Water-soluble unit dose articles containing metalloproteinases

Abstract

This invention provides a new water-soluble unit-dose detergent article that offers excellent protein stain removal and good overall cleaning. [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 at least 80% by weight, preferably at least 90% by weight, of the anionic non-soap surfactant as linear alkylbenzene sulfonate, the composition comprises up to 15% by weight of water, serine protease, metalloproteinase, and the weight ratio of the non-soap anionic surfactant to the nonionic surfactant is greater than 1.5:1.

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] There are several reasons for formulating water-soluble unit-dose articles containing different detergent compositions, which can be determined by factors such as the availability of raw materials, the compatibility between raw materials, and the compatibility between raw materials and water-soluble films. Formulating higher levels of anionic non-soap surfactants compared to nonionic surfactants is typically advantageous for grease stain removal performance, but such a formulation approach typically presents challenges for enzyme-sensitive stain removal performance. Water-soluble unit-dose detergent articles should be formulated to provide good overall cleaning, i.e., cleaning of different types of stains, including both grease, sebum, and enzyme-sensitive stains, including protein stain removal and whiteness. [Overview of the project] [Problems that the invention aims to solve]

[0004] Therefore, there is a need to provide a new water-soluble unit-dose detergent article that offers good protein stain removal and good overall cleaning. [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 water-soluble unit-dose detergent article comprising a non-soap surfactant system containing an anionic non-soap surfactant and a nonionic surfactant. The anionic non-soap surfactant is at least 80% by weight, preferably at least 90% by weight, of the anionic non-soap surfactant, Moisture content of less than 15% by weight of the composition Serine protease, Contains metalloproteinase, The weight ratio of non-soap anionic surfactants to nonionic surfactants is greater than 1.5:1.

[0006] The detergent provides excellent protein stain removal. [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, the water solubility of the film is at least 50%, preferably at least 75%, or even more than 95%, when measured by the method described herein after using a glass filter with a maximum pore size of 20 micrometers.

[0018] Add 5 grams ± 0.1 grams of 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 set at 600 rpm (Labline model number 1250 or equivalent and a 5 cm magnetic stirrer). Next, filter the mixture through a pleated qualitative sintered glass filter with the pore size (maximum 20 micrometers) 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 fraction or dispersed fraction). Next, the percentage of solubility or dispersibility can be calculated.

[0019] Preferred film materials are preferably polymeric materials. The film materials can be obtained by, for example, casting, blow molding, extrusion or coextrusion of polymeric materials known in the art.

[0020] Preferred polymers, copolymers or derivatives thereof suitable for use as pouch materials are selected from polyvinyl alcohol, polyvinyl pyrrolidone, polyalkylene oxide, acrylamide, acrylic acid, cellulose, cellulose ether, cellulose ester, cellulose amide, polyvinyl acetate, polycarboxylic acid and salts, polyamino acids or peptides, polyamides, polyacrylamides, copolymers of maleic acid / acrylic acid, polysaccharides including starch and gelatin, and natural gums such as xanthan and carrageenan. More preferred polymers are selected from polyacrylates and water-soluble acrylate copolymers, methylcellulose, sodium carboxymethylcellulose, dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylate, and most preferably from polyvinyl alcohol, polyvinyl alcohol copolymers and hydroxypropylmethylcellulose (HPMC), and combinations thereof. Preferably, the concentration of the polymer in the pouch material, for example, the 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, even more preferably about 20,000 to 150,000.

[0021] Preferably, the water-soluble film contains a polyvinyl alcohol polymer, preferably a polyvinyl alcohol homopolymer or polyvinyl alcohol copolymer, or a mixture thereof, preferably a blend of polyvinyl alcohol homopolymer and / or 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 polyvinyl alcohol homopolymer and 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.

[0022] A preferred film is one that exhibits good solubility in cold water, i.e., unheated distilled water. Preferably, such a film exhibits good solubility at a temperature of 24°C, and more preferably at a temperature of 10°C. Good solubility means that the film exhibits water solubility of at least 50%, preferably at least 75%, or even more preferably at least 95%, when measured by the method herein after using a glass filter with a maximum pore size of 20 micrometers as described above.

[0023] Preferred films include those supplied by Monosol under product reference numbers M8630, M8900, M8779, and M8310.

[0024] The film may be opaque, transparent, or translucent. The film may include printed areas. The printed areas can be obtained using standard techniques such as flexographic printing or inkjet printing.

[0025] 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.

[0026] 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.

[0027] 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.

[0028] The laundry detergent composition may be used for hand washing of fabrics or for washing fabrics in an automatic washing machine.

[0029] 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.

[0030] 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. The weight ratio of the non-soap surfactant to the nonionic surfactant is greater than 1.5:1, preferably greater than 1.5:1 to 8:1, and more preferably 2:1 to 5:1.

[0031] The non-soap anionic surfactant contains at least 80% by weight, preferably at least 90% by weight, of linear alkylbenzene sulfonate. More preferably, the anionic non-soap surfactant consists of a linear alkylbenzene sulfonate anionic surfactant. The anionic non-soap anionic surfactant preferably contains less than 1% by weight, more preferably less than 0.1% by weight, of alkyl sulfate, alkoxylated alkyl sulfate, or a mixture thereof. Most preferably, the anionic non-soap surfactant does not contain alkyl sulfate and / or alkoxylated alkyl sulfate anionic surfactants, and in particular does not contain alkoxylated alkyl sulfate anionic surfactants.

[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] Non-soap anionic surfactants include linear alkylbenzene sulfonates. Preferably, the linear alkylbenzene sulfonate is C 10 ~C16 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 may preferably be 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.

[0034] 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 35% by weight, or 10% to 30% by weight, or 15% to 25% 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. The narrow-range ethoxylated alcohol nonionic surfactant comprises alcohol ethoxylate nonionic surfactant molecules, which constitute at least 85% by weight of the total narrow-range ethoxylate alcohol surfactant, and which contain polyethoxy groups comprising 5 to 12, preferably 6 to 10, ethoxy groups.The broad-spectrum ethoxylated alcohol nonionic surfactant contains polyethoxy groups, preferably 15% to 45% by weight, preferably 25% to 40% by weight of the total broad-spectrum ethoxylated alcohol surfactant, which consists of ethoxylated alcohol nonionic surfactant molecules containing polyethoxy groups with 6 to 10 ethoxy groups, and 30% to 70% by weight, preferably 40% to 65% by weight of the total broad-spectrum ethoxylated alcohol surfactant, which consists of ethoxylated alcohol nonionic surfactant molecules containing polyethoxy groups with 5 to 12 ethoxy groups. The ethoxylated alcohol nonionic surfactant may be derived from a natural alcohol source, a synthetic alcohol source, or a mixture thereof. The most preferred natural sources include palm kernel oil, coconut oil, or a mixture 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.

[0035] 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, wherein 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.

[0036] 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.

[0037] 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."

[0038] 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.

[0039] Examples of such metalloproteinases and their variants are 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).

[0040] 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.

[0041] 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.

[0042] 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).

[0043] 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.

[0044] 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).

[0045] 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.

[0046] 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).

[0047] 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.

[0048] 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.

[0049] 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).

[0050] 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.

[0051] The neutral metalloproteinases of the present invention are also called "neutral metalloendopeptidases" and include enzymes of class EC 3.4.24.

[0052] 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.

[0053] 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.

[0054] Serine protease The composition of the present invention comprises one or more proteases. A mixture of two or more proteases can contribute to improved washing over a wider temperature, cycle duration, and / or substrate range, providing superior washing benefits.

[0055] Suitable proteases for use in combination with metalloproteases include 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 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 as described in International Publication Nos. 05 / 052161 and 05 / 052146, and 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).

[0056] 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).

[0057] 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

[0058] 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).

[0059] 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®; iii) Those 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, hereafter 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); those that may contain further mutations 101E / D, S156D, L262E, 206A / L / S / T / , 209K / V / W, 215W, 216N / S / T; and iv) Products sold by BASF under the trademark names Lavergy®, Lavergy® Pro, and Lavergy® C Bright.

[0060] 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.

[0061] Preferred concentrations of protease in the product of the present invention include about 0.05 to about 10 mg of active protease per gram of composition, more preferably about 0.5 to about 7 mg, and particularly about 1 to about 6 mg.

[0062] 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.

[0063] 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.

[0064] 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 in addition to metalloproteinase. The detergent article preferably comprises at least two compartments, the first compartment containing a metalloproteinase and the other compartment containing a serine protease and / or another enzyme according to the present invention.

[0065] 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.

[0066] 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.

[0067] 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.

[0068] 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.

[0069] 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, 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, 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, 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.

[0070] 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]

[0071] The effect of metalloproteinases on stain removal was tested by varying the ratio of non-soap anionic surfactants to nonionic surfactants.

[0072] Cleaning test procedure using an automated turgotometer 1. One liter of hard water at a grain per gallon (GPG) of 8 US gallons was heated to 30°C and added to each turgot meter pot. 2. 1.1 g of detergent was added to the turgotometer washing pot, and then the enzyme was added as shown in Tables 1 and 2. 3. Eight CFT stain samples (5 x 5 cm) were added to a turgot meter pot (two samples per stain type: Pigment, Oil, Milk, POM (CFT C-10), Whole Egg with Aged Carbon Black on Cotton Fabric (CS-39), Aged Chocolate Soymilk (CSM) Drink on Cotton Fabric (CFT CS-45), and Aged Sheep's Blood (CFT CS-85) applied in a double layer to the cotton fabric). Subsequently, a 5 x 5 cm cotton knit ballast (supplied by Warwick Equest, Consett, United Kingdom) was added to obtain a fabric with a total load weight of 60 g. 4. The Turgotometer was set to mix at 208 RPM for 17 minutes to simulate the main cleaning process. 5. Next, the wash water was removed and replaced with 1 liter of 8-gallon grain (GPG) water at 15°C. 6. The turgotometer was set to mix at 208 RPM for 5 minutes to simulate the rinsing process. 7. Next, all the fabrics were removed from each pot. 8. Steps 1-8 were repeated three more times. 9. Tracers with CFT stains were separated from the cleaned ballast and air-dried overnight. 10. The dried stain was evaluated for stain removal using the L reading obtained with a shutter speed of 1 / 2 and aperture 8, calibrated before use, with DigiEye (VeriVide Ltd, Leicester, UK). * a * b * The readings were used to evaluate stain removal. * a * b * Measurements were taken for unwashed stains, washed stains, and unstained fabric, and Delta E calculations were performed to determine the level of stain for both unwashed and washed stains compared to the unstained fabric using the following formula. In the formula, suffix 1 indicates the value for the unstained, and suffix 2 indicates the value for the unwashed or washed stain. * The stain removal index (SRI) was calculated as a percentage of the level of stain removal as follows: SRI = 100×(A - B) / A.

[0073]

Equation

[0074] Where A = Delta E of the area of the fabric with unwashed stain A = Delta E of the stained area of the unwashed fabric * B = Delta E of the stained area of the washed fabric * .

[0075] Tables 3 and 4 show the stain removal results.

[0076] Test formulations:[[ID=G44]] Table 1 shows four metalloproteinase-free reference formulations with varying ratios of non-soap anionic surfactant to nonionic surfactant. Table 2 shows test formulations containing the relevant metalloproteinases. Examples E and F have non-soap anionic surfactant to nonionic surfactant ratios outside the scope of the present invention, while Examples 1 and 2 have non-soap anionic surfactant to nonionic surfactant ratios according to the present invention. All eight formulations also contain a certain level of serine protease. The metalloproteinases were added to the washing solution separately from the metalloproteinase-free base formulations.

[0077] [Table 1] * comparison 1 A 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). → ppm level = level of active enzyme in the washing solution 2 Sequence ID No. 20 of International Publication No. 2009 / 058661; → ppm level = level of active oxygen in the washing solution

[0078] [Table 2] * comparison

[0079] Test results: Table 3 summarizes the stain removal performance of different test legs across a set of protease-sensitive stains. The table illustrates that in the absence of metalloproteinase, increasing the ratio of non-soap anionic surfactant to nonionic surfactant results in a significant decrease in performance. This significant decrease in performance is not observed further with the addition of a single change of metalloproteinase.

[0080] Table 4 summarizes the effect of single-change metalloproteinase addition on performance. The data in Table 4 show that the effect of metalloproteinases increases more strongly as the weight ratio of non-soap anionic to nonionic surfactants increases. A more robust overall performance profile across surfactant ratios is obtained in the presence of metalloproteinases.

[0081] [Table 3]

[0082] [Table 4]

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 at least 80% by weight, preferably at least 90% by weight, of the anionic non-soap surfactant, a linear alkylbenzene sulfonate. Up to 15% by weight of water in the above composition, Serine protease, Contains metalloproteinase, A water-soluble, unit-dose detergent article having a weight ratio of non-soap anionic surfactant to nonionic surfactant greater than 1.5:

1.

2. The detergent article according to claim 1, wherein the anionic non-soap surfactant comprises at least 95% by weight, preferably at least 99% by weight, of the anionic non-soap surfactant, and more preferably consists of a linear alkylbenzene sulfonate.

3. The detergent article according to claim 1 or 2, wherein the detergent composition comprises 30% to 65% by weight of the non-soap surfactant system.

4. The detergent article according to any one of claims 1 to 3, wherein the anionic non-soap surfactant comprises less than 1% by weight, preferably less than 0.1% by weight, of the anionic non-soap surfactant, and more preferably does not contain alkyl sulfate and / or alkoxylated alkyl sulfate anionic surfactant.

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, or 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 M4 metalloproteinase.

10. The detergent article according to any one of claims 1 to 9, wherein the metalloproteinase is a metalloproteinase variant having at least 60%, preferably at least 80%, more preferably at least 90% sequence identity with the metalloproteinase of Sequence ID No. 18 of International Publication No. 2007 / 044993, having one or more mutations selected from the group consisting of S129I, S129V, S129L, F130L, M138L, V190I, and D220P.

11. The detergent article according to claim 9, wherein the metalloproteinase is a metalloproteinase variant having at least 60%, preferably at least 80%, and more preferably at least 90% sequence identity with the metalloproteinase of Sequence ID No. 33 of International Publication No. 2014194034.

12. The serine protease is located at 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, X A detergent article according to any one of claims 1 to 11, which is a subtilase mutant derived from Bacillus amyloricephaciens (BPN') comprising at least one mutation from one or more of 183N, S183T, X204Q, X206Y, X217Q, Y217L, X218S, X222Q, X248A, or X254A (in the BPN' numbering system).

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, pectinate lyase, and mixtures thereof.

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 the serine protease and / or any of the additional enzymes described in claims 1 to 13.

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 comprising 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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