oriented in a "tire and rim" arrangement, that is, the first compartment is positioned adjacent to the second compartment, but the first compartment at least partially surrounds the second compartment but does not completely enclose it. Alternatively, one compartment may be completely enclosed within another compartment.

[0011] If the unit-dose article has at least two compartments, one of the compartments may be smaller than the other. If the unit-dose article has at least three compartments, two of the compartments may be smaller than a third compartment, preferably with the smaller compartments overlapping the larger compartments. The overlapping compartments are preferably oriented adjacent to each other. The unit-dose article may contain at least four compartments, three of which may be smaller than a fourth compartment, preferably with the smaller compartments overlapping the larger compartments. The overlapping compartments are preferably oriented adjacent to each other.

[0012] In a multi-compartment orientation, the detergent composition according to the present invention may be contained within at least one compartment. For example, the detergent composition may be contained within one compartment, two compartments, or even three or four compartments. Alternatively, the detergent composition according to the present invention may be divided into different compartments so that the individual components can be combined in the cleaning solution at the time of use. For example, one compartment may contain a non-soap surfactant system according to the present invention, and another compartment may contain a metalloproteinase according to the present invention.

[0013] Each section may contain the same composition or different compositions. The different compositions may all be in the same form or in different forms.

[0014] The water-soluble unit-dose article may contain at least two internal compartments, with the laundry detergent composition contained in at least one of these compartments; preferably, the unit-dose article contains at least three compartments, with the detergent composition contained in at least one of these compartments.

[0015] The water-soluble unit dose article may contain a laundry detergent composition in an amount of 1 to 60 grams, preferably 5 to 50 grams, more preferably 10 to 40 grams, most preferably 12 to 25 grams, or 30 to 40 grams. The water-soluble unit dose article may also contain a liquid laundry detergent composition in an amount of 1 ml to 60 ml, preferably 5 to 50 ml, more preferably 10 to 40 ml, most preferably 12 to 25 ml, or 30 to 40 ml.

[0016] Water-soluble film The film of the present invention is water-soluble or water-dispersible. The water-soluble film preferably has a thickness of 20 to 150 micrometers, preferably 35 to 125 micrometers, more preferably 50 to 110 micrometers, and most preferably about 76 micrometers.

[0017] Preferably, after use of a glass filter with a maximum pore size of 20 micrometers, when measured by the method described herein, the water solubility of the film is at least 50%, preferably at least 75%, or even more preferably at least 95%. Add 5 grams ± 0.1 grams of the film material to a pre-weighed 3 L beaker and add 2 L ± 5 ml of distilled water. Stir this vigorously for 30 minutes at 30 °C with a magnetic stirrer (Labline model number 1250) or equivalent set at 600 rpm and a 5 cm magnetic stirrer. Next, filter the mixture through a pleated qualitative sintered glass filter with a pore size (maximum 20 micrometers) as defined above. Dry the water from the recovered filtrate by any conventional method and determine the weight of the remaining material (this is the dissolved or dispersed fraction). Next, the percentage of solubility or dispersibility can be calculated.

[0018] Preferred film materials are preferably polymeric materials. The film material can be obtained by methods known in the art, such as casting, blow molding, extrusion, or coextrusion of polymeric materials.

[0019] Preferred polymers, copolymers, or derivatives thereof suitable for use as pouch materials are selected from polyvinyl alcohol, polyvinylpyrrolidone, polyalkylene oxide, acrylamide, acrylic acid, cellulose, cellulose ether, cellulose ester, celluloseamide, polyvinyl acetate, polycarboxylic acids and salts, polyamino acids or peptides, polyamides, polyacrylamide, maleic acid / acrylic acid copolymers, polysaccharides including starch and gelatin, xanthan gum, and natural gums such as cara gum. More preferred polymers are selected from polyacrylate and water-soluble acrylate copolymers, methylcellulose, sodium carboxymethylcellulose, dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropyl methylcellulose, maltodextrin, and polymethacrylate, and most preferably from polyvinyl alcohol, polyvinyl alcohol copolymer and hydroxypropyl methylcellulose (HPMC), and combinations thereof. Preferably, the concentration of the polymer in the pouch material, for example, PVA polymer, is at least 60%. The polymer may have any weight-average molecular weight, preferably about 1,000 to 1,000,000, more preferably about 10,000 to 300,000, and even more preferably about 20,000 to 150,000.

[0020] Preferably, the water-soluble film contains a polyvinyl alcohol polymer, preferably the polyvinyl alcohol polymer is a polyvinyl alcohol homopolymer or a polyvinyl alcohol copolymer, or a mixture thereof, preferably a blend of a polyvinyl alcohol homopolymer and / or a polyvinyl alcohol copolymer, preferably the polyvinyl alcohol copolymer is selected from sulfonated and carboxylated anionic polyvinyl alcohol copolymers, particularly carboxylated anionic polyvinyl alcohol copolymers, most preferably the polyvinyl alcohol polymer contains a blend of a polyvinyl alcohol homopolymer and a carboxylated anionic polyvinyl alcohol copolymer, or a blend of polyvinyl alcohol homopolymers. Alternatively, the water-soluble film may contain a single polyvinyl alcohol polymer, preferably a carboxylated anionic polyvinyl alcohol copolymer.

[0021] Preferred films exhibit good dissolution in cold water, i.e., in distilled water that has not been heated. Preferably, such films exhibit good solubility at a temperature of 24 °C, more preferably at 10 °C. Good dissolution means that when measured by the method described herein after using a glass filter with a maximum pore size of 20 micrometers as described above, the film exhibits at least 50%, preferably at least 75%, or even at least 95% water solubility.

[0022] Some preferred films are supplied by Monosol under product reference numbers M8630, M8900, M8779, M8310.

[0023] The film may be opaque, transparent or translucent. The film may contain printed areas. The printed areas can be obtained using standard techniques such as flexographic printing or inkjet printing.

[0024] The film may contain an aversive agent, such as a bittering agent. Suitable bittering agents include, but are not limited to, naringin, sucrose octaacetate, quinine hydrochloride, denatonium benzoate, or mixtures thereof. Any suitable concentration of the aversive agent may be used in the film. Suitable concentrations include, but are not limited to, 1 to 5000 ppm, or more specifically, 100 to 2500 ppm, or more specifically, 250 to 2000 ppm.

[0025] Preferably, a water-soluble film, or a water-soluble unit-dose article, or both, is coated with a lubricant, preferably selected from talc, zinc oxide, silica, siloxane, zeolite, silicic acid, alumina, sodium sulfate, potassium sulfate, calcium carbonate, magnesium carbonate, sodium citrate, sodium tripolyphosphate, potassium citrate, potassium tripolyphosphate, calcium stearate, zinc stearate, magnesium stearate, starch, modified starch, clay, kaolin, gypsum, cyclodextrin, or mixtures thereof.

[0026] Detergent composition The water-soluble unit-dose article comprises a detergent composition, which may be any cleaning or treatment composition, such as a hard surface cleaning composition, an automatic dishwasher cleaning composition, or a laundry composition. Preferably, the composition is a laundry detergent composition. The term "liquid laundry detergent composition" refers to, but is not limited to, any laundry detergent composition containing a liquid capable of wetting and treating fabrics, such as liquids, gels, pastes, and dispersions. The liquid composition may preferably contain solids or gases in subdivided forms, but excludes forms that are non-flowing as a whole, such as tablets or granules.

[0027] The laundry detergent composition may be used for hand washing of fabrics or for washing fabrics in an automatic washing machine.

[0028] The laundry detergent composition contains a non-soap surfactant and a metalloproteinase. The non-soap surfactant and surfactant will be described in more detail below.

[0029] The laundry detergent composition contains 30% to 65% by weight, preferably 30% to 55% by weight, and more preferably 30% to 50% by weight of a non-soap surfactant system. The non-soap surfactant system includes anionic non-soap surfactants and nonionic surfactants.

[0030] The anionic non-soap surfactant comprises an anionic non-soap surfactant selected from the group consisting of alkyl sulfates, alkoxylated alkyl sulfates, and mixtures thereof, in an amount of more than 0% by weight and less than 20% by weight of the anionic non-soap surfactant.

[0031] Preferably, the weight ratio of the anionic non-soap surfactant to the nonionic surfactant is greater than 1.5:1, preferably greater than 1.5:1 to 10:1, or 2:1 to 5:1, or 5:1 to 10:1.

[0032] When calculating the weight percentage or weight ratio of surfactants, the weight of neutralizing counterions is not considered in the case of anionic surfactants. For example, when calculating the weight percentage of anionic soap or non-soap surfactant or the weight ratio of anionic soap or non-soap surfactant to nonionic surfactant for anionic soap or non-soap surfactants, only the weight of the surfactant anion is considered.

[0033] Anionic non-soap surfactants include alkyl sulfates, alkoxylated alkyl sulfates, or mixtures thereof. (Alkoxylated) alkyl sulfate anionic surfactants may be primary (alkoxylated) alkyl sulfate anionic surfactants or secondary (alkoxylated) alkyl sulfate anionic surfactants, or mixtures thereof, preferably primary (alkoxylated) alkyl sulfate anionic surfactants. Preferably, alkoxylated alkyl sulfates include ethoxylated alkyl sulfates, propoxylated alkyl sulfates, mixed ethoxylated / propoxylated alkyl sulfates, or mixtures thereof, more preferably ethoxylated alkyl sulfates. Preferably, ethoxylated alkyl sulfates have an average degree of ethoxylation of 0.1 to 5, preferably 0.5 to 3. Alternatively, alkyl sulfate anionic surfactants do not contain alkoxylation. Preferably, the (alkoxylated)alkyl sulfate anionic surfactant has an average alkyl chain length of 8 to 18, more preferably 10 to 16, and most preferably 12 to 15. Preferably, the alkyl chain of the (alkoxylated)alkyl sulfate anionic surfactant is linear, branched, or a mixture thereof. Preferably, the branched (alkoxylated)alkyl sulfate anionic surfactant is a branched primary (alkoxylated)alkyl sulfate, a branched secondary (alkoxylated)alkyl sulfate, or a mixture thereof, preferably a branched primary (alkoxylated)alkyl sulfate, where the branching is preferably at the 2 position, or may be located further down the alkyl chain, or the branching may be polybranched, spreading over the alkyl chain. The weight-average degree of branching of the (alkoxylated)alkyl sulfate anionic surfactant may be 0% to 100%, preferably 0% to 95%, more preferably 0% to 60%, and most preferably 0% to 20%. Alternatively, the weight-average branching degree of the (alkoxylated) alkyl sulfate anionic surfactant may be 70% to 100%, preferably 80% to 90%. Preferably, the alkyl chain is selected from naturally derived materials, synthetic materials, or mixtures thereof.Preferably, the synthetic-derived material includes oxo-synthetic materials, Ziegler-synthetic materials, Guerbet-synthetic materials, aldol-condensation-synthetic materials, Fischer-Tropsch-synthetic materials, iso-alkyl-synthetic materials, or mixtures thereof, preferably oxo-synthetic materials. Preferably, the laundry detergent composition contains 1% to 20% by weight, preferably 2% to 15% by weight, more preferably 4% to 10% by weight of (alkoxylated) alkyl sulfate anionic surfactant. If alkyl ethoxysulfates are present in the laundry detergent composition, the alkyl ethoxysulfate starting material may be treated to reduce the 1,4-dioxane content to a low concentration of less than 1 ppm per surfactant. Those skilled in the art will be aware of technical means for reducing the dioxane content in the surfactant starting material, including (multi-step) steam stripping, nanofiltration, or a combination thereof.

[0034] Anionic non-soap surfactants may include linear alkylbenzene sulfonates. Preferably, the linear alkylbenzene sulfonate is C 10 ~C 16 Alkylbenzene sulfonate, C 11 ~C 14 The laundry detergent composition contains alkylbenzene sulfonates or mixtures thereof. Preferably, the alkylbenzene sulfonates are amine-neutralized alkylbenzene sulfonates, alkali metal-neutralized alkylbenzene sulfonates, or mixtures thereof. The amine is preferably selected from monoethanolamine, triethanolamine, monoisopropanolamine, or mixtures thereof, and preferably the amine is monoethanolamine. The alkali metal is preferably selected from sodium, potassium, magnesium, or mixtures thereof. Preferably, the laundry detergent composition contains 5% to 45% by weight, preferably 7.5% to 40% by weight, more preferably 10% to 35% by weight of linear alkylbenzene sulfonates.

[0035] Preferably, the anionic non-soap surfactant comprises at least 80% by weight of a linear alkylbenzene sulfonate anionic surfactant. Most preferably, the anionic non-soap surfactant consists of a linear alkylbenzene sulfonate anionic surfactant and an alkyl sulfate, an alkoxylated alkyl sulfate, or a mixture thereof. Preferably, the anionic non-soap surfactant system consists of more than 0% to 20% of a linear alkylbenzene sulfonate anionic surfactant and at least 80% of an alkyl sulfate anionic surfactant, an alkoxylated alkyl sulfate anionic surfactant, or a mixture thereof.

[0036] The laundry detergent composition contains a nonionic surfactant. The nonionic surfactant includes, and preferably consists of, an ethoxylated alcohol nonionic surfactant. Preferably, the laundry detergent composition contains 5% to 45% by weight, or 10% to 40% by weight, or 15% to 35% by weight of an ethoxylated alcohol nonionic surfactant. The ethoxylated alcohol nonionic surfactant may be a primary nonionic surfactant, a secondary nonionic surfactant, or a mixture thereof. Preferably, the nonionic surfactant includes a mixture of a primary ethoxylated alcohol nonionic surfactant and a secondary ethoxylated alcohol nonionic surfactant, and more preferably, the primary ethoxylated alcohol nonionic surfactant and the secondary ethoxylated alcohol nonionic surfactant are present in a weight ratio of 2:1 to 1:10, preferably 1.5:1 to 1:7, and more preferably 1:1 to 1:5. The ethoxylated alcohol nonionic surfactant may be linear or branched. In the branched chain form, the branching may be at position 1, position 2, or further down the alkyl chain, where the carbon position numbering begins from the carbon linked to the oxygen linker between the alkyl chain and the ethoxylated chain. The branching may be single-branched or multi-branched. Most preferably, the branching is single-branched at position 2. The branching is preferably alkyl-branched, more preferably methyl-branched, ethyl-branched, propyl-branched, butyl-branched, or pentyl-branched, most preferably a mixture thereof. In the linear chain form, the alkyl chain of the alcohol may have a natural distribution of C6-C20 alkyl chains depending on the source of the material. Alternatively, the linear alkyl alcohol may be fractionated to increase the C12-C14 alkyl chain content. The ethoxylated alcohol nonionic surfactant contains an alkyl chain having an average of 8-18 carbon atoms, preferably 10-16 carbon atoms, more preferably 12-15 carbon atoms. The ethoxylated alcohol nonionic surfactant has an average degree of ethoxylation of 5-12, preferably 6-10. Ethoxylated alcohol nonionic surfactants may have a broad range (BRE) or narrow range (NRE) ethoxylation distribution.Narrow-range ethoxylates (NREs) are alcohol polyglycol ethers with a narrow congener distribution and are known nonionic surfactants. Peak-type alkoxylation and peak-type ethoxylation are also often used to describe the methods and materials used in their production. They can be produced industrially, for example, by adding ethylene oxide to an alcohol in the presence of a suitable catalyst (a calcined or fatty acid-hydrophobized layered compound). Examples of narrow-range alkoxylation catalysts include many alkaline earth (Mg, Ca, Ba, Sr, etc.) derived catalysts, Lewis acid catalysts such as zirconium dodecanoxide sulfate, and certain boron halide catalysts, such as those described by Dupont, in the form of MB(OR1)x(X)4-x or B(OR1)3 / MX (wherein R1 is an optionally substituted linear, branched, cyclic, or aromatic hydrocarbyl group having 1 to 30 carbon atoms, M is Na+, K+, Li+, R2R3R4R5N+, or R2R3R4R5P+, where R2, R3, R4, and R5 are independently hydrocarbyl groups, and x is 1 to 3). This process can be carried out for a variety of other hydrophobic materials and can be performed using various alkoxylation compounds (e.g., propylene oxide and butylene oxide) by modifying the catalytic properties. A narrow-range ethoxylated alcohol nonionic surfactant contains at least 85% by weight of alcohol ethoxylate nonionic surfactant molecules of the total narrow-range ethoxylate alcohol surfactant, each containing a polyethoxy group with 5 to 12, preferably 6 to 10, ethoxy groups. A broad-range ethoxylated alcohol nonionic surfactant contains a polyethoxy group, preferably 15% to 45% by weight, preferably 25% to 40% by weight of the total broad-range ethoxylated alcohol surfactant, which consists of ethoxylated alcohol nonionic surfactant molecules containing a polyethoxy group with 6 to 10 ethoxy groups, and 30% to 70% by weight, preferably 40% to 65% by weight of the total broad-range ethoxylated alcohol surfactant, which consists of ethoxylated alcohol nonionic surfactant molecules containing a polyethoxy group with 5 to 12 ethoxy groups.Ethoxylated alcohol nonionic surfactants may be derived from natural alcohol sources, synthetic alcohol sources, or mixtures thereof. Most preferred natural sources include palm kernel oil, coconut oil, or mixtures thereof, with palm kernel oil being preferred. When the ethoxylated alcohol nonionic surfactant is derived from a synthetic alcohol source, the synthetic alcohol source is preferably produced via an oxo process, Ziegler process, Guerbet process, aldol condensation process, or a mixture thereof. The resulting alcohol can optionally, but preferably, be further fractionated to increase the C12-C15 content of the starting alcohol. Suitable examples of narrow-range ethoxylated alcohol nonionic surfactants are commercially available from Nouryon under the trade names Berol or Ethylan, and from Sasol under the trade name Novel.

[0037] The laundry detergent composition may contain fatty acids, preferably neutralized fatty acid soap. The fatty acid soap may be an amine neutralized fatty acid soap, and the amine is an alkanolamine, more preferably selected from monoethanolamine, diethanolamine, triethanolamine, monoisopropanolamine, or a mixture thereof, and more preferably monoethanolamine. The laundry detergent composition may contain 1.5% to 20% by weight, preferably 3% to 17% by weight, more preferably 5% to 15% by weight of fatty acids, preferably neutralized fatty acid soap.

[0038] The laundry detergent contains water up to 15% by weight of the composition, preferably 5% to 15% by weight of the detergent composition, and more preferably 7% to 15% by weight of the water.

[0039] metalloproteinase The term "metalloprotease" is used herein in its conventional sense within the field of enzyme research and refers to a protease that requires a bound metal ion to be catalytically active. This is usually the zinc ion. Metalloproteases are preferably neutral metalloproteases, i.e., those that are active even at neutral pH and require a zinc ion for their catalytic effect. The molecular weight of this type of protease is usually in the range of about 30 to about 40 kDa. Neutral metalloproteases are also called "neutral metalloendopeptidases."

[0040] In various embodiments, at least one metalloproteinase is used to target Bacillus amyloricephaciens, Bacillus, Geobacillus, Alicyclobacillus, Lactobacillus, Exigobacterium, Brevibacillus, Paenibacillus, Herpetosiphon, Oceanobacillus, Shewanella, Clostridium, Staphylococcus, Flavobacterium, Stigmatella, Myxococcus, Metanosarkina, Chryseobacterium, Streptomyces, Crybella, Janibacter, Nocardioides, and K Santhomonas, Micromonospora, Burkholderia, Dehalococcoides, Chlorebacter, Cordia, Microsilla, Thermoactinomyces, Chloroflexus, Listeria, Plesiocystis, Hariscomenobacter, Cytophaga, Hahera, Arthrobacter, Brachybacterium, Clavibacter, Microbacterium, Intrasporangium, Frankia, Meiothermus, Pseudomonas, Lycinus, Catenulispora, Anabaena, Nostoc, Halomonas, Chromohalobacter Kutar, Bordetella, Variovorax, Diceya, Pectobacterium, Citrobacter, Enterobacter, Salmonella, Erwinia, Pantoea, Ranella, Geodermatophyllus, Gemata, Xenorhabdus, Photorhabdus, Aspergillus, Neosartria, Pyrenophora, Saccharopolispora, Nectaria, Gibberella, Metallidium, Wadria, Cyanoseis, Serulophaga, Providencia, Brasirhizobium, Agrobacterium, Musilaginibacter, Serratia, Sorah The metalloproteinases are selected from those derived from Langium, Streptosporangium, Renibacterium, Aeromonas, Chromobacterium, Moritera, Hariangium, Candiella, Marinomonas, Vibrioles, Listonella, Salinivibrio, Photobacterium, Alteromonadeles, Legionella, Terezinibacter, Reinecea, Hydrogenibulga, Pseudoalteromonas, Crivella, Thermoscus, Lysobacter, Achromobacter, Aeromonas, and Streptomyces.

[0041] Examples of such metalloproteinases and their variants include those described in International Publication No. 2015 / 158723 (SEQ ID NO: 2), International Publication No. 2015 / 193488 (SEQ ID NO: 2), International Publication No. 2014 / 029819 (SEQ ID NO: 2), International Publication No. 2014 / 029820 (SEQ ID NO: 2 and SEQ ID NO: 4), International Publication No. 2016 / 075078 (SEQ ID NO: 2 and SEQ ID NO: 4), International Publication No. 2014 / 029821 (SEQ ID NO: 2 and SEQ ID NO: 4), International Publication No. 2019 / 105675 (SEQ ID NO: 1), International Publication No. 2019 / 142774, and Japanese Patent No. JP7057140(B2) (SEQ ID NOs: 2, 4, 6, 8).

[0042] Preferably, the protease is selected from the M4, M5, M7, M8, M23, or M35 family, more preferably an M4 metalloprotease, and most preferably a neutral metalloprotease.

[0043] As used herein, the terms “M4 metalloproteinase family,” “M4 metalloproteinase,” or “M4” refer to polypeptides classified into the M4 metalloproteinase family according to Rawlings et al., Biochem. J., 290, 205-218 (1993), and further described in MEROPS- (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270-272, 2006). M4 metalloproteinases are neutral metalloproteinases, primarily endopeptidases. All peptidases in this family bind to a single catalytic zinc ion. Members of the M4 metalloproteinase family contain a common HEXXH motif, where the histidine residue functions as a zinc ligand and glutamic acid is the active site residue. M4 metalloproteinases have pH optimal conditions, primarily at neutral pH. Examples of the M4 metalloprotease family include Neutrase (trademark) (Novozymes) (classified as MEROPS subclass M04.014), thermolysin, basiliolisin, vibriolisin, pseudodrysin, Msp peptidase, cocolicin, oleolisin, vimericin, lambda toxin neutral peptidase B, PA peptidase (Aeromonas type), glycericin, stearolisin, Mprlll (Alteromonas strain 0-7), pap6 peptidase, neutral peptidase (Thermoactinomyces type), ZmpA peptidase (Burkholderia species), zpx peptidase, PrtS peptidase (Photorhabdus luminescence), protearisin, and ZmpB peptidase (Burkholderia species). The M4 metalloprotease family of polypeptides has been further characterized and currently includes at least 22 subclasses, each assigned a distinct MEROPS ID (i.e., an identifier for formula M04.xxx) according to MEROPS, as well as non-peptidase homologs and unassigned peptidases.

[0044] As used herein, the terms “M5 metalloprotease family,” “M5 metalloprotease,” “M5,” or “mycolysin family” refer to polypeptides classified into the M5 metalloprotease family according to Rawlings et al., Biochem. J., 290, 205-218 (1993), and further as described in MEROPS- (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270-272, 2006).

[0045] As used herein, the terms “M7 metalloprotease family,” “M7 metalloprotease,” “M7,” or “snaparicin family” refer to polypeptides classified into the M7 metalloprotease family as described in Rawlings et al., Biochem. J., 290, 205-218 (1993), and further in MEROPS- (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270-272, 2006). The M7 protease family includes the metalloendopeptidase snaparicin.

[0046] As used herein, the terms “M8 metalloproteinase family,” “M8 metalloproteinase,” “M8,” or “Reisimanolicin family” refer to polypeptides classified into the M8 metalloproteinase family according to Rawlings et al., Biochem. J., 290, 205-218 (1993), and further as described in MEROPS- (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270-272, 2006).

[0047] As used herein, the term “M23 metalloprotease family” refers to polypeptides classified into the M23 metalloprotease family as described in Proteolysis in Cell Function, pp13-21, IOS Press, Amsterdam (1997), Rawlings et al., Biochem. J., 290, 205-218 (1993), and further in MEROPS- (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270-272, 2006). The M23 family includes stafolicin and lysostafin.

[0048] As used herein, the terms “M35 metalloprotease family,” “M35 metalloprotease,” “M35,” or “deuterolysin family” refer to polypeptides classified into the M35 metalloprotease family as described in Proteolysis in Cell Function, pp13-21, IOS Press, Amsterdam (1997), Rawlings et al., Biochem. J., 290, 205-218 (1993), and further as described in MEROPS- (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270-272, 2006).

[0049] Preferred metalloproteinases include thermolysin, matrix metalloproteinase, and metalloproteinases derived from Bacillus subtilis, Bacillus thermoproteolisticus, Geobacillus stearothermophilus or Geobacillus species, Bacillus amyloricephasiensis, or Paenibacillus hunanensis. Particularly preferred metalloproteinases belong to the M4 family as described in Rawlings et al., Biochem. J., 290, 205-218 (1993), and further in MEROPS- (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270-272, 2006). Metalloproteinases derived from Paenibacillus hunanensis are particularly preferred for use in this specification.

[0050] In one embodiment, preferred metalloproteases are neutral metalloprotease variants described in International Publication No. 2007 / 044993, International Publication No. 2009 / 058661, and U.S. Patent Application Publication No. 20140315775. In one embodiment, the protease is located at the following positions compared to Sequence ID No. 18 of International Publication No. 2007 / 044993: T004C, T004E, T004H, T004I, T004K, T004L, T004M, T004N, T004P, T004R, T004S, T004V, T004W, T004Y, G012D, G012E, G0 12I, G012K, G012L, G012M, G012Q, G012R, G012T, G012V, G012W, K013A, K013C, K013D, K013 E, K013F, K013G, K013H, K013I, K013L, K013M, K013N, K013Q, K013S, K013T, K013V, K013Y,T014F、T014G、T014H、T014I、T014KJ014L、T014M、T014P、T014Q、T014R、T014S、T014V、T014W、T014Y、S023A、S023D、S023F、S023G、S023I、S023K、S023L、S023M、S023N、S023P、S023Q、S023R、S023S、S023T、S023V、S023W、S023Y、G024A、G024D、G024F、G024G、G024H、G024I、G024K、G024L、G024M、G024N、G024P、G024R、G024S、G024T、G024V、G024W、G024Y、K033H、Q045C、Q045D、Q045E、Q045F、Q045H、Q045I、Q045K、Q045L、Q045M、Q045N、Q045P、Q045R、Q045T、Q045W、N046A、N046C、N046E、N046F、N046G、N046H、N046I、N046K、N046L、N046M、N046P、N046Q、N046R、N046S、N046T、N046V、N046W、N046Y、R047E、R047K、R047L、R047M、R47Q、R047S、R047T、Y049A、Y049C、Y049D、Y049E、Y049F、Y049H、Y049I、Y049K、Y049L、Y049N、Y049R、Y049S、Y049T、Y049V、Y049W、N050D、N050F、N050G、N050H、N050I、N050K、N050L、N050M、N050P、N050Q、N050R、N050W、N050Y、T054C、T054D、T054E、T054F、T054G、T054H、T054I T054K、T054L、T054M、T054N、T054P、T054Q、T054R、T054S、T054V、T054W、T054Y、S058D、S058H、S058I、S058L、S058N、S058P、S058Q、T059A、T059C、T059E、T059G、T059H、T059I、T059K、T059L T059M、T059N、T059P、T059Q、T059R、T059S、T059V,T059W、T060D、T060F、T060I、T060K、T060L、T060N、T060Q、T060R、T060V、T060W、T060Y、T065C、T065E,T065F、T065H、T065I、T065K、T065L、T065M、T065P、T065Q、T065R、T065V、T065Y、S066C、S066D、S066E、S066F、S066H、S066I、S066K、S066L,S066N、S066P、S066Q、S066R、S066T、S066V、S066W、S066Y、Q087A、Q087D、Q087E、Q087H、Q087I、Q087K、Q087L、Q087M、Q087N、Q087R、Q087S、Q087T、Q087V、Q087W、N090C、N090D、N090E、N090F、N090G、N090H、N090K、N090L、N090R、N090T、N096G、N096H、N096K、N096R、K097H、K097Q、K097W、K100A、K100D、K100E1 K100F、K100H、K100N、K100P、K100Q、K100R、K100S、K100V、K100Y、R110A、R110C、R110E、R110H、R110K、R110L、R110M、R110N、R110Q、R110S、R110Y、D119E、D119H、D119I、D119L、D119Q、D119R、D119S、D119T、D119V、D119W、G128C、G128F、G128H、G128K、G128L、G128M、G128N、G128Q、G128R、G128W、G128Y、S129A、S129C、S129D、S129F、S129G、S129H、S129I、S129K、S129L、S129M、S129Q、S129R、S129T、S129V、S129W、S129Y、F130I、F130K、F130L、F130M、F130Q、F130R、F130T、F130V、F130Y、S135P、G136I、G136L、G136P、G136V、G136W、G136Y、S137A,M138I、M138K、M138L、M138Q、M138V、D139A、D139C、D139E、D139G、D139H、D139I、D139K、D139L、D139M、D139P、D139R、D139S、D139V、D139W、D139Y、V140C、Q151I、E152A、E152C、E152D、E152F、E152G、E152H、E152L、E152M、E152N、E152R、E152S、E152W、N155D、N155K、N155Q、N155R、D178A、D178C、D178G、D178H、D178K、D178L、D178M、D178N、D178P、D178Q、D178R、D178S、D178T、D178V、D178W、D178Y、T179A,T179F、T179H、T179I、T179K、T179L、T179M、T179N、T179P、T179Q、T179R、T179S、T179V、T179W、T179Y、E186A、E186C、E186D、E186G、E186H、E186K、E186L、E186M、E186N、E186P、E186Q、E186R、E186S、E186T、E186V、E186W、E186Y、V190H、V190I、V190K、V190L、V190Q、V190R、S191F、S191G、S191H、S191I、S191K、S191L、S191N、S191Q、S191R、S191W、L198M、L198V、S199C、S199D、S199E、S199F、S199I、S199K、S199L、S199N、S199Q、S199R、S 199V、Y204H、Y204T、G205F、G205H、G205L、G205M、G205N、G205R、G205S、G205Y、K211A、K211C、K211D、K211G、K211M、K211N、K211Q、K211R、K211S、K211T、K211V、K214A、K214C、K214E、K214I、K214L、K214M、K214N、K214Q、K214R、K214S、K214V、L216A、L216C、L216F、L216H、L216Q、L216R、L216S、L216Y、N218K、N218P、T219D、D220A、D220E、D220H、D220K、D220N、D220P、A221D、A221E、A221F、A221I,A221K、A221L、A221M、A221N、A221S、A221V、A221Y、G222C、G222H、G222N、G222R、Y224F、Y224H、Y224N、Y224R、T243C、T243G、T243H、T243I、T243K、T243L、T243Q、T243R、T243W、T243Y、K244A、K244C、K244D、K244E、K244F、K244G、K244L、K244M、K244N、K244Q、K244S、K244T、K244V、K244W、K244Y、V260A、V260D、V260E、V260G、V260H、V260I、V260K、V260L,V260M, V260P, V260Q, V260R V260S, V260T, V260W,V260Y, Y261C, Y261F, Y261I, Y261L, T263E, T263F, T263H, T263I, T263L, T263M, T263Q, T263V, T263W, T263Y, S265A, S265C, S265D, S265E, S265K, S265N, S265P, S265Q, S265R, S265T, S265V, S265W, K269E, K269F, K269G, K269H, K269I, K269L, K269M, K269N, K269P, K269Q, K269S, K269T, K269V, K269W, K269Y, A273C, A273D, A273H, A273I, A273K, A273L, A273N, A273Q, A273R, A273Y, R280A, R280C, R280D, R280E, R280F, R280G, R280H, R280K, R280L, R280M, R280S, R280T, R280V, R 280W, R280Y, L282F, L282G, L282H, L282I, L282K, L282M, L282N, L282Q, L282R, L282V, L282Y, S285A, S285C, S285D, S285E, S 285K, S285P, S285Q, S285R, S285W, Q286A, Q286D, Q286E, Q286K, Q286P, Q286R, A289C, A289D, A289E, A289K, A289L, A289R, A These are variants having at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or even 100% identity with Sequence ID No. 18 of International Publication No. 2007 / 044993, including those having one or more substitutions from among 293C, A293R, N296C, N296D, N296E, N296K, N296R, N296V, A297C, A297K, A297N, A297Q, A297R, and G299N.

[0051] In some preferred embodiments, the metalloproteinase is a metalloproteinase variant having at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or even 100% sequence identity with SEQ ID NO: 18 of International Publication No. 2007 / 044993, including substitutions at one or more of the following positions: S129I, S129V, S129L, F130L, M138I, M138L, V190I, D220P (SEQ ID NO: 20 of International Publication No. 2009 / 058661).

[0052] More preferable metalloproteases are derived from members of the Bacillales order, Bacillidae family, Paniebacillidae family, Geobacillidae family, Brevibacillidae family, Paenibacillidae family, Alicyclobacillidae family, Lactobacillidae family, and Exigobacterium species, as described in International Publication Nos. 2014194034 and 2014194117. In one embodiment, the protease is derived from Paenibacillus hunanensis as described in International Publication No. 2014194034. In one embodiment, the protease has at least 80%, or 85%, or 90%, or 95%, or 96%, or 97%, or 98%, or 99%, or even 100%, identity with Sequence ID No. 33 of International Publication No. 2014194034.

[0053] The neutral metalloproteinases of the present invention are also called "neutral metalloendopeptidases" and include enzymes of class EC 3.4.24.

[0054] Suitable commercially available metalloproteinase enzymes include those sold by Novozymes A / S (Denmark) under the trademark name Neutrase®, the Corolase® product range including Corolase® 8000 and Corolase® 7089 from AB Enzymes, Protex 14L and Protex 15L from IFF (Palo Alto, Calif.), those sold by Sigma as Thermolysin, and the Thermoase product range (PC10F and C100) and Thermolysin enzymes sold by Amano enzymes.

[0055] Preferred concentrations of metalloproteinase in the product of the present invention include about 0.05 to about 10 mg per gram of composition, more preferably about 0.5 to about 7 mg, and particularly about 1 to about 6 mg of active metalloproteinase.

[0056] protease The composition of the present invention may contain one or more proteases, and preferably, the composition of the present invention contains at least one protease. A mixture of two or more proteases can contribute to improved washing over a wider temperature, cycle duration, and / or substrate range, and can provide superior washing benefits.

[0057] Suitable proteases for use in combination with metalloproteases are serine proteases, including neutral or alkaline microbial serine proteases such as subtilisin (EC 3.4.21.62). Suitable proteases may be of animal, plant, or microbial origin. In one embodiment, such suitable proteases may be of microbial origin. Suitable proteases may be chemically or genetically modified variants of the aforementioned suitable proteases. In one embodiment, suitable proteases may be alkaline microbial proteases and / or serine proteases such as trypsin-type proteases. Examples of suitable neutral or alkaline proteases include the following: i) Subtilisin (EC 3.4.21.62), particularly International Publication Nos. 2004067737, 2015091989, 2015091990, 2015024739, 2015143360, U.S. Patent Nos. 6,312,936(B1), 5,679,630, 4,760,025, International Publication Nos. 03 / 055974, 03 / 054185, 03 / 054184, 2017 / 215925, German Patent Application Publication No. 102006022216(A1), International Publication Nos. 2015089447, 2015089441, Bacillus species listed in Nos. 2016066756, 2016066757, 2016069557, 2016069563, 2016069569, 2016174234, 2017 / 089093, 2020 / 156419, and 2016 / 183509, as well as Bacillus species such as Bacillus lentus, Bacillus alkarophilus, Bacillus subtilis, Bacillus amyloricephasiens, Bacillus gibsoni, Bacillus akibai, Bacillus clauzi, and Bacillus clarchi. (Specifically, mutations S9R, A15T, V66A, A188P, V199I, N212D, Q239R, N255D, X9E, X200L, X256E, X9R, X19L, X60D (Savinase numbering system)) ii) Subtilisins derived from Bacillus pumilus, such as those described in German Patent Application Publication No. 102006022224(A1), International Publication Nos. 2020 / 221578, 2020 / 221579, and 2020 / 221580 (including variants containing amino acid substitutions at least one of the positions selected from 9, 130, 133, 144, 224, 252, and 271 (BPN' numbering system)). iii) Trypsin-type or chymotrypsin-type proteases such as trypsin (e.g., of porcine or bovine origin) (including Fusarium proteases and chymotrypsin as described in International Publication No. 89 / 06270) iv) Proteases derived from Cerulomonas described in International Publication Nos. 05 / 052161 and 05 / 052146 v) Proteases having at least 90% identity with the subtilase derived from Bacillus species TY145, NCIMB 40339, as described in International Publication No. 92 / 17577 (Novozymes A / S) (including variants of this Bacillus species TY145 subtilase as described in International Publication Nos. 2015024739 and 2016066757).

[0058] The additional proteases preferred in the detergent of the present invention exhibit at least 90%, preferably at least 95%, more preferably at least 98%, even more preferably at least 99%, and especially 100% identity with the wild-type enzyme derived from Bacillus lentus, and are located at the following positions: S9R, A15T, V68A, N76D, N87S, S99D, S99SD, S99A, S101G, S101M, S103A, V104N / I, G118V, G11 A polypeptide comprising one or more, preferably two or more, more preferably three or more mutations from among 8R, 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 illustrated in International Publication No. 00 / 37627 incorporated herein by reference).

[0059] Particularly preferred additional proteases are selected from a group of proteases containing the following mutations (BPN' numbering system) compared to either PB92 wild-type (Sequence ID 2 of International Publication No. 08 / 010925) or subtilisin 309 wild-type (a sequence that follows the PB92 backbone except for containing the natural version of 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

[0060] The most preferred additional protease is the subtyrase variant derived from Bacillus amyloricephaciens (BPN'), described in International Publication No. 2011 / 072117. Particularly useful BPN' variants include mutations in one or more of the following positions: X003Q, X006W, X022Y, X024K, X024Q, X024G, X033T, X045V, X053G, X055P, S063T, X076D, X078N, X087D, X101N, X109Q, X118R, X128A, X128S, X145R, X166Q, X169A, X162Q, X182Q, X183N, S183T, X204Q, X206Y, X217Q, Y217L, X218S, X222Q, X248A, or X254A (in the BPN' numbering system).

[0061] Suitable commercially available additional protease enzymes include: i) Products sold by Novozymes A / S (Denmark) under the trademark names Alcalase®, Savinase®, Primase®, Durazym®, Polarzyme®, Kannase®, Liquanase®, Liquanase Ultra®, Savinase Ultra®, Liquanase® Evity®, Savinase® Evity®, Ovozyme®, Neutrase®, Everlase®, Coronase®, Blaze®, Blaze Ultra®, Blaze® Evity®, Blaze® Exceed, Blaze® Pro, Esperase®, Progress® Uno, Progress® Excel, Progress® Key, Ronozyme®, Vinzon®, and Het Ultra®; Products sold by IFF (formerly Dupont) under the trademark names Maxatase®, Maxacal®, Maxapem®, Properase®, Purafect®, Purafect Prime®, Purafect Ox®, FN3®, FN4®, Excellase®, Ultimase®, and Purafect OXP® and Preferenz®; ii) Products sold by Solvay Enzymes under the trademark names Opticlean® and Optimase®; Available from Henkel / Kemira, namely BLAP (sequence shown in Figure 29 of U.S. Patent No. 5,352,604, having the mutation S99D+S101R+S103A+V104I+G159S, hereinafter referred to as BLAP), BLAP R (BLAP having S3T+V4I+V199M+V205I+L217D), BLAP X (BLAP having S3T+V4I+V205I), and BLAP F49 (BLAP having S3T+V4I+A194P+V199M+V205I+L217D); and those that may contain further mutations 101E / D, S156D, L262E, 206A / L / S / T / , 209K / V / W, 215W, 216N / S / T; and iii) Products sold by BASF under the trademark names Lavergy®, Lavergy® Pro, and Lavergy® C Bright.

[0062] A commercially available protease selected from the group consisting of Properase®, Blaze®, Ultimase®, Everlase®, Savinase®, Excellase®, Blaze Ultra®, BLAP, and BLAP variants (Lavergy® Pro) is particularly preferred for use herein in combination with the metalloprotease of the present invention.

[0063] Preferred concentrations of protease in the product of the present invention include about 0.05 to about 10 mg per gram of composition, more preferably about 0.5 to about 7 mg, and particularly about 1 to about 6 mg of active protease.

[0064] Preferably, the laundry detergent composition contains 5% to 30% by weight, preferably 10% to 30% by weight, of a non-aqueous organic solvent, preferably selected from 1,2-propanediol, dipropylene glycol, tripropylene glycol, glycerol, sorbitol, polyethylene glycol, ethoxylated glycerin, or mixtures thereof. Preferably, the non-aqueous organic solvent contains 1,2-propanediol and glycerol, more preferably in a weight ratio of 1:3 to 12:1, preferably 1:2 to 9:1, and more preferably 1:1 to 6:1. Preferably, the laundry composition contains less than 1% by weight, preferably less than 0.5% by weight, of ethanol, and most preferably, the laundry composition does not contain ethanol.

[0065] Preferably, the laundry detergent composition contains additive components selected from the group including builders, fragrances, enzymes, citrates, bleaches, bleaching catalysts, dyes, color dyes, whitening agents, cleaning polymers (including alkoxylated polyamines and polyethyleneimines), stain-removing polymers, fabric care polymers (including cationic hydroxyethylcellulose, cationic guar gum, and cationic polyglucans), surfactants, solvents, color transfer inhibitors, chelating agents, encapsulated fragrances, polycarboxylates, structuring agents, pH adjusters, antioxidants (including Ralox 35), defoamers, and mixtures thereof.

[0066] Preferably, the laundry detergent composition contains hemicellulase, peroxidase, protease, cellulase, xylanase, lipase, phospholipase, esterase, cutinase, pectinase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, pullulanase, tannase, pentosanase, maranase, β-glucanase, arabinosidase, hyaluronidase, chondroitinase, laccase, xyloglucanase, mannanase, and amylase, nuclease, pectinate lyase, or mixtures thereof, more enzymes selected from the group, preferably protease, amylase, cellulase, lipase, xyloglucanase, mannanase, nuclease, pectinate lyase, and mixtures thereof. Most preferably, the laundry detergent composition contains protease. The detergent article preferably comprises at least two compartments, wherein a metalloproteinase is present in the first compartment and another enzyme is present in the other compartment.

[0067] Preferably, the laundry detergent composition has a pH of 6 to 10, more preferably 6.5 to 8.9, and most preferably 7 to 8, and the pH of the laundry detergent composition is measured as the 10% product concentration in desalinated water at 20°C.

[0068] In the case of liquids, liquid laundry detergent compositions may be Newtonian or non-Newtonian. Preferably, liquid laundry detergent compositions are non-Newtonian. While we do not wish to be bound by theory, non-Newtonian liquids have different properties from Newtonian liquids; more specifically, the viscosity of non-Newtonian liquids depends on the shear rate, whereas Newtonian liquids have a constant viscosity regardless of the shear rate applied. The decrease in viscosity of non-Newtonian liquids when shear is applied is thought to further promote the dissolution of the liquid detergent. The liquid laundry detergent compositions described herein may have any preferred viscosity depending on factors such as the components they are formulated with and the purpose of the composition.

[0069] Manufacturing method Those skilled in the art will recognize the standard techniques for producing the laundry detergent composition and water-soluble unit-dose articles according to the present invention. Those skilled in the art will also recognize the standard techniques and methods for producing the components of the laundry detergent composition according to the present invention.

[0070] How to use A further aspect of the present invention is a method for washing fabric, comprising the steps of: preparing a washing solution by diluting a water-soluble unit-dose article according to the present invention with water 200 to 3000 times, preferably 300 to 2000 times; and bringing the fabric to be treated into contact with the washing solution.

[0071] Preferably, the cleaning solution contains 5 L to 75 L, preferably 7 L to 40 L, more preferably 10 L to 20 L of water. Alternatively, the cleaning solution may contain 35 L to 65 L of water. Preferably, the cleaning solution is at a temperature of 5°C to 90°C, preferably 10°C to 60°C, more preferably 12°C to 45°C, and most preferably 15°C to 40°C. Preferably, the washing of the fabric in the cleaning solution takes 5 to 60 minutes, preferably 5 to 40 minutes, more preferably 5 to 30 minutes, even more preferably 5 to 20 minutes, and most preferably 6 to 18 minutes to complete. Alternatively, the washing of the fabric in the cleaning solution may take 30 to 60 minutes. Preferably, the cleaning solution contains 1 kg to 20 kg, preferably 3 kg to 15 kg, and most preferably 5 to 10 kg of fabric. Preferably, the cleaning solution may contain water of any hardness ranging from 0 gpg to 40 gpg.

[0072] The dimensions and values ​​disclosed herein should not be understood as being strictly limited to the exact numerical values ​​listed. Instead, unless otherwise specified, each such dimension is intended to mean both the listed value and the functionally equivalent range encompassing that value. For example, a dimension disclosed as "40 mm" is intended to mean "approximately 40 mm." [Examples]

[0073] The effect of metalloproteinases on stain removal was tested by varying the concentration of alkyl ethoxy sulfate (AES) surfactants.

[0074] Cleaning test procedure using an automated turgotometer One liter of hard water with a grain per gallon (GPG) of 1.21 US gallons was heated to 30°C and added to each turgot meter pot. 2. 1.7g of detergent was added to the turgotometer washing pot, and then metalloproteinase enzyme was added as shown in Table 1. 3. To ensure complete mixing of the detergent and wash water, the wash water was mixed in a turgotometer at 417 RPM for 1 minute. 4. Ten CFT stain samples (5 x 5 cm) were added to the targot meter pot (two samples per stain type: blood, milk, ink on cotton fabric (C-05), pigment, oil, milk (POM) on cotton fabric (C-10), whole egg with aged carbon black (CB) on cotton fabric (CS-39), grass on cotton fabric (CS-07), aged chocolate soy milk (CSM) on cotton fabric (CS-45), and aged sheep's blood double-coated on cotton fabric (CS-85)). Then, ten 6 x 6 cm SBL 2004 sheets (supplied by WFK-Testgewebe GmbH (Bruggen-Bracht, Germany)) were added, followed by 5 x 5 cm cotton knit ballast (Warwick). A fabric with a total load weight of 60g was obtained by adding Equest (supplied by Consett, United Kingdom). 5. The main cleaning process was simulated by setting the Turgotometer to mix at 208 RPM for 30 minutes. 6. Next, the wash water was removed and replaced with 1 liter of 30°C water at a rate of 21 gallons per grain (GPG). 7. The turgotometer was set to mix at 208 RPM for 5 minutes to simulate the rinse process. 8. The wash water was removed again, and the second replacement was carried out with 1 liter of water at 30 °C with a grain (gpg) of 21 per gallon. 9. The turgotometer was set to mix at 208 RPM for 5 minutes to simulate the second rinse process. 10. Then, all the fabrics were taken out of each pot. 11. Steps 1 to 10 were repeated three more times. 12. The CFT-stained tracer was separated from the wash ballast, tumble dried, packed in aluminum foil to protect it from light and moisture, and then evaluated the next day. 13. The fabrics were analyzed for the L * a * b * values of the unwashed stain, the washed stain, and the unstained fabric using image analysis software. Delta E * calculations were performed, and the levels of both the unwashed stain and the washed stain were determined compared to the unstained fabric using the following formula (where the suffix 1 indicates the value of the unstained fabric and the suffix 2 indicates the value of the unwashed stain or the washed stain):

[0075]

Equation

[0076] The stain removal index (SRI) is the level of stain removal calculated as a percentage as follows: SRI = 100×(A - B) / A. Where A = Delta E of the area of the unstained fabric with stain * B = Delta E of the area of the washed fabric with stain * . Table 2 shows the stain removal results.

[0077] Test formulation: Table 1 shows two reference formulations (Examples A and B) without metalloproteinases, each with a different relative alkyl ethoxy sulfate (AES) content, as well as test formulations (Examples C and 1) containing related metalloproteinases. All four formulations also contain a certain level of traditional protease.

[0078] [Table 1] * comparison 1 Lutensit Z96 (a zwitterionic polyamine manufactured by BASF - a zwitterionic hexamethylenediamine with the following formula: 100% is quaternized, and approximately 40% of the polyethoxy (EO24) groups are sulfonated).

[0079] [ka] 2 Lutensol FP620 - Ethoxylated polyethyleneimine (PEI600 EO20) manufactured by BASF 3 A polyethylene glycol graft polymer containing a polyethylene glycol main chain (Pluriol E6000) and hydrophobic vinyl acetate side chains, comprising a polymer-based polyethylene glycol backbone polymer of 40% by weight and a polymer-based polyethylene glycol backbone polymer of 60% by weight. 4A subtylasase variant derived from Bacillus amyloricephasiensis (BPN'), described in International Publication No. 2011 / 072117. Particularly useful BPN' variants include mutations in one or more of the following positions: X003Q, X006W, X022Y, X024K, X024Q, X024G, X033T, X045V, X053G, X055P, S063T, X076D, X078N, X087D, X101N, X109Q, X118R, X128A, X128S, X145R, X166Q, X169A, X162Q, X182Q, X183N, S183T, X204Q, X206Y, X217Q, Y217L, X218S, X222Q, X248A, or X254A (in the BPN' numbering system). 5 SEQ ID NO: 20-Level = Active protein level in washing solution, metalloproteinase was added to the washing solution separately from the rest of the detergent composition. (International Publication No. 2009 / 058661)

[0080] Test results: Table 2 summarizes the average stain removal performance of four different test legs across a set of protease-sensitive stains. The results show that the effect of metalloproteinase addition on performance is higher at lower relative AES content according to the present invention (index 145) compared to metalloproteinase addition at higher relative AES content outside the scope of the present invention (index 130).

[0081] [Table 2]

Claims

1. A water-soluble unit-dose detergent article comprising a water-soluble film and a liquid laundry detergent composition, wherein the detergent composition is A non-soap surfactant system comprising an anionic non-soap surfactant and a nonionic surfactant, wherein the anionic non-soap surfactant comprises an anionic non-soap surfactant selected from the group consisting of alkyl sulfates, alkoxylated alkyl sulfates, and mixtures thereof, in an amount of more than 0% by weight and less than 20% by weight of the anionic non-soap surfactant. Metalloproteinases, and A water-soluble unit-dose detergent article comprising up to 15% by weight of water in the aforementioned composition.

2. The detergent article according to claim 1, wherein the anionic non-soap surfactant comprises a linear alkylbenzene sulfonate.

3. The detergent article according to claim 2, wherein the anionic non-soap surfactant comprises at least 80% by weight of a linear alkylbenzene sulfonate.

4. The detergent article according to any one of claims 1 to 3, wherein the detergent composition comprises 30% to 65% by weight of the non-soap surfactant system.

5. The detergent article according to any one of claims 1 to 4, wherein the nonionic surfactant is selected from the group consisting of primary alcohol ethoxylate nonionic surfactants, secondary alcohol ethoxylate nonionic surfactants, and mixtures thereof.

6. The detergent article according to any one of claims 1 to 5, wherein the detergent composition comprises 5% to 30% by weight of an organic solvent, the organic solvent is preferably selected from the group consisting of 1,2-propanediol, dipropylene glycol, tripropylene glycol, glycerol, sorbitol, polyethylene glycol, ethoxylated glycerin, and mixtures thereof.

7. The detergent article according to any one of claims 1 to 6, wherein the weight ratio of the anionic non-soap surfactant to the nonionic surfactant is greater than 1.5:1 to 10:1, preferably 2:1 to 5:

1.

8. The detergent article according to any one of claims 1 to 7, wherein the detergent composition further comprises a fatty acid, preferably the detergent composition comprising 1.5% to 20% by weight of the fatty acid.

9. The detergent article according to any one of claims 1 to 8, wherein the metalloproteinase is a metalloproteinase selected from the M4, M7, M23, or M35 family, preferably a metalloproteinase from the M4 family.

10. The detergent article according to any one of claims 1 to 9, wherein the metalloproteinase is a metalloproteinase variant having at least 80%, preferably at least 90%, preferably at least 95%, preferably at least 98%, and more preferably at least 99% sequence identity with the metalloproteinase of Sequence ID No. 18 of International Publication No. 2007 / 044993.

11. The detergent article according to any one of claims 1 to 9, wherein the metalloproteinase is a metalloproteinase variant having at least 80%, preferably at least 90%, preferably at least 95%, preferably at least 98%, and more preferably at least 99% sequence identity with the metalloproteinase of Sequence ID No. 2009 / 058661 or the metalloproteinase of Sequence ID No. 33 of International Publication No. 2014 / 194034.

12. The detergent article according to claim 10, wherein the metalloproteinase is a metalloproteinase variant having at least 80%, preferably at least 90%, preferably at least 95%, preferably at least 98%, more preferably at least 99% sequence identity with the metalloproteinase of SEQ ID NO: 18 of International Publication No. 2007 / 044993, preferably having at least 80%, preferably at least 90%, preferably at least 95%, preferably at least 98%, more preferably at least 99% sequence identity with the metalloproteinase of SEQ ID NO: 18 of International Publication No. 2007 / 044993.

13. The detergent article according to any one of claims 1 to 12, wherein the detergent composition further comprises an additional enzyme selected from the group consisting of protease, amylase, cellulase, lipase, xyloglucanase, mannanase, nuclease, pectin acid lyase, and mixtures thereof, preferably the additional enzyme further comprises an additional enzyme which includes at least a protease.

14. The detergent article according to claim 13, wherein the article comprises at least two compartments, a first compartment containing the metalloproteinase and a second compartment containing a further enzyme.

15. The detergent article according to any one of claims 1 to 14, wherein the detergent composition further comprises an alkanolamine selected from the group including monoethanolamine, diethanolamine, triethanolamine, and mixtures thereof, preferably monoethanolamine.

16. The detergent article according to any one of claims 1 to 15, wherein the detergent composition has a pH of 6 to 10 when measured in a 10% by weight desalted aqueous solution at 20°C.

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