Detergents and cleaning agents with improved cleaning performance against greasy stains

Abstract

The present invention relates to a detergent and / or cleaning agent comprising at least one peptide and at least one enzyme having hydrolytic activity on ester bonds, preferably selected from the group consisting of lipases and esterases, in particular esterases having lipolytic activity, especially preferred lipases, wherein the peptide is suitable to adhere to an oil and / or fat containing and / or oil containing surface, or a surface coated with oil and / or fat, or a surface provided with at least one oil and / or fat containing and / or oil containing stain, and the surface is selected from the group consisting of hard surfaces, more preferably surfaces comprising or consisting of ceramic (e.g. porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, lacquered and enamel surfaces, wood, laminate, linoleum and mixtures thereof, especially preferred tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g. tableware or pots) or glass and mixtures thereof, especially preferred tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g. tableware or pots) or glass, and / or textiles, more preferably textiles comprising or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, especially preferred cotton, polyester and mixtures thereof. The present invention further relates to a method for cleaning hard surfaces and / or textiles, the use of such peptides and a formulation for improving the cleaning performance on at least one oil and / or fat containing and / or oil containing stain.

Description

Technical Field

[0001] This invention relates to a detergent and / or cleaning agent comprising at least one peptide and at least one enzyme having hydrolytic activity against ester bonds, wherein the enzyme is preferably selected from lipases and esterases, particularly esterases having fat-decomposing activity, especially lipases, wherein the peptide is adapted to adhere to grease- and / or oily surfaces, or surfaces coated with grease and / or oil, or surfaces having at least one grease- and / or oily stain, and wherein the surface is selected from hard surfaces, more preferably comprising or composed of ceramics (e.g., porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamel surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass and mixtures thereof, and / or textiles, more preferably comprising or composed of textiles such as cotton, polyester, polyamide, polypropylene and mixtures thereof, especially preferably cotton, polyester and mixtures thereof. The present invention also relates to methods for cleaning hard surfaces and / or textiles, uses of such peptides, and formulations for improving cleaning performance against at least one grease and / or oil stain.

[0002] In particular, peptides that specifically bind to or interact with oxidized surfaces such as metal surfaces, as well as peptides that specifically bind to plastic material surfaces, have been described (WO 2014 / 072313 A1, WO 2023 / 110572 A1). However, adhesive peptides are also significant for many other surfaces, especially for functionalizing such surfaces or endowing them with other desired properties.

[0003] For example, so-called “functional polymers” are known to be used in detergents and cleaning agents, such as “stain-removing polymers” in detergents to improve stain removal from textiles, or “stain-resistant polymers” in detergents to prevent / reduce stain buildup on textiles. These stain-removing polymers (SRPs) are water-soluble or water-dispersible condensation polymers based on dicarboxylic acids and glycols or cellulose ethers. SRPs can have a positive impact on the ability to wash oils and greases out of textiles. Typical SRPs are based on copolymers of, for example, polyesters and polyethers, and also on terephthalates, such as polypropylene terephthalate. However, these polymers are not biodegradable. Therefore, there is a need for alternatives or improvements, particularly biodegradable SRPs and / or their substitutes, for use in detergents and / or cleaning agents.

[0004] Dispersed polymers, used in automatic dishwasher detergents to prevent or reduce stain buildup, perform a similar function. These are typically (co)polymerized polycarboxylate esters, such as poly(meth)acrylates, or polymers based on (meth)acrylic acid containing sulfonic acid groups. However, the biodegradability of such polymers is currently limited, and therefore, alternative, biodegradable alternatives are being sought for dishwashers.

[0005] Grease and / or oil stains on hard surfaces and / or textiles are considered a more stubborn type of stain and are not easily removed. In conventional washing and / or cleaning methods, these stains are removed by first liquefying the grease through washing and / or cleaning temperatures (typically between approximately 40°C and 60°C), and then removing it from the surface by surfactants present in the detergent and / or cleaning agent (“curling mechanism”). The removed liquefied fat molecules are then carried away mechanically during washing and / or rinsing, i.e., rinsed away. Additionally or alternatively, grease and / or oil stains can be removed by esterases, lipases, or fat-degrading enzymes, as these enzymes break down grease and / or oil, and the breakdown products are subsequently rinsed away. However, the use of lipases can produce an unpleasant odor on washed items, especially textiles, after the washing process, because the lipases are adsorbed by the textiles and also hydrolyze fatty acid esters into low molecular weight fatty acids. These low molecular weight fatty acids are perceived as having an unpleasant odor. The intensity of the odor may vary depending on the condition of the textile. Therefore, there is currently no satisfactory alternative for removing grease and / or oily stains at low temperatures, i.e., below 40°C, especially for example at about 20°C or about 30°C, because grease does not liquefy or liquefies insufficiently at temperatures below about 30°C or about 40°C.

[0006] The inventors have discovered and developed specific peptides that are unexpectedly suitable for adhesion to greasy and / or oily surfaces as described herein, thereby allowing the removal of at least one greasy and / or oily stain from the surface, and consequently enabling improved cleaning performance of detergents and / or cleaning agents containing them for at least one greasy and / or oily stain. Furthermore, the inventors have found that, in particular, the combination of a lipase and at least one peptide according to the invention results in improved removal of at least one greasy and / or oily stain from the surface.

[0007] Within the scope of this invention, "grease- and / or oily surface" is understood to mean a surface containing or composed of grease and / or oil, and / or a surface coated with grease and / or oil, and / or a surface soiled with at least one grease- and / or oily stain. Within the scope of this invention, "grease" is understood to mean a macromolecule formed from glycerol and fatty acids, in addition to monoglycerides and diglycerides, particularly so-called triglycerides or triglycerides, wherein three fatty acids are combined with glycerol. All known fatty acids having 8 to 36, preferably 10 to 24 carbon atoms, including monounsaturated or polyunsaturated fatty acids and saturated fatty acids, are also covered by this invention. Within the scope of this invention, "oil" or "oils" is understood to mean a fatty substance that is liquid or flowable at room temperature and immiscible with water. This invention includes synthetic and biological fats and / or oils. Within the scope of this invention, "grease- and / or oily stain" is understood to mean a stain on a surface, particularly a hard surface and / or a textile surface, containing or composed of grease and / or oil. Typical examples of grease and / or oily stains include grease and / or oily foods and food residues, such as vegetable fats (e.g., coconut oil), animal fats (e.g., butter, clarified butter), edible oils (e.g., olive oil, sunflower oil, rapeseed oil), frying oils, mayonnaise, margarine, deep fryer grease, meat fats (e.g., beef tallow, lard, pork fat), as well as burnt food residues, and / or synthetic fats and / or oils, such as mineral oils and / or mineral greases, engine oils, bicycle chain oils, pigmented greases, pigmented oils, and / or fats and / or oils from personal care products, such as lipstick, cosmetics, lotions, creams, and / or body oil residues, such as sebum, grease. In a preferred embodiment, the grease-containing surface contains or consists of grease that is solid at room temperature. In a preferred embodiment, the grease-coated surface is coated with grease that is solid at room temperature. In a preferred embodiment, the surface with at least one grease-containing stain is provided with or soiled by at least one solid grease, i.e., the at least one grease-containing stain preferably contains or consists of grease that is solid at room temperature.

[0008] Within the scope of this invention, surfaces containing grease and / or oil and / or coated with grease and / or oil and / or having at least one grease and / or oil stain are preferably selected from hard surfaces and / or textiles.

[0009] Preferably, the grease- and / or oily surface and / or surface coated with grease and / or oil and / or surface with at least one grease- and / or oily stain is a hard surface comprising or composed of ceramics (e.g., porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamel surfaces, wood, laminate, linoleum and mixtures thereof, especially preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass.

[0010] Preferably, a grease- and / or oily surface and / or a surface coated with grease and / or oil and / or a surface with at least one grease- and / or oily stain is a textile surface. The term “textile surface” as used herein is synonymous with the term “textile” or “textile.” The term “textile” or “textile” as used herein means any textile material, including yarns, yarn precursors, fibers, nonwovens, natural materials, synthetic materials, and all other textile materials, fabrics made from these materials, and products made from fabrics (e.g., clothing and other articles). Textiles or fabrics can be in the form of knitted fabrics, woven fabrics, denim, nonwovens, felt, yarns, and terry cloth. Textiles can be based on cellulose, such as natural cellulose fibers like cotton, flax / linen, jute, ramie, sisal, or coconut fiber, or synthetically produced cellulose fibers (e.g., from pulp) such as viscose / rayon, cellulose acetate fiber (triacetate fiber), lyocell fiber, or mixtures thereof. Textiles or fabrics may also be composed of non-cellulose fibers, such as natural polyamides like wool, camel hair, cashmere, mohair, rabbit hair, and silk, or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene, and spandex / elastomeric fibers or mixtures thereof, as well as mixtures of cellulose and non-cellulose fibers. Examples of blends are blends of cotton and / or rayon / viscose fibers with one or more accompanying materials such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers) and / or cellulose-containing fibers (e.g., rayon / viscose fibers, ramie, flax / linen, jute, cellulose acetate fibers, lyocell fibers). Fabrics can be conventionally washable, such as soiled household clothes. When the terms "fabric" or "clothing" are used, it is intended to include the broader term "textiles." Textiles containing or composed of cotton, polyester, polyamide, polypropylene, and mixtures thereof are preferred, with cotton, polyester, and mixtures thereof being particularly preferred.

[0011] The present invention particularly preferably relates to a hard surface and / or textile having at least one grease- and / or oil stain, i.e., soiled with grease, wherein the hard surface is preferably selected from tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, and the textile contains or is composed of cotton, polyester and mixtures thereof.

[0012] The substrate-specific peptides adhere to grease and / or oily surfaces, particularly as defined herein, i.e., to at least one grease and / or oily stain on surfaces (as described herein), preferably selected from hard surfaces, tableware (preferably made of ceramics such as porcelain or stoneware and plastics), metals (e.g., cutlery or pots), or glass, and textiles, preferably textiles containing or composed of cotton, polyester, and mixtures thereof, wherein functional groups can selectively bind to grease and / or oil molecules on the surface. This enables substrate-specific removal of grease and / or oily stains. The peptides of the present invention, which specifically bind to grease and / or oil on the surface, preferably solid grease, or grease and / or oily stains, preferably grease-containing stains, can therefore be used for targeted removal of said grease and / or oil, particularly solid grease, from surfaces.

[0013] In a particularly preferred embodiment, the peptide according to the invention enables the improvement of the cleaning performance of detergents and / or cleaning agents on at least one grease- and / or oil-containing stain on a surface, wherein the surface is selected from hard surfaces, preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, and / or textiles, particularly textiles containing or composed of cotton, polyester and mixtures thereof.

[0014] Therefore, in a first aspect, the present invention relates to a detergent and / or cleaning agent comprising (A) At least one peptide, wherein the peptide is selected from... a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3Selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or b) A peptide having an amino acid sequence identity of at least 80%, and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%, with one of the amino acid sequences listed in SEQ ID NOs: 1-31; and (B) At least one enzyme that has hydrolytic activity against ester bonds, preferably selected from lipases and esterases, especially esterases with lipolytic activity, and particularly preferably lipases.

[0015] In a preferred embodiment, the peptide has an amino acid sequence that is 80% identical to one of the amino acid sequences listed in SEQ ID NOs: 1-31, and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%; preferably, the peptide has an amino acid sequence according to one of the amino acid sequences listed in SEQ ID NOs: 1-31, more preferably an amino acid sequence of one of SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, and particularly preferably an amino acid sequence of one of SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0016] In a preferred embodiment, the at least one enzyme with hydrolytic activity against ester bonds is a lipase, wherein the lipase is selected from... (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in sequence over its entire length at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38, preferably 100%.

[0017] In a preferred embodiment, the peptide binds to an oily surface or a surface coated with oil or having at least one oily and / or greasy stain, and the surface is preferably selected from hard surfaces, more preferably surfaces comprising or composed of ceramics (e.g., porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamel surfaces, wood, laminate, linoleum and mixtures thereof, especially preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, and / or textiles, more preferably textiles comprising or composed of cotton, polyester, polyamide, polypropylene and mixtures thereof, especially preferably cotton, polyester and mixtures thereof, wherein the adhesion is determined as described in Example 2.

[0018] In other respects, the present invention relates to preferred embodiments of the formulations described herein.

[0019] Other subjects of the present invention relate to - A method for cleaning textiles, particularly textiles containing or composed of cotton, polyester and mixtures thereof, and / or for cleaning hard surfaces, particularly tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, wherein a detergent and / or cleaning agent as described herein is used in at least one method step. - A method for cleaning textiles, particularly textiles containing or composed of cotton, polyester and mixtures thereof, and / or for cleaning hard surfaces, particularly tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, wherein in a first step, the at least one peptide is brought into contact with the article to be washed or rinsed, and in a second step, the at least one lipase is brought into contact with the article to be washed or rinsed. - A method for cleaning textiles, particularly textiles containing or composed of cotton, polyester and mixtures thereof, and / or for cleaning hard surfaces, particularly tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, wherein the method is carried out in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, and very particularly preferably about 20°C; - The formulations described herein are used for cleaning textiles, particularly those containing or composed of cotton, polyester, and mixtures thereof, and / or for cleaning hard surfaces, particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass. - The use of peptides as described herein in detergents and / or cleaning agents to improve the cleaning performance of detergents and / or cleaning agents on at least one grease and / or oil stain, preferably grease stain; - The use of peptides as described herein as detergency, particularly degreasing and / or oil-removing active ingredients in detergents and / or cleaning agents; - Use in the temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, and very particularly preferably about 20°C.

[0020] These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art upon studying the following detailed description and claims. Any feature of one aspect of the invention may be used in any other aspect of the invention. Furthermore, it should be readily understood that the embodiments contained herein are intended to describe and illustrate, and not to limit, the invention, and in particular, is not limited to these embodiments.

[0021] Unless otherwise stated, all percentages are by weight (wt.%), and in each case are based on the total weight of the respective composition or formulation.

[0022] Numerical ranges expressed in the format "from x to y" also include the mentioned values. If several preferred numerical ranges are specified in this format, it is readily understood that any range resulting from combinations of different endpoints is also included.

[0023] As used herein, “at least one” means one or more, i.e., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14 or more. Regarding an ingredient, it refers to the type of ingredient, not the absolute number of molecules. “At least one peptide” therefore means, for example, at least one type of peptide, i.e., it can mean one type of peptide or a mixture of several different peptides. Along with weight information, this information pertains to all compounds of the specified type present in the formulation, i.e., the formulation generally does not contain any other compound of that type in greater quantities than the specified amount of the corresponding compound.

[0024] As used herein, “about” or “approximately” for numerical values ​​refers to the corresponding value ±10%, preferably ±5%.

[0025] As used herein, the terms “detergent and cleaning agent” or “laundry or cleaning agent” are synonymous with the term “preparation” and refer to compositions used for cleaning textiles, particularly those containing or composed of cotton, polyester, or mixtures thereof, and / or for cleaning hard surfaces, particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., cutlery or pots) or glass, as described in the specification.

[0026] Within the scope of this invention, unless otherwise expressly stated, the term "room temperature" is understood to mean 20°C at 1013 millibars.

[0027] As used herein, “liquid” includes liquids, gels, and paste compositions. Preferably, the liquid composition is flowable and pourable at room temperature, but it may also have flow limits.

[0028] According to the definition of the present invention, a substance, such as a composition or preparation, is solid if it is solid at 20°C and 1013 mbar.

[0029] According to the definition of this invention, a substance, such as a composition or formulation, is a liquid if it is in a liquid state at 20°C and 1013 mbar. Liquids also include gel forms.

[0030] In the context of this invention, the term "N-terminus" or "N-end" generally describes the amino acid chain terminus of a peptide that has a free amino group.

[0031] In the context of this invention, the term "C-terminus" or "C-terminus" generally describes the amino acid chain terminus of a peptide that has a free carboxyl group.

[0032] In the context of this invention, the expression "in the direction from the N-terminus to the C-terminus" refers to an amino acid sequence, wherein the amino acid sequence is described from the N-terminus toward the C-terminus.

[0033] When referring to various bonded or individual amino acid sequences, unless otherwise stated, these sequences are always indicated in the N-to-C-terminal direction. Furthermore, unless otherwise stated, individual amino acids or amino acid sequences are bonded to each other by peptide bonds.

[0034] In the context of this invention, “adhesion” or “adhesiveness” is understood to mean the interaction between a peptide and a surface, thereby enabling the peptide to adhere to the surface. Therefore, the term “mediated adhesion” refers to the ability, under suitable conditions, typically non-denaturing conditions, to interact with and / or adhere to a particular surface, such as textile surfaces, particularly those containing or composed of cotton, polyester, or mixtures thereof, or hard surfaces, particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastics), metals (e.g., cutlery or pots), or glass. As used herein, “fat-binding peptide” means a peptide that binds to fats, for example, to at least one grease- and / or oil-containing stain on a surface. In a preferred embodiment, the binding affinity is greater than that of a reference sequence or reference molecule that does not have mediated adhesion properties. The adhesion of the fat-binding peptide described herein to a given surface is preferably 10 times greater than that of a reference molecule (the peptide according to SEQ ID NO:32), more preferably 20 times, 50 times, or 100 times greater. In the context of this invention, the term “binding” preferably refers to a “covalent bond” between the peptide and the surface. In the context of this invention, if the ability of a peptide to adhere to a grease- and / or oily surface and / or a surface coated with grease and / or oil and / or at least one grease- and / or oily stain on the surface is demonstrated in the method according to Example 2, wherein the binding affinity is greater than that of a reference molecule (the peptide according to SEQ ID NO:32), then the peptide is particularly a fat-binding peptide.

[0035] This invention is based on the inventors' unexpected discovery that specific peptides bind to and adhere to greasy and / or oily surfaces as described herein, thereby allowing the removal of at least one greasy and / or oily stain from the surface, thus improving the cleaning performance of detergents and / or cleaning agents containing them for at least one greasy and / or oily stain. Furthermore, the inventors have discovered that the combination of enzymes, particularly those with hydrolytic activity against ester bonds (preferably selected from lipases and esterases, especially esterases with fat-decomposing activity, and particularly preferred lipases), with the peptides according to the invention results in improved removal of at least one greasy and / or oily stain from the surface. This is unexpected because the peptides according to the invention have not previously been described as capable of removing greasy and / or oily stains from surfaces, i.e., of having cleaning performance for at least one greasy and / or oily stain, nor have they been described as improving the cleaning performance of lipases.

[0036] Therefore, the present invention relates to a detergent and / or cleaning agent comprising (A) At least one peptide, wherein the peptide is selected from... a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3 Selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or b) A peptide having an amino acid sequence identity of at least 80%, and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%, with one of the amino acid sequences listed in SEQ ID NOs: 1-31; and (B) At least one enzyme that has hydrolytic activity against ester bonds, preferably selected from lipases and esterases, especially esterases with lipolytic activity, and particularly preferably lipases.

[0037] In the context of this invention, "peptide" means a polymer composed of amino acids, preferably 20 protein-derived L-amino acids, preferably linearly structured, having a maximum of 100 amino acids interconnected by peptide bonds. According to the invention, the peptides of this invention have an amino acid sequence of 4 to 50 amino acids. In the context of this invention, amino acids are represented using single-letter codes, such as sequence (C). m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t In this context, "C" represents a cysteine ​​residue. It is further understood that, unless otherwise stated, the amino acids in the amino acid sequences disclosed herein are linked by peptide bonds, and the sequences are listed in an N-to-C-terminal orientation, unless otherwise stated.

[0038] Table 1: Protein-derived amino acids

[0039] Typical acidic or negatively charged amino acids (depending on pH) are D and E. Positively charged or basic amino acids (depending on pH) typically include R, K, and H. Amino acids such as G, A, C, I, L, M, F, V, P, S, T, W, Y, N, and Q are generally uncharged, i.e., neutral amino acids. When this article refers to "any" amino acid, it generally means one of 20 naturally occurring protein-derived amino acids (Table 1).

[0040] Amino acids are typically L-amino acids unless otherwise stated. In alternative embodiments, the peptide may also consist of D-amino acids, although it is probably preferred that D- and L-amino acids not be present simultaneously in the peptides described herein. In various embodiments, any such amino acid encompasses all the amino acids described above.

[0041] In various embodiments, the total charge of the peptide is from 0 to +12, for example, 0, +1, +2, +3, +4, +5, +6, +7, +8, +9, +10, +11, +12. The total charge of the peptide is based on the number of positively and negatively charged amino acids in the peptide, particularly R, K, H, D, and E, and is the sum of the positive and negative charges, where the positive and negative charges cancel each other out. Therefore, a peptide having 2 R residues and 1 E residue has a total charge of +1. In a preferred embodiment, the total charge of the peptide is from 0 to +4.

[0042] In various implementation schemes, peptides have (a1) Total charge is 0 to +4, or (a2) If r ≥ 4, the total charge is 0 to +4, or (a3) If r < 4, the total charge is +1 to +4, preferably +2 or +3.

[0043] In various implementation schemes, (b) The N-terminus containing the first 1-5 amino acids has a net positive charge; and / or (c1) The C-terminus containing the last 1-5 amino acids has a net negative charge, such that the sum of the net charges of the first 1-5 amino acids at the N-terminus and the last 1-5 amino acids at the C-terminus is greater than or equal to 0, preferably greater than 0, or (c2) The C-terminus containing the last 1-5 amino acids has a net neutral charge, such that the sum of the net charges of the first 1-5 amino acids at the N-terminus and the last 1-5 amino acids at the C-terminus is greater than 0, preferably greater than 1, or (c3) The C-terminus containing the last 1-5 amino acids has a net positive charge, such that the sum of the net charges of the first 1-5 amino acids at the N-terminus and the last 1-5 amino acids at the C-terminus is greater than 0, preferably greater than 1.

[0044] All of the above features can be implemented individually or in any combination.

[0045] The feature “the peptide has a net positive charge at the N-terminus containing the first 1-5 amino acids” means that the N-terminal 1-5 amino acids contain more positively charged amino acids than negatively charged amino acids. In various embodiments, this feature is satisfied, for example, when the N-terminal 1-5 amino acids have 1 or 2 positively charged amino acids, i.e., H, K, or R, preferably K or R, more preferably R, and there are no negatively charged amino acids such as E or D. If the N-terminus contains negatively charged amino acids, the number of positively charged amino acids must be at least 2 to maintain a positive net charge.

[0046] The characteristic "the peptide has a net negative charge at the C-terminus containing the last 1-5 amino acids" means that the number of charged amino acids must be 0, or the number of negatively charged amino acids, i.e., D and E, must be greater than the number of positively charged amino acids. In various embodiments, this characteristic is satisfied, for example, when the C-terminal 1-5 amino acids, i.e., the last 5 amino acids at the C-terminus, contain 1 or 2 negatively charged amino acids, i.e., D or E, and no positively charged amino acids, i.e., H, K, or R. Examples of such C-terminal sequences include, for example, EAL or a duplex sequence of this motif.

[0047] The characteristic "the peptide has a net neutral charge at the C-terminus containing the last 1-5 amino acids" means that the number of charged amino acids must be 0, or the number of negatively charged and positively charged amino acids must be equal.

[0048] In various embodiments, the peptide has the following amino acid sequence in the N-to-C-terminal direction: (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3 Selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4.

[0049] In various implementations, within the peptide, if o = 1, p = 0, 1, or 2, q = 2, and r = 4, then the sequence (X) 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s Equal to Z 1 Z 2 Z3 [(Z 4 ) u Z 5 Z 6 ]3(Z 7 ) v , in Z 1 Defined as X above 2 And selected from R, H and K, with R preferred, Z 2 Z 3 Z 5 and Z 6 Defined as X above 4 And selected from A, L, and V, with A and L being preferred. Z 4 Defined as X above 3 And selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with F, R, E, A, Q, and W preferred. u is 1 or 2. Z 7 Defined as X above 5 And selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V. v is defined as above s and is an integer from 0 to 4.

[0050] In various implementation schemes, (i) If u = 1, Z 4 Selected from R, E, and Q, or (ii) If u = 2, (Z 4 )2 is selected from FR, FE, AR, WE, WR and AQ.

[0051] In various implementation schemes, peptides include (i) at least one motif selected from RAL and RLA, preferably RAL, wherein the sequence is preferably located at the N-terminal amino acid at positions 1-3; and / or (ii) at least one motif selected from EAL and ELA, preferably EAL, and wherein the motif is preferably not located in the N-terminal amino acids at positions 1-4; and / or (iii) at least one motif selected from QAL and QLA, preferably QAL; and / or (iv) at least one of the RAL motif and QAL or EAL, preferably both; and / or (v) at least one, preferably two or three, RAL motifs; and / or (vi) RAL motif at least twice and at least one of QAL or EAL, preferably both.

[0052] In various embodiments, the peptide comprises a motif selected from RAL, RSI, and RLA, preferably RAL and RLA, and more preferably RAL. The N-terminal sequence RAL or RLA not only advantageously has a net positive charge but also contains an amino acid with a particularly high α-helix formation potential. In various embodiments, the R residue may also be replaced by K, but the N-terminal R residue is particularly preferred.

[0053] In various embodiments, the peptide comprises an amino acid having a high α-helix formation potential, wherein these amino acids are selected from E, A, L, M, Q, K, R, F, I, H, W, and D, more preferably E, A, L, M, Q, K, R, F, I, and H, and even more preferably E, A, L, M, Q, K, R, and H.

[0054] In various embodiments, the peptide is composed of at least 50%, and preferably increasing to at least 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of amino acids with high α-helix formation potential, wherein these amino acids are preferably selected from E, A, L, M, Q, K, R, F, I, H, W, and D, more preferably E, A, L, M, Q, K, R, F, I, and H, and particularly preferably E, A, L, M, Q, K, R, and H.

[0055] In various embodiments, the peptide forms a helical secondary structure, particularly an α-helical structure, wherein the α-helix content is preferably at least 70%, and preferably increasing to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%. The use of AL or LA motifs in the amino acid sequence of the peptide according to the invention contributes to the stability of the helical structure because these amino acids have high α-helical potential.

[0056] In various implementations, within the peptide, if o = 1, p = 3-6, q = 1 or 2 and r = 2, then the sequence (X) 2 )o [(X 3 ) p (X 4 ) q ] r Equal to Z 11 (Z 12 )6Z 13 Z 14 (Z 15 ) w Z 16 , in Z 11 Defined as X above 2 And selected from R, H and K, Z 12 Defined as X above 3 And selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, preferably A, N, C, Q, G, I, L, M, F, P, S, T, W, Y, and V, more preferably M, I, S, T, N, V, and F. Z 13 Z 14 Z 16 Defined as X above 4 And selected from A, L, and V, with A and L preferred. Z 15 Defined as X above 3 And selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with R, K, E, S, Q, and N being preferred. w is an integer from 3 to 6.

[0057] In various implementation schemes, in peptides, (i) Z 13 Z 14 Selected from AL and LA, with AL preferred; and / or (ii) (Z 15 ) w Where w = 3-6, and contains a sequence containing at least one positively charged amino acid (R, H, or K); and / or (iii) (Z 15 ) w Where w = 3-6, comprising motifs selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, more preferably RQN; and / or (iv) Z 16 Choose from A and L, with A being the preferred option.

[0058] In various embodiments, the peptide may have a high proportion of hydrophobic amino acids selected from A, L, F, W, V, M, I, and P, particularly A, L, F, W, V, M, and I. In various embodiments, the proportion of hydrophobic amino acids, i.e., the number of hydrophobic amino acids relative to the total number of amino acids in the peptide, is at least 30%, preferably at least 40%, more preferably at least 50%, and particularly preferably at least 60%. In various embodiments, the proportion of hydrophobic amino acids in the peptide is at least 30% and preferably increases to at least 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%. In various embodiments, at least three, preferably at least four, hydrophobic amino acids, particularly those selected from A, L, F, W, V, M, and I, are arranged adjacent to each other in the peptide sequence. In various embodiments, the proportion of hydrophobic amino acids, i.e., the number of hydrophobic amino acids relative to the total number of amino acids in the peptide, is at least 30%, preferably at least 40%, more preferably at least 50%, particularly preferably at least 60%, and at least three, preferably four, hydrophobic amino acids, particularly those selected from A, L, F, W, V, M, and I, are arranged adjacent to each other in the peptide sequence.

[0059] In various embodiments, the peptide has an amino acid sequence length of 10 to 24 amino acids, such as 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, particularly 12 to 18 amino acids.

[0060] In various embodiments, the peptide has an amino acid sequence length of 10 to 24 amino acids, such as 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, particularly 12 to 18 amino acids, and the proportion of hydrophobic amino acids, i.e. the number of hydrophobic amino acids relative to the total number of amino acids in the peptide, is at least 30%, preferably at least 40%, more preferably at least 50%, particularly preferably at least 60%, and at least three, preferably four, hydrophobic amino acids, particularly those selected from A, L, F, W, V, M and I, are arranged adjacent to each other in the peptide sequence.

[0061] In various embodiments, the peptide has a cysteine ​​amino acid (C) at its C-terminus. In various embodiments, the peptide has a cysteine ​​amino acid at its N-terminus. This amino acid can be coupled to other molecules, structures, or substrates via a free thiol group. Therefore, this amino acid serves as a linker but typically does not participate in the desired adhesion effect.

[0062] In a preferred embodiment, the peptide has an amino acid sequence identity of at least 80%, and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%, with one of the amino acid sequences listed in SEQ ID NOs: 1-31.

[0063] In a preferred embodiment, the peptide is selected from: HFVKTPARWAWG (SEQ ID NO:1), IYASNHSHPASY (SEQ ID NO:2), GHQGHWYGMFRA (SEQ ID NO:3), SLAFMPAWHASR (SEQ ID NO:4), HNHHQLALVESY (SEQ ID NO:5), SQLFNSQRLAYS (SEQ ID NO:6), WRHPRLRCGNLL (SEQ ID NO:7), SRARLFVVTYHKC (SEQ ID NO:8), HMISTMNAASRRC (SEQ ID NO:9), RSIVTFSLRQNRC (SEQ ID NO:10), RSIVTFSLRQNSEQAC (SEQ ID NO:11), KSIVTFSLRQNRC (SEQ ID NO:12), KSIVTFSLKQNRC (SEQ ID NO:13), RALFRALFEALEALRC (SEQ ID NO:14), RALFEALQALFRALEALC (SEQ ID NO:15), RALRALFEALEALC (SEQ ID NO:16), RALFEALFRALEALRC (SEQ ID NO:17), RALEALFRALEALC (SEQ ID NO:18), RALFRALWEALFEALC (SEQ ID NO:19), RALFEALWRALFEALC (SEQ ID NO:20), RALFEALFRALEALC (SEQ ID NO:21), SHTWGSQATSSS (SEQ ID NO:22), RALEALWRALEALC (SEQ ID NO:23), RALRALQALEALEALC (SEQ ID NO:24), RALRALQALQALEALC (SEQ ID NO:25), RALRALQALQALEAELC (SEQ ID NO:26), RALARALARALAQALAC (SEQ ID NO:27), RALARALARALARALAC (SEQ ID NO:28), RALRALRALEALEALC (SEQ ID NO:29), RALQALRALQALEALC (SEQ ID NO:30), RALRALEALQALEALC (SEQ ID NO:31).

[0064] In a preferred embodiment, the peptide has the sequences listed in SEQ ID NOs: 1-31, particularly preferred are SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, and very particularly preferred are SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0065] In various embodiments, the peptide according to the invention may be surface-active or non-surface-active.

[0066] In a preferred embodiment, the peptide according to the invention is not surface-active.

[0067] In a preferred embodiment, the peptide according to the invention is surface-active.

[0068] Various methods for determining surface activity are known to those skilled in the art. In the context of this invention, dynamic surface tension is particularly determined as a measure of surface activity, based on the bubble pressure method (also known as the bubble pressure difference method). The dynamic surface tension of surfactants or molecules with surfactant-like properties in liquids, particularly aqueous liquids, is measured at pH 8.0 and 20°C using a SITAscience line t100 laboratory tensiometer (from SITA Messtechnik GmbH, Dresden). Dynamic surface tension provides information, in particular, about surfactant kinetics and is therefore a measure of the surface activity of surfactants and other molecules (see https: / / www.sita-messtechnik.de / wissen / oberflaechenspannung). If the dynamic surface tension remains constant throughout the bubble lifetime, the corresponding test substance is not surface-active. Even a deviation of only a few mN / m from the ideal surface tension of pure water at 72 mN / m indicates a surfactant effect and will be an indication of surface-active behavior. Within the scope of this invention, "non-surface-active" is understood to mean a substance whose dynamic surface tension remains constant throughout the bubble lifetime, i.e., a deviation of less than 10 mN / m, preferably less than 8 mN / m, more preferably less than 6 mN / m, particularly preferably less than 5 mN / m, and very particularly preferably less than 2 mN / m. In the context of this invention, "surface-active" is understood to mean a substance whose dynamic surface tension does not remain constant throughout the bubble lifetime, i.e., a deviation of at least 2 mN / m, preferably at least 5 mN / m, more preferably at least 6 mN / m, particularly preferably at least 8 mN / m, and very particularly preferably at least 10 mN / m.

[0069] In various embodiments, the peptide according to the invention may be surface-active or non-surface-active, wherein the surface activity is determined according to the bubble pressure method as described herein.

[0070] In a preferred embodiment, the peptide according to the invention is not surface-active, wherein the surface activity is determined according to the bubble pressure method as described herein.

[0071] In a preferred embodiment, the peptide according to the invention is surface-active, wherein the surface activity is determined according to the bubble pressure method as described herein.

[0072] In various embodiments, the peptide according to the invention may be surface-active or non-surface-active, wherein the surface activity is determined as described in Example 4.

[0073] In a preferred embodiment, the peptide according to the invention is not surface-active, wherein the surface activity is determined as described in Example 4.

[0074] In a preferred embodiment, the peptide according to the invention is surface-active, wherein the surface activity is determined as described in Example 4.

[0075] According to the present invention, preferred peptides bind to grease- and / or oily surfaces and / or surfaces coated with grease and / or oil and / or surfaces with at least one grease- and / or oily stain, wherein said surfaces are preferably selected from hard surfaces, more preferably surfaces comprising or composed of ceramics (e.g., porcelain, stoneware), metals, steel, stainless steel, plastics, glass, natural and artificial stone, painted and enamel surfaces, wood, laminates, linoleum, and mixtures thereof, particularly preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastics), metals (e.g., tableware or pots), or glass, and / or textiles, more preferably textiles comprising or composed of cotton, polyester, polyamide, polypropylene, and mixtures thereof, particularly preferably cotton, polyester, and mixtures thereof, i.e., the peptide has the ability to adhere to the corresponding surface under suitable conditions, i.e., generally non-denaturing conditions, and therefore has adhesive properties. Such peptide adhesion / binding can occur directly through terminal N- or C-terminal groups. Alternatively or additionally, such peptide adhesion / binding can also occur through other functional groups bound to the N- and / or C-termini. Furthermore, peptides can be covalently bound to carrier substances, particularly to surfaces containing grease and / or oil, and / or coated with grease and / or oil, and / or with at least one grease and / or oil stain, as described herein, via N- and / or C-terminal bonding and / or via suitable side chains and / or similar suitable binding mechanisms under desired application conditions.

[0076] According to the present invention, preferred peptides bind to oily and / or greasy surfaces, particularly textiles, preferably textiles containing or composed of cotton, polyester, and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass.

[0077] According to the present invention, preferred peptides bind to surfaces coated with grease and / or oil, particularly textiles, preferably textiles containing or composed of cotton, polyester, and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass.

[0078] According to the invention, preferred peptides bind to at least one grease- and / or oily stain on a surface, particularly textiles, preferably textiles containing or composed of cotton, polyester, and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass.

[0079] In a particularly preferred embodiment, the peptide according to the invention binds to at least one oily and / or greasy stain on a textile, preferably an oily stain. In a particularly preferred embodiment, the peptide according to the invention binds to at least one oily and / or greasy stain on a textile containing or composed of cotton, polyester, or mixtures thereof.

[0080] For textile surfaces, especially those made of synthetic fibers, such as polyester-containing textiles, good adhesion can be achieved, for example, by having a distinct helical structure (especially an α-helical structure) and / or a high arginine content, particularly peptides with a high arginine content at one of their ends.

[0081] A preferred peptide exhibiting good to very good adhesion to oily and / or greasy stains, preferably oily stains, on polyester textiles, having an amino acid sequence having at least 80% and incrementally preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity with one of the amino acid sequences shown in SEQ ID NOs: 1, 3, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 16, 17, 18, 19, 20, 21, 22, 25, 26, 27, 29, 30, 31. Other preferred peptides exhibiting good to very good adhesion to at least one oily and / or greasy stain on polyester textiles, having an amino acid sequence identical to one of the amino acid sequences shown in SEQ ID NOs: 1, 3, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 16, 17, 18, 19, 20, 21, 22, 25, 26, 27, 29, 30, 31. Particularly preferred peptides exhibiting good to very good adhesion to at least one oily and / or greasy stain on polyester textiles, having an amino acid sequence identical to one of the amino acid sequences shown in SEQ ID NOs: 1, 3, 7, 8, 9, 10, 11, 12, 13, 17, 19, 20, 21, 25, 26, 27, 29, 31. A particularly preferred peptide exhibiting good to very good adhesion to at least one grease- and / or oil-containing, preferably grease-containing stain on polyester textiles, having an amino acid sequence identical to one of the amino acid sequences shown in SEQ ID NOs: 8, 10, 21, 25, 26.

[0082] A preferred peptide exhibiting good to very good adhesion to oily and / or greasy stains, preferably oily stains, on cotton textiles, having an amino acid sequence having at least 80% and preferably increasing at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity with one of the amino acid sequences shown in SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17, 18, 19, 20, 22, 23, 24, 25, 26, 27, 28, 29, 30. Other preferred peptides exhibiting good to very good adhesion to at least one oily and / or greasy stain on cotton textiles, having an amino acid sequence identical to one of the amino acid sequences shown in SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17, 18, 19, 20, 22, 23, 24, 25, 26, 27, 28, 29, 30. Particularly preferred peptides exhibiting good to very good adhesion to at least one oily and / or greasy stain on cotton textiles, having an amino acid sequence identical to one of the amino acid sequences shown in SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 17, 18, 19, 20, 23, 24, 25, 26, 27, 29. A particularly preferred peptide that exhibits good to very good adhesion to at least one oily and / or greasy stain on cotton textiles, having an amino acid sequence identical to one of the amino acid sequences shown in SEQ ID NOs: 1, 3, 4, 6, 7, 8, 9, 10, 12, 13, 23, 26, 27.

[0083] In a particularly preferred embodiment, the peptide according to the invention binds to at least one grease- and / or oil-containing stain on a hard surface, preferably a grease-containing stain, particularly tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g., tableware or pot) or glass, such as grease- and / or oil-containing stains on tableware, pots, tableware (metal) or glass.

[0084] A preferred peptide exhibiting good to very good adhesion to at least one grease- and / or oily stains, preferably grease-containing, on hard surfaces, particularly tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g., tableware or pots), or glass, having an amino acid sequence having at least 80% and preferably increasing at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity with one of the amino acid sequences shown in SEQ ID NOs: 1-31. Other preferred peptides exhibiting good to very good adhesion to hard surfaces, particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots), or glass containing at least one grease and / or oil, preferably grease-containing stains, having an amino acid sequence identical to one of the amino acid sequences shown in SEQ IDNOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31. A particularly preferred peptide, having a sequence identical to one of the amino acid sequences shown in SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, exhibiting good to very good adhesion to at least one grease and / or oil stain on hard surfaces, particularly tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g., tableware or pots), or glass.

[0085] Methods for determining adhesion are known to those skilled in the art, and all suitable methods can be used. Other methods are described in the embodiments.

[0086] If the peptide used according to the invention is coupled with at least one other (macro)molecule, it can also be called a peptide derivative. The peptide used according to the invention is then derivatized. In such embodiments, the peptide can act as an adhesive tag, causing the molecule coupled to it to bind to a desired surface. Such a molecule can also be called a conjugate.

[0087] In some embodiments, the peptides used according to the invention may have N-terminal and / or C-terminal cysteine ​​amino acids, for example for coupling purposes, preferably with suitable amino acids and / or N- and / or C-termini in the chain coupled with biotin (functionalization modification).

[0088] The peptides used according to the invention can also be part of proteins or polypeptides. Such proteins and polypeptides can be recombined to produce, for example, as fusion proteins. In such embodiments, the peptides according to the invention are located at the N- or C-terminus to provide adhesion of the entire molecule to the surface. In such embodiments, the peptides also function as adhesive tags.

[0089] All of the above features and implementation schemes can be implemented individually or in any combination.

[0090] Furthermore, the peptide according to the invention can also be at least one subunit (module) of a larger peptide or polypeptide, wherein the polypeptide can comprise polymers of the sequence described herein, such as 1 to 30 repeats of the peptide, more preferably 2 to 15 repeats, particularly preferably 2 to 10 repeats, for example 2, 3, 4, 5 or 6 repeats. The polypeptide can comprise or consist of such polymers. In this context, the term "polypeptide" specifically refers to such peptides containing 100 or more amino acids. The term "larger peptide" preferably refers to a peptide having at least 40 amino acids, unless otherwise described.

[0091] In various embodiments, the peptides used according to the invention are peptides or polypeptides (polymers) comprising two or more peptides as described herein. In various embodiments, two or more peptides may be linked by at least one spacer region; preferably, said at least one spacer region comprises or is composed of 1 to 10 amino acid residues, particularly 2, 3 or 4 amino acid residues, preferably selected from G, P, I, A and S or combinations thereof, particularly GPI or GAS. In such embodiments, individual peptides may optionally be linearly linked to each other by peptide bonds, or possibly by spacer regions.

[0092] At least one peptide according to the invention may be in the form of an aqueous solution. In various embodiments, the peptide content of the solution is preferably 0.00001 to 10 parts by weight of peptide to 100 parts by weight of water, for example 0.00001 to 10 wt.%, preferably 0.0001 to 7.5 wt.%, more preferably 0.001 to 5 wt.%, based on the total weight of the solution in each case.

[0093] The formulation according to the invention, in addition to containing at least one peptide according to the invention, also contains at least one enzyme with hydrolytic activity against ester bonds, preferably selected from lipases and esterases, particularly esterases with lipolytic activity, and especially preferably lipases. In a preferred embodiment, the formulation according to the invention, in addition to containing at least one peptide according to the invention, also contains at least one lipase.

[0094] Enzymes that are active in hydrolyzing ester bonds are those that can hydrolyze (saponify) esters into alcohols and acids. Therefore, they are hydrolases.

[0095] Lipases are enzymes that catalyze the hydrolysis of lipid substrates, particularly ester bonds in fats and oils. Therefore, lipases represent a group of esterases. Lipases are generally multifunctional enzymes that accept a wide range of substrates, including aliphatic, alicyclic, bicyclic, and aromatic esters, thioesters, and activated amines. Lipases, for example, act on grease residues in clothing and catalyze their hydrolysis (fat breakdown). Lipases with a broad substrate spectrum are particularly useful in situations where heterogeneous raw materials or substrate mixtures must be treated, such as in detergents and cleaning agents, because stains can consist of fats and oils with different structures. Lipases used in detergents or cleaning agents known in the art are typically derived from microorganisms, usually bacteria or fungi, such as those from the genera *Thermomyces*, *Bacillus*, *Pseudomonas*, *Acinetobacter*, *Micrococcus*, *Humicola*, *Trichoderma*, or *Trichosporon*. Lipases are typically produced by suitable microorganisms using known biotechnological methods, such as through transgenic expression hosts of the genus Bacillus, or through filamentous fungi.

[0096] Typically, only selected lipases are suitable for liquid surfactant formulations. Many lipases do not exhibit sufficient catalytic performance or stability in such formulations. However, the use of lipases can produce unpleasant odors on washed items, particularly textiles, after the washing process, because the lipases are adsorbed by the textiles and continue to hydrolyze fatty acid esters into low molecular weight fatty acids. These low molecular weight fatty acids are perceived as having an unpleasant odor. The intensity of the odor may vary depending on the condition of the textile.

[0097] Examples of suitable lipases include, for example, lipases from the genus *Thermophilus*, such as *T. lanuginosus* (formerly known as *Humicola lanuginosa*), as described in EP 0258068 and EP0305216; lipases from strains of the genus *Pseudomonas* (some of which have now been reclassified as *Burkholderia*), such as *P. alcaligenes* or *P. pseudoalcaligenes*, *P. cepacia*, *P. sp.* strain SD705, and *P. wisconsinensis*; *Streptomyces* lipases of the GDSL type; and lipases from *Thermobifida*. Lipases derived from *Geobacillus stearothermophilus*, *Bacillus subtilis*, and *Streptomyces griseus* and *S. pristinaespiralis*. Preferred lipases include those originally obtained from or developed from *Humicola lanuginosa*, particularly those derived from said lipases with one or more of the following amino acid substitutions: D96L, T213R, and / or N233R, with T213R and N233R being particularly preferred. Preferred commercial lipase products include Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A / S), Lumafast (Genencor / DuPont) and Lipomax (Gist-Brocades).

[0098] Methods for determining lipase activity are familiar to those skilled in the art of enzyme technology and are routinely used by them (see, for example, Bruno Stellmach, “Methods for determining enzymes for pharmacy, foodchemistry, technology, biochemistry, biology, medicine,” Steinkopff VerlagDarmstadt, 1988, p. 172 et seq.). Here, a lipase-containing sample is added to an olive oil emulsion in water containing an emulsifier and incubated at 30°C and pH 9.0. Fatty acids are released. The solution is titrated continuously for 20 minutes using an automated titrator with 0.01 N sodium hydroxide solution to maintain a constant pH (“pH-stat titration”). Lipase activity is determined based on the amount of sodium hydroxide consumed and with reference to a reference lipase sample. An alternative test for determining the lipolytic activity of the lipase according to the invention is an optical measurement method, preferably photometry. A suitable assay involves the lipase-dependent cleavage of the substrate p-nitrophenol butyrate (pNP-butyrate). This substrate is cleaved by the lipase into p-nitrophenolate and butyrate. The presence of p-nitrophenol salts can be determined at 405 nm using a photometer (e.g., a Tecan Sunrise device and XFLUOR software), which allows for the inference of lipase activity.

[0099] In a preferred embodiment, the formulation according to the invention comprises at least one lipase selected from the following: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one position selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, and I255A. The amino acid substitutions of P256T, wherein the lipase has an amino acid substitution combination selected from the following: T231R-N233R, P208N-T231R-N233R, F211N-T231R-N233R, T231R-N233R-P253N, N33Q-G91Q-E210Q-I255A, N33Q-G91Q-E210Q-T231R-N233R-I255A, D96E-T231R-N233R, N33Q-D96E-T231R-N233R, N3 3Q-D111A-T231R-N233R, N33Q-T231R-N233R-P256T, N33Q-G38A-G91T-G163K-T231R-N233R-D254S, N33Q-G38A-G91T-D 96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R -N33Q-G38A-G91T-D96E-D111A-G163K-T231R-N233R-P256T, D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T231R-N233R -D254S, D27R-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-T231R-N233R-D254S, T231R-N233R-D 254S-P256T, G163K-T231R-N233R-D254S, D27R-N33Q-G38A-G91T-D96E-G163K-T231R-N233R-D254S-P256T, D27R-G91T -D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-G163K-T231R-N233R-D254S, D27R-G163K-T231R-N233R-D254S,D27R-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S、D27R-G38A-G 91T-D96E-G163K-T231R-N233R-D254S-P256T、D27R-G38A-D96E-D111A-G1 63K-T231R-N233R-D254S-P256T、D27R-D96E-G163K-T231R-N233R-D254S、 D27R-D96E-D111A-G163K-T231R-N233R-D254S-P256T、D27R-G38A-D96E-G 163K-T231R-N233R-D254S-P256T、D111A-G163K-T231R-N233R-D254S-P256T、D111A-T231R-N233R、D111A-T231R-N233R-D254S-P256T、D27R-D96E-D 111A-G163K-T231R-N233R, D27R-D96E-D111A-T231R-N233R, D27R-N33Q-G38A-D96E-D111A-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G1 63K-E210Q-T231R-N233R-D254S-P256T, D27R-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R, D96E-D111A-G163K-T231R-N233R-D2 54S-P256T, D96E-D111A-G163K-T231R-N233R-P256T, D96E-D111A-T231R-N233R, D96E-D111A-T231R-N233R-D254S, D96E-D111A-T231R-N233R-D254 S-P256T、D96E-D111A-T231R-N233R-P256T、D96E-G163K-T231R-N233R-D2 54S-P256T、D96E-T231R-N233R-D254S-P256T、D96E-T231R-N233R-P256T、 G38A-D96E-D111A-T231R-N233R, G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, G91T-D96E-D111A-T231R-N233R, G91T-D96E-T231R-N233RG91T-T231R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231R-N233R-D254S-P256T, T231R-N233R-D254S-P256T, and T231R-N233R-P256T; and / or (c) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in ascending order of at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38; and / or (d) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO: 33 over its entire length; and / or (e) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO: 34 over its entire length; and / or (f) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO: 35 over its entire length; and / or (g) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO: 36 over its entire length; and / or (h) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and increasing, preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO: 37 over its entire length; and / or (i) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:38 over its entire length.

[0100] In a more preferred embodiment, the formulation according to the invention comprises at least one lipase selected from the following: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (j) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (iii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one position selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, and I255A. The amino acid substitutions of P256T, wherein the lipase has an amino acid substitution combination selected from the following: T231R-N233R, P208N-T231R-N233R, F211N-T231R-N233R, T231R-N233R-P253N, N33Q-G91Q-E210Q-I255A, N33Q-G91Q-E210Q-T231R-N233R-I255A, D96E-T231R-N233R, N33Q-D96E-T231R-N233R, N3 3Q-D111A-T231R-N233R, N33Q-T231R-N233R-P256T, N33Q-G38A-G91T-G163K-T231R-N233R-D254S, N33Q-G38A-G91T-D 96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R -N33Q-G38A-G91T-D96E-D111A-G163K-T231R-N233R-P256T, D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T231R-N233R -D254S, D27R-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-T231R-N233R-D254S, T231R-N233R-D 254S-P256T, G163K-T231R-N233R-D254S, D27R-N33Q-G38A-G91T-D96E-G163K-T231R-N233R-D254S-P256T, D27R-G91T -D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-G163K-T231R-N233R-D254S, D27R-G163K-T231R-N233R-D254S,D27R-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S、D27R-G38A-G 91T-D96E-G163K-T231R-N233R-D254S-P256T、D27R-G38A-D96E-D111A-G1 63K-T231R-N233R-D254S-P256T、D27R-D96E-G163K-T231R-N233R-D254S、 D27R-D96E-D111A-G163K-T231R-N233R-D254S-P256T、D27R-G38A-D96E-G 163K-T231R-N233R-D254S-P256T、D111A-G163K-T231R-N233R-D254S-P256T、D111A-T231R-N233R、D111A-T231R-N233R-D254S-P256T、D27R-D96E-D 111A-G163K-T231R-N233R, D27R-D96E-D111A-T231R-N233R, D27R-N33Q-G38A-D96E-D111A-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G1 63K-E210Q-T231R-N233R-D254S-P256T, D27R-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R, D96E-D111A-G163K-T231R-N233R-D2 54S-P256T, D96E-D111A-G163K-T231R-N233R-P256T, D96E-D111A-T231R-N233R, D96E-D111A-T231R-N233R-D254S, D96E-D111A-T231R-N233R-D254 S-P256T、D96E-D111A-T231R-N233R-P256T、D96E-G163K-T231R-N233R-D2 54S-P256T、D96E-T231R-N233R-D254S-P256T、D96E-T231R-N233R-P256T、 G38A-D96E-D111A-T231R-N233R, G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, G91T-D96E-D111A-T231R-N233R, G91T-D96E-T231R-N233RG91T-T231R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231R-N233R-D254S-P256T, T231R-N233R-D254S-P256T, and T231R-N233R-P256T; and / or (c) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO: 33 over its entire length; and / or (d) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0101] In a particularly preferred embodiment, the formulation according to the invention comprises at least one lipase selected from: a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one position selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, and I255A. The amino acid substitutions of P256T, wherein the lipase has an amino acid substitution combination selected from the following: T231R-N233R, P208N-T231R-N233R, F211N-T231R-N233R, T231R-N233R-P253N, N33Q-G91Q-E210Q-I255A, N33Q-G91Q-E210Q-T231R-N233R-I255A, D96E-T231R-N233R, N33Q-D96E-T231R-N233R, N3 3Q-D111A-T231R-N233R, N33Q-T231R-N233R-P256T, N33Q-G38A-G91T-G163K-T231R-N233R-D254S, N33Q-G38A-G91T-D 96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R -N33Q-G38A-G91T-D96E-D111A-G163K-T231R-N233R-P256T, D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T231R-N233R -D254S, D27R-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-T231R-N233R-D254S, T231R-N233R-D 254S-P256T, G163K-T231R-N233R-D254S, D27R-N33Q-G38A-G91T-D96E-G163K-T231R-N233R-D254S-P256T, D27R-G91T -D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-G163K-T231R-N233R-D254S, D27R-G163K-T231R-N233R-D254S,D27R-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S、D27R-G38A-G 91T-D96E-G163K-T231R-N233R-D254S-P256T、D27R-G38A-D96E-D111A-G1 63K-T231R-N233R-D254S-P256T、D27R-D96E-G163K-T231R-N233R-D254S、 D27R-D96E-D111A-G163K-T231R-N233R-D254S-P256T、D27R-G38A-D96E-G 163K-T231R-N233R-D254S-P256T、D111A-G163K-T231R-N233R-D254S-P256T、D111A-T231R-N233R、D111A-T231R-N233R-D254S-P256T、D27R-D96E-D 111A-G163K-T231R-N233R, D27R-D96E-D111A-T231R-N233R, D27R-N33Q-G38A-D96E-D111A-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G1 63K-E210Q-T231R-N233R-D254S-P256T, D27R-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R, D96E-D111A-G163K-T231R-N233R-D2 54S-P256T, D96E-D111A-G163K-T231R-N233R-P256T, D96E-D111A-T231R-N233R, D96E-D111A-T231R-N233R-D254S, D96E-D111A-T231R-N233R-D254 S-P256T、D96E-D111A-T231R-N233R-P256T、D96E-G163K-T231R-N233R-D2 54S-P256T、D96E-T231R-N233R-D254S-P256T、D96E-T231R-N233R-P256T、 G38A-D96E-D111A-T231R-N233R, G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, G91T-D96E-D111A-T231R-N233R, G91T-D96E-T231R-N233RG91T-T231R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231R-N233R-D254S-P256T, T231R-N233R-D254S-P256T, and T231R-N233R-P256T.

[0102] In a particularly preferred embodiment, the formulation according to the invention comprises at least one lipase selected from the group consisting of: a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0103] In a particularly preferred embodiment, the formulation according to the invention comprises at least one lipase selected from the group consisting of: a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0104] In a very particularly preferred embodiment, the formulation according to the invention comprises at least one lipase selected from: a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) At at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T, wherein the lipase has an amino acid substitution combination selected from the following: T231R-N233R, P208N-T231R-N233R, F21 1N-T231R-N233R, T231R-N233R-P253N, N33Q-G91Q-E210Q-I255A, N33Q- G91Q-E210Q-T231R-N233R-I255A, D96E-T231R-N233R, N33Q-D96E-T231R -N233R, N33Q-D111A-T231R-N233R, N33Q-T231R-N233R-P256T, N33Q-G3 8A-G91T-G163K-T231R-N233R-D254S, N33Q-G38A-G91T-D96E-D111A-G16 3K-T231R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111A-G163K-T 231R-N233R-D254S-P256T, D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T 231R-N233R-P256T, D27R-N33Q-G38A-G91T-D96E-D111A-G163K-T231R- N233R-D254S, D27R-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S -P256T, D96E-T231R-N233R-D254S, T231R-N233R-D254S-P256T, G163K- T231R-N233R-D254S, D27R-N33Q-G38A-G91T-D96E-G163K-T231R-N233R- D254S-P256T, D27R-G91T-D96E-D111A-G163K-T231R-N233R-D254S-P25 6T, D96E-G163K-T231R-N233R-D254S, D27R-G163K-T231R-N233R-D254S,D27R-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S、D27R-G38A-G 91T-D96E-G163K-T231R-N233R-D254S-P256T、D27R-G38A-D96E-D111A-G1 63K-T231R-N233R-D254S-P256T、D27R-D96E-G163K-T231R-N233R-D254S、 D27R-D96E-D111A-G163K-T231R-N233R-D254S-P256T、D27R-G38A-D96E-G 163K-T231R-N233R-D254S-P256T、D111A-G163K-T231R-N233R-D254S-P256T、D111A-T231R-N233R、D111A-T231R-N233R-D254S-P256T、D27R-D96E-D 111A-G163K-T231R-N233R, D27R-D96E-D111A-T231R-N233R, D27R-N33Q-G38A-D96E-D111A-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G1 63K-E210Q-T231R-N233R-D254S-P256T, D27R-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R, D96E-D111A-G163K-T231R-N233R-D2 54S-P256T, D96E-D111A-G163K-T231R-N233R-P256T, D96E-D111A-T231R-N233R, D96E-D111A-T231R-N233R-D254S, D96E-D111A-T231R-N233R-D254 S-P256T、D96E-D111A-T231R-N233R-P256T、D96E-G163K-T231R-N233R-D2 54S-P256T、D96E-T231R-N233R-D254S-P256T、D96E-T231R-N233R-P256T、 G38A-D96E-D111A-T231R-N233R, G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, G91T-D96E-D111A-T231R-N233R, G91T-D96E-T231R-N233RG91T-T231R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231R-N233R-D254S-P256T, T231R-N233R-D254S-P256T, and T231R-N233R-P256T.

[0105] In a very particularly preferred embodiment, the formulation according to the invention comprises at least one lipase selected from the group consisting of a lipase having lipolytic activity and comprising an amino acid sequence that is 100% identical in its entire length to the amino acid sequence shown in SEQ ID NO:33.

[0106] In a particularly preferred embodiment, the formulation according to the invention comprises at least one lipase selected from the group consisting of a lipase having lipolytic activity and comprising an amino acid sequence having at least 100% identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0107] Within the scope of this invention, cleaning performance is understood to mean the ability of an agent to partially or completely remove existing stains, particularly the whitening performance of one or more stains on textiles and / or hard surfaces. Within the scope of this invention, both the agent and the washing and / or cleaning liquid formed from the agent possess their respective cleaning properties.

[0108] Washing or cleaning liquids are understood to refer to working solutions containing detergents or cleaning agents that act on textiles or fabrics or surfaces, particularly tableware or household surfaces, and thus come into contact with stains present on the textiles or fabrics or surfaces. Washing / cleaning liquids are typically formed at the start of a washing / cleaning process and when the formulation is diluted with water, for example in a washing machine or dishwasher or in another suitable container.

[0109] The composition of the detergent or cleaning agent according to the invention and the amount of its components depend on the specific intended use, and the appropriate dosage of these components is generally familiar to those skilled in the art and can be obtained from relevant professional literature.

[0110] The detergents and cleaning agents according to the invention include all conceivable types of detergents or cleaning agents, including concentrates and formulations intended for direct use, for commercial-scale, machine-washing, or hand-washing or cleaning. These include, for example, detergents for textiles, carpets, or natural fibers, for which the term "detergent" is used. These also include, for example, dishwasher detergents (automatic dishwasher detergents) or hand-wash dishwashing agents for dishwashers, or cleaning agents for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood, or leather, for which the term "cleaning agent" is used; that is, in addition to hand-washing and automatic dishwasher detergents, this includes, for example, scrubbing agents, glass cleaners, toilet cleaner tablets, etc. The detergents and cleaning agents within the scope of the invention also include auxiliary detergents, which are added to the actual detergent during manual or automatic textile washing to achieve further effects. Furthermore, within the scope of this invention, detergents and cleaning agents also include textile pretreatment and posttreatment agents, such as formulations that bring clothing into contact with the fabric prior to actual washing, for example, for dissolving stubborn stains, and formulations that impart further desired properties to the clothing in downstream steps after actual textile washing, such as a comfortable feel, wrinkle resistance, or low static charge. Fabric softeners, in particular, are included in the latter formulation. This also includes formulations for (semi-)automatic washing or cleaning systems such as robotic mopping robots or wet vacuum cleaners.

[0111] The detergents and / or cleaning agents according to the invention may be in the form of powdered or granular solids, compacted or further compacted granules, homogeneous solutions or suspensions, and may contain all the known ingredients conventionally found in such formulations. In particular, formulations according to the invention may include surfactants, builders, complexing agents, polymers, glass corrosion inhibitors, corrosion inhibitors, bleaching agents such as peroxides, bleaching activators or bleaching catalysts, water-miscible organic solvents, enzyme stabilizers, chelating agents, electrolytes, pH adjusters and / or other additives such as optical brighteners, anti-ashing agents, dye transfer inhibitors, foam conditioners, and dyes and fragrances. Beneficial components of the formulations according to the invention are disclosed in International Patent Application WO 2009 / 121725, from the second-to-last paragraph on page 5 to the end of the second paragraph on page 13. This disclosure is expressly referenced and is incorporated herein by reference.

[0112] The formulation according to the invention contains the peptide according to the invention, preferably in increments of 1 x 10. -8 Up to 10 wt.%, 0.00001 to 5 wt.%, 0.00005 to 2.5 wt.%, 0.0001 to 1.5 wt.%, 0.001 to 0.75 wt.% (based on the total weight of the active protein and the formulation).

[0113] In various embodiments, the formulation according to the invention contains a sufficient amount of the peptide according to the invention for a single wash and rinse cycle. Preferably, the peptide according to the invention is present in the formulation according to the invention in increments of 0.5 to 1,500 mg / wash, 5 to 500 mg / wash, and particularly 10 to 200 mg / wash, based on the amount of active protein. Unless the formulation according to the invention is a single dose, calculations should be based on the usual amount of formulation applied per wash / rinse cycle.

[0114] The formulation according to the invention contains the lipase according to the invention, preferably in an increasing amount of 1 x 10⁻⁶. -8 Up to 10 wt.%, 0.00001 to 5 wt.%, 0.00005 to 2.5 wt.%, 0.0001 to 1.5 wt.%, 0.001 to 0.75 wt.% (based on the total weight of the active protein and the formulation).

[0115] Protein concentrations can be determined using known methods, such as the BCA method (2,2'-biquinoline carboxylic acid) or the biuret method (Gornall et al. J. Biol. Chem., 1948, 177, 751-766). In this respect, the concentration of active proteins can be determined by titrating the active site with a suitable irreversible inhibitor and measuring residual activity (Bender et al., J. Am. Chem. Soc., 1966, 88, 24, 5890-5913). Those skilled in the art of peptides and proteins also know of various suitable methods for determining peptide or protein concentrations that can be used within the scope of this invention.

[0116] Further embodiments of the formulations according to the invention, including all solid, powder, liquid, gel, or paste dosage forms, are also included, which may optionally also consist of multiple phases and may be present in compressed or uncompressed form. The formulations may be present as free-flowing powders, particularly having a bulk density of 300 g / l to 1200 g / l, particularly 500 g / l to 900 g / l or 600 g / l to 850 g / l. Solid application forms of the formulations also include extrudates, granules, tablets, or sachets. Alternatively, the formulations may also be present in liquid, gel, or paste form, for example, as a non-aqueous liquid detergent or non-aqueous paste, or as an aqueous liquid detergent or aqueous paste. Liquid formulations are generally preferred. Furthermore, the formulations may exist as a single-component system. Such a formulation consists of one phase. Alternatively, the formulation may also consist of multiple phases. Such a formulation is correspondingly divided into multiple components.

[0117] If the formulations according to the invention are in liquid form, they preferably contain more than 20 wt.%, preferably 30 to 90 wt.%, and particularly preferably 40 to 80 wt.% water (based on their total weight).

[0118] The formulations according to the invention may contain one or more surfactants, with anionic surfactants, nonionic surfactants, and mixtures thereof being particularly suitable, although cationic, amphoteric, and / or amphoteric surfactants may also be contained. The product preferably contains 0.5 to 70 wt.% surfactant. In textile detergents, 35 to 60 wt.%, more preferably 40 to 55 wt.%, surfactant (based on the total weight of the formulation) is preferred; in a preferred embodiment, the formulation preferably contains 3 to 35 wt.%, more preferably 5 to 30 wt.%, surfactant (based on the total weight of the formulation).

[0119] Suitable anionic surfactants, particularly soaps and those containing sulfate or sulfonate groups, preferably have alkali metal ions as cations. Usable soaps are preferably saturated or unsaturated C466. 12-18 Alkali metal salts of fatty acids. These fatty acids can also be used in an incompletely neutralized form. Suitable sulfate-type surfactants include C... 12-18 The sulfated half-ester salt of fatty alcohol atoms and the sulfated product of the nonionic surfactant having low ethoxylation. Available sulfonate surfactants include, for example, C... 9-14 Alkylbenzene sulfonates, composed of C 12-18 Alkanes, such as alkane sulfonates obtained by sulfonation or sulfonation followed by hydrolysis or neutralization, and C2O2 produced by the reaction of the corresponding monoolefins with sulfur trioxide. 12-18 Olefin sulfonates, mixtures of olefin and hydroxyalkane sulfonates, disulfonates, such as those composed of C atoms with terminal or internal double bonds. 12-18 Monoolefins obtained by sulfonation with gaseous sulfur trioxide followed by alkaline or acidic hydrolysis of the sulfonation product, as well as α-sulfonated fatty acid esters (sulfonates) produced by sulfonation of fatty acid methyl esters or ethyl esters, such as α-sulfonated methyl esters of hydrogenated coconut oil, palm kernel oil, or tallow fatty acids.

[0120] Preferably, the formulation, particularly textile detergent, contains 2 to 55 wt.%, more preferably 3 to 35 wt.%, of anionic surfactant (based on the total weight of the formulation). Very particularly preferably, the formulation contains 3 to 25 wt.%, of alkylbenzene sulfonate. Furthermore, the formulation may preferably also contain other anionic surfactants, particularly alkyl ether sulfates, and nonionic surfactants, particularly fatty alcohol alkoxylates. These may then constitute the remainder of the surfactant.

[0121] Suitable alkylbenzene sulfonates are preferably selected from linear or branched alkylbenzene sulfonates, having the formula... R' and R'' are independently hydrogen or alkyl, and contain a total of 6 to 19, preferably 7 to 15, and especially 9 to 13 C atoms. A very particularly preferred example is sodium dodecylbenzenesulfonate.

[0122] As an alkyl(alkene) sulfate, C is preferred. 12-18 Fatty alcohols (such as coconut fatty alcohol, tallow fatty alcohol, lauryl alcohol, myristyl alcohol, cetyl alcohol, or stearyl alcohol) or C 10-20 Alkali metal salts, particularly sodium salts, of the sulfate half-esters of carbonyl synthetic alcohols, and half-esters of secondary alcohols having these chain lengths. Alkyl (olefin) sulfates of the aforementioned chain lengths, having synthetic straight-chain alkyl functional groups prepared from petrochemical feedstocks and exhibiting degradation behavior similar to corresponding compounds based on aliphatic chemical feedstocks, are also preferred. From a washing perspective, C 12-16 Alkyl sulfates and C 12-15 Alkyl sulfates and C 14-15 Alkyl sulfates are preferred.

[0123] Using 1 to 6 moles of ethoxylated linear or branched C-chain oxides 7-21 Sulfated monoesters of alcohols, such as 2-methyl branched C-esters ethoxylated with an average of 3.5 moles of ethylene oxide (EO). 9-11 Alcohol or C ethoxylated with 1 to 4 EO 12-18 Fatty alcohols are also suitable.

[0124] Suitable alkyl ether sulfates are, for example, of formula R 1 -O-(AO) n -SO3 - X + Compounds. In this formula, R 1 Representing a linear or branched, substituted or unsubstituted alkyl functional group, preferably a linear or unsubstituted alkyl functional group, and particularly preferably a fatty alcohol functional group. Preferred functional group R 1 The functional groups are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecanyl, octadecyl, nonadecanyl, eicosyl, and mixtures thereof, with those having an even number of carbon atoms being preferred. A particularly preferred functional group is R. 1 Derived from C 12-18 Fatty alcohols, such as coconut fatty alcohol, tallow fatty alcohol, lauryl alcohol, myristyl alcohol, cetyl alcohol, or stearyl alcohol, or derived from C 10-20Carbonyl synthesis of alcohols. AO represents an ethylene oxide (EO) group or a propylene oxide (PO) group, preferably an ethylene oxide group. The index n represents an integer from 1 to 50, preferably 1 to 20, particularly 2 to 10. Very particularly preferably, n represents the number 2, 3, 4, 5, 6, 7, or 8. X + This represents a fraction of n of a monovalent or n-valent cation, preferably an alkali metal ion, including Na. + or K + Na + It is the optimal choice. Other cations X + Optional from NH4 + ½ Zn 2+ ½ Mg 2+ ½ Ca 2+ ½ Mn 2+ and its mixtures.

[0125] In various embodiments, the alkyl ether sulfate may be selected from fatty alcohol ether sulfates having the following formula. Where k = 11 to 19, and n = 2, 3, 4, 5, 6, 7, or 8. A particularly preferred example is Na-C with 2 EO. 12-14 Fatty alcohol ether sulfates (k = 11-13, n = 2). The indicated degree of ethoxylation represents a statistical mean and can be an integer or a fraction for a specific product. The indicated degree of alkoxylation represents a statistical mean and can be an integer or a fraction for a specific product. Preferred alkoxylates / ethoxylates have a narrow homologue distribution (narrow-range ethoxylates, NRE).

[0126] It has been demonstrated that the presence of soaps in the formulation enhances cold-water washing performance. Therefore, preferred formulations are characterized by the presence of soaps. Saturated fatty acid soaps are suitable, such as salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid, and behenic acid, especially soap mixtures derived from natural fatty acids such as coconut fatty acids, palm kernel fatty acids, or tallow fatty acids.

[0127] The preferred class of nonionic surfactants used (which are used as the sole nonionic surfactant or in combination with other nonionic surfactants) are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably having 1 to 4 C atoms in the alkyl chain, especially fatty acid methyl esters.

[0128] Another class of advantageously usable nonionic surfactants are alkyl polysaccharides (APGs). Usable alkyl polysaccharides have the general formula RO(G). zIn this formula, R represents a linear or branched saturated or unsaturated aliphatic functional group having 8 to 22, preferably 12 to 18, carbon atoms, particularly methyl-branched at the 2-position, and G is a symbol representing a sugar unit having 5 or 6 carbon atoms, preferably glucose. The degree of glycosylation z is between 1 and 4, preferably between 1 and 2, particularly between 1.1 and 1.4. Linear alkyl polyglycosides are preferred, i.e., alkyl polyglycosides in which the polyol functional group is a glucose functional group and the alkyl functional group is a n-alkyl functional group.

[0129] Nonionic surfactants of the amine oxide type, such as N-cocoyl-N,N-dimethylamine oxide and N-tallowyl-N,N-dihydroxyethylamine oxide, as well as fatty acid alkanolamides, may also be suitable. The amount of these nonionic surfactants preferably does not exceed the amount of ethoxylated fatty alcohol, and particularly does not exceed half of it.

[0130] Suitable amphoteric surfactants are, for example, those of formula (R) iii (R) iv (R) v )N + CH2COO - betaine, of which R iii R represents an alkyl functional group having 8 to 25, preferably 10 to 21, carbon atoms, which is optionally interrupted by a heteroatom or heteroatom group. iv and R v This refers to alkyl functional groups that are the same or different, having 1 to 3 carbon atoms, especially C. 10-18 Alkyl dimethyl carboxymethyl betaine and C 11-17 Alkylamidopropyldimethylcarboxymethyl betaine.

[0131] Suitable cationic surfactants, especially those of formula (R) vi (R) vii (R) viii (R) ix )N + X - Quaternary ammonium compounds, of which R vi To R ix Representing four identical or different alkyl functional groups, specifically two long-chain and two short-chain alkyl functional groups, X - Representing anions, particularly halide ions, such as dialcyldimethylammonium chloride, alkylbenzyldidecylammonium chloride, and mixtures thereof. Other suitable cationic surfactants are quaternary ammonium surfactants, especially those with sulfonium, phosphonium, iodonium, or arsene groups, which are also known as antimicrobial active ingredients. By using quaternary ammonium surfactants with antimicrobial effects, formulations can acquire antimicrobial effects or improve antimicrobial effects that may already exist due to other components.

[0132] Suitable nonionic surfactants are particularly alkyl glycosides and ethoxylated and / or propoxylated products of alkyl glycosides or linear or branched alcohols, each having 8 to about 18 carbon atoms and 3 to 20, preferably 4 to 10, alkyl ether groups in the alkyl moiety. Additionally, corresponding ethoxylated and / or propoxylated products of N-alkylamines, vicinal diols, fatty acid esters and fatty acid amides (which correspond in the alkyl moiety to the aforementioned long-chain alcohol derivatives) and alkylphenols having 5 to 12 carbon atoms in the alkyl functional group can be used.

[0133] The preferred nonionic surfactants, especially in textile detergents, are alkoxylated, advantageously ethoxylated, particularly primary alcohols having preferably 8 to 18 carbon atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol, wherein the alcohol functional group can be linear or preferably branched at the 2-position with methyl groups, or can contain a mixture of linear and methyl-branched functional groups, as is commonly found in carbonyl synthetic alcohols. However, alcohol ethoxylates having linear functional groups of naturally derived alcohols (e.g., coconut oil, palm oil, tallow alcohol, or oleyl alcohol) and an average of 2 to 8 EO per mole of alcohol are particularly preferred. Preferred ethoxylated alcohols include, for example, C atoms having 3 or 4 EO. 12-14 Alcohols, C with 7 EO 9-11 Alcohols, C with 3EO, 5EO, 7EO or 8EO 13-15 Alcohols, C with 3EO, 5EO or 7EO 12-18 Alcohols, and mixtures thereof, such as C3E ... 12-14 Alcohols and C with 5 EO 12-18 A mixture of alcohols. The specified degree of ethoxylation represents a statistical average and may correspond to an integer or a fraction for a particular product. Preferred alcohol ethoxylates have a narrow homologue distribution (narrow range ethoxylate, NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples are tallow fatty alcohols with 14 EO, 25 EO, 30 EO, or 40 EO.

[0134] For dishwasher detergents, the use of nonionic surfactants is particularly suitable, as described below. Therefore, the formulation specifically contains one or more nonionic surfactants as surfactants. The weight percentage relative to the total weight of the formulation is preferably 0.5 to 30 wt.%, more preferably 1.0 to 20 wt.%, and even more preferably 1.5 to 15 wt.%.

[0135] Examples of nonionic surfactants that can be used as the sole nonionic surfactant or in combination with other nonionic surfactants are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably having 1 to 4 carbon atoms in the alkyl chain. Amine oxide type nonionic surfactants, such as N-cocoalkyl-N,N-dimethylamine oxide and N-tallow alkyl-N,N-dihydroxyethylamine oxide, as well as fatty acid alkylolamides, may also be suitable. The amount of these nonionic surfactants preferably does not exceed the amount of ethoxylated fatty alcohol, particularly not more than half of it. These are also used in hand-washing dishwashing detergents. Other suitable surfactants are polyhydroxy fatty acid amides, known as PHFAs. However, low-foaming nonionic surfactants, particularly alkoxylated, and especially ethoxylated, low-foaming nonionic surfactants, are preferred in dishwasher detergents. Particularly preferred are detergents containing nonionic surfactants from the alkoxylated alcohol group. Nonionic surfactants with melting points above room temperature are particularly preferred. Nonionic surfactants with melting points above 20°C, preferably above 25°C, particularly between 25°C and 60°C, and especially between 26.6°C and 43.3°C, are particularly preferred. The surfactants used are preferably from the alkoxylated nonionic surfactant group, particularly ethoxylated primary alcohols and mixtures of these surfactants with structurally complex surfactants such as polyoxypropylene / polyoxyethylene / polyoxypropylene ((PO / EO / PO) surfactants). Such (PO / EO / PO) nonionic surfactants are also characterized by achieving good foam control. Nonionic surfactants having alternating ethylene oxide and alkylene oxide units are particularly preferred. Surfactants having EO-AO-EO-AO blocks are especially preferred, with one to ten EO and AO groups respectively linked to each other before the block of the other group. Here, the preferred general formula is... nonionic surfactants, wherein R 1 Represents linear or branched, saturated, monounsaturated, or polyunsaturated C 6-24 Alkyl or alkenyl functional groups; each R 2 or R 3 The groups are independently selected from -CH3, -CH2CH3, -CH2CH2-CH3, and -CH(CH3)2, and the indices w, x, y, and z independently represent integers from 1 to 6.

[0136] Therefore, it is particularly preferred to have C 9-15 A nonionic surfactant consisting of an alkyl functional group, 1 to 4 ethylene oxide units, followed by 1 to 4 propylene oxide units, followed by 1 to 4 ethylene oxide units, followed by 1 to 4 propylene oxide units.

[0137] The preferred nonionic surfactant here is of general formula R. 1 -CH(OH)CH2O-(AO) w -(A'O) x -(A''O) y -(A'''O) z -R 2 Of those, R 1 Represents linear or branched, saturated, monounsaturated, or polyunsaturated C 6-24 Alkyl or alkenyl functional groups; R 2 Represents H or a linear or branched hydrocarbon functional group having 2 to 26 C atoms; A, A', A'', and A''' independently represent functional groups from -CH2CH2, -CH2CH2-CH2, -CH2-CH(CH3), -CH2-CH2-CH2-CH2, -CH2-CH(CH3)-CH2-, -CH2-CH(CH2-CH3); and w, x, y, and z represent values ​​between 0.5 and 120, where x, y, and / or z can also be 0.

[0138] Particularly preferred are end-capped poly(oxyalkylated) nonionic surfactants, which are formulated according to formula R 1 O[CH2CH2O] x CH2CH(OH)R 2 In addition to the functional group R representing a linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon functional group having 2 to 30 C atoms, preferably 4 to 22 C atoms, 1 In addition, it also contains linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon functional groups R with 1 to 30 C atoms. 2 , where x represents a value between 1 and 90, preferably between 30 and 80, and especially between 30 and 60.

[0139] Formula R 1 O[CH2CH(CH3)O] x [CH2CH2O] y CH2CH(OH)R 2 The surfactant is particularly preferred, wherein R 1 R represents a linear or branched aliphatic hydrocarbon functional group or a mixture thereof having 4 to 18 C atoms. 2 This group represents linear or branched hydrocarbon functional groups or mixtures thereof having 2 to 26 carbon atoms, where x represents a value between 0.5 and 1.5, and y represents a value of at least 15. This group of nonionic surfactants includes, for example, C... 2-26 Fatty alcohols-(PO)1-(EO) 15-40 -2-hydroxyalkyl ethers, especially those including C 8-10 Fatty alcohols-(PO)1-(EO)22 -2-hydroxydecyl ether.

[0140] Formula R 1 O[CH2CH2O] x [CH2CH(R 3 )O] y CH2CH(OH)R 2 End-capped poly(oxyalkylated) nonionic surfactants are also particularly preferred, among which R 1 and R 2 Each group independently represents a linear or branched, saturated or monounsaturated or polyunsaturated hydrocarbon functional group having 2 to 26 carbon atoms. 3 The terms are independently selected from -CH3, -CH2CH3, -CH2CH2-CH3, and -CH(CH3)2, but preferably represent -CH3, and x and y independently represent values ​​between 1 and 32, where R 3 Nonionic surfactants with -CH3 and x values ​​of 15 to 32 and y values ​​of 0.5 and 1.5 are particularly preferred.

[0141] Other preferred nonionic surfactants are those of general formula R. 1 O[CH2CH(R 3 )O] x [CH2] k CH(OH)[CH2) j OR 2 End-capped poly(oxyalkylated) nonionic surfactants, wherein R 1 and R 2 R represents a functional group of linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbons having 1 to 30 carbon atoms. 3 The group represents H or a functional group of methyl, ethyl, n-propyl, isopropyl, n-butyl, 2-butyl, or 2-methyl-2-butyl, where x represents a value between 1 and 30, and k and j represent values ​​between 1 and 12, preferably between 1 and 5. If the value x ≥ 2, then the above formula R 1 O[CH2CH(R 3 )O] x [CH2] k CH(OH)[CH2) j OR 2 Each R in 3 They can be different. R 1 and R 2 Preferably, the functional groups are linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbons having 6 to 22 carbon atoms, with functional groups having 8 to 18 carbon atoms being particularly preferred. For functional group R... 3H, -CH3, or -CH2CH3 are particularly preferred. Particularly preferred values ​​for x are in the range of 1 to 20, especially 6 to 15. As mentioned above, if x ≥ 2, each R in the above formula... 3 They can be different. In this way, the alkylene oxide unit in the square brackets can be varied. For example, if x represents 3, the functional group R can be chosen. 3 To form ethylene oxide (R 3 =H) or propylene oxide (R 3 =CH3) units, which can be linked together in any order, such as (EO)(PO)(EO), (EO)(EO)(PO), (EO)(EO)(EO), (PO)(EO)(PO), (PO)(PO)(EO)(EO), and (PO)(PO)(PO)(PO). The value of 3 chosen for x here is an example, and it can certainly be larger. In this case, as the value of x increases, the range of variation increases, and includes, for example, combinations of a large number of (EO) groups with a small number of (PO) groups, and vice versa. Particularly preferred end-capped poly(oxyalkylated) alcohols of the above formula have values ​​of k=1 and j=1, thus the preceding formula simplifies to R. 1 O[CH2CH(R 3 )O] x CH2CH(OH)CH2OR 2 In the last formula mentioned, R 1 R 2 and R 3 As defined above, x represents numbers from 1 to 30, preferably from 1 to 20, and especially from 6 to 18. The functional group R... 1 and R 2 Having 9 to 14 C atoms, R 3 Surfactants representing H with x values ​​of 6 to 15 are particularly preferred.

[0142] Finally, the general formula R 1 -CH(OH)CH2O-(AO) w -R 2 Nonionic surfactants have been shown to be particularly effective, among which R 1 Represents linear or branched, saturated, monounsaturated, or polyunsaturated C 6-24 Alkyl or alkenyl functional groups; R 2 The group represents a linear or branched hydrocarbon functional group having 2 to 26 carbon atoms; A represents a functional group derived from CH2CH2, CH2CH2CH2, or CH2CH(CH3), preferably CH2CH2; w represents a value between 1 and 120, preferably 10 to 80, and particularly 20 to 40. This group of nonionic surfactants includes, for example, C... 4-22 Fatty alcohols (EO) 10-80 -2-hydroxyalkyl ethers, particularly including C8-12 Fatty alcohols (EO) 22 -2-hydroxydecyl ether and C 4-22 Fatty alcohols (EO) 40-80 -2-hydroxyalkyl ether.

[0143] In various embodiments of the invention, corresponding uncapped hydroxyl mixed ethers can be used instead of the capped hydroxyl mixed ethers defined above. These can satisfy the above formula, but where R 2 It is hydrogen and R 1 R 3 A, A', A'', A''', w, x, y, and z are as defined above. In various embodiments, the formulation, particularly automatic dishwasher detergents, contains at least one nonionic surfactant from the hydroxyl mixed ether group.

[0144] The formulations according to the invention preferably also contain a builder, preferably at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. Builders particularly include silicates, carbonates and / or organic (co)builders.

[0145] Polycarboxylates / polycarboxylate, polymeric polycarboxylates, aspartic acid, polyacetal, dextrin, other organic co-agents, and phosphonates are particularly noteworthy as organic (co-)agents. These categories of substances are described below. Organic co-agent substances may be included in formulations according to the invention in an amount of up to 60 wt.% based on the total weight of the formulation.

[0146] Suitable organic building blocks are, for example, polycarboxylic acids that can be used in the form of free acids and / or their sodium salts, where polycarboxylic acids are understood to mean carboxylic acids with more than one acid function. Examples include citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, glycolic acid, and carboxymethyl inulin; monomeric and polymeric amino polycarboxylic acids, particularly glycinic acid diacetate, methylglycinic acid diacetate, glutamine diacetate, iminodisuccinates such as ethylenediamine-N,N'-disuccinic acid and hydroxyiminodisuccinate, ethylenediaminetetraacetic acid and polyaspartic acid; polymeric hydroxy compounds such as dextrin; and polymeric (poly)carboxylic acids, particularly polycarboxylates obtainable through the oxidation of polysaccharides or dextrins; and / or polymeric acrylic acid, methacrylic acid, maleic acid, and their mixed polymers, which may also contain small amounts of polymerizable materials in polymeric form without carboxylic acid functional groups. Organic co-adjuvants, if desired, are included in textile detergents in an amount of up to 25 wt.%, preferably 1 to 8 wt.%, based on the total weight of the formulation. Automatic dishwasher detergents preferably contain organic co-adjuvants in an amount of 10 to 55 wt.%, particularly preferably 15 to 50 wt.%, based on the total weight of the formulation.

[0147] In addition to their role as builders, free acids often also possess the properties of acidifying components, and are therefore used to set lower and milder pH values ​​in formulations. Of particular note are citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid, and any mixtures thereof. Citric acid or its citrates are particularly preferred as builders. Further particularly preferred builders are selected from methylglycine diacetate (MGDA), glutamic acid diacetate (GLDA), aspartic acid diacetate (ASDA), hydroxyethyliminodiacetic acid (HEIDA), iminodisuccinate (IDS), ethylenediaminedisuccinate (EDDS), carboxymethyl inulin, and polyaspartate.

[0148] In a preferred embodiment, citric acid and / or citrates are used as water-soluble organic building blocks. Particularly preferred is the use of 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.%, of citric acid and / or 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.%, of citrates, preferably alkali metal citrates, and even more preferably sodium citrate, based on the total weight of the formulation. Citric acid / citrates can each be used in their hydrated forms; for example, citric acid can be used as a monohydrate, and citrates can be used as sodium tricitrate dihydrate.

[0149] Complexing agents are another preferred component of the formulations according to the invention. Particularly preferred complexing agents are phosphonates, provided their use is permitted by regulations. In addition to 1-hydroxyethane-1,1-bisphosphonic acid, complexed phosphonates include many different compounds such as diethylenetriaminepentamethylenephosphonic acid (DTPMP). Hydroxyalkyl or aminoalkylphosphonates are particularly preferred in this application. Among hydroxyalkylphosphonates, 1-hydroxyethane-1,1-bisphosphonate (HEDP) is particularly important as a co-agent. It is preferably used as a sodium salt; the disodium salt reacts neutrally, and the tetrasodium salt reacts alkalinely (pH 9). Possible aminoalkylphosphonates preferably include ethylenediaminetetramethylenephosphonate (EDTMP), diethylenetriaminepentamethylenephosphonate (DTPMP), and their higher homologues. They are preferably used in the form of neutral-reacting sodium salts, such as the hexasodium salt of EDTMP or the heptasodium and octasodium salts of DTPMP. Among phosphonates, HEDP is preferably used as a co-agent. Aminoalkane phosphonates also have a significant heavy metal binding capacity. Therefore, it may be preferred, especially if the formulation also contains a bleaching agent, to use an aminoalkane phosphonate, particularly DTPMP, or a mixture of the above phosphonates. In the context of this application, preferred formulations contain one or more phosphonates selected from: aminotrimethylenephosphonic acid (ATMP) and / or its salts; ethylenediaminetetra(methylenephosphonic acid) (EDTMP) and / or its salts; diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) and / or its salts; 1-hydroxyethane-1,1-diphosphonic acid (HEDP) and / or its salts; 2-phosphonobutane-1,2,4-tricarboxylic acid (PBTC) and / or its salts; hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP) and / or its salts; and nitrilotri(methylenephosphonic acid) (NTMP) and / or its salts. Formulations containing 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or diethylenetriaminepenta (methylenephosphonic acid) (DTPMP) as phosphonates are particularly preferred. Formulations according to the invention may, of course, contain two or more different phosphonates.

[0150] The preferred formulation according to the invention is characterized in that it contains at least one complexing agent from the phosphonate group, preferably 1-hydroxyethane-1,1-bisphosphonate, wherein the weight ratio of the phosphonate to the total weight of the formulation is preferably 0.1 to 10.0 wt.%, preferably 0.2 to 8.0 wt.%, preferably 0.25 to 5.0 wt.%, more preferably 0.3 to 3.0 wt.%, particularly preferably 0.5 to 2.0 wt.%, preferably 1-hydroxyethane-1,1-bisphosphonate, for use in textile detergents. At least one complexing agent from the phosphonate group, preferably 1-hydroxyethane-1,1-bisphosphonate, is preferably used in the automatic dishwasher detergent according to the invention, wherein the weight ratio of the phosphonate to the total weight of the formulation is preferably 0.5 to 8.0 wt.%, preferably 1.0 to 7.0 wt.%, particularly preferably 1.5 to 6.5 wt.%.

[0151] In a further preferred embodiment, the formulations according to the invention are substantially free of phosphonate compounds. In this context, "substantially free of phosphonate compounds" means that, based on the total weight of the formulation, the corresponding formulation or composition contains less than 2 wt.%, preferably less than 1 wt.%, more preferably less than 0.5 wt.%, and particularly preferably less than 0.1 wt.% of phosphonate compounds. In a particularly preferred embodiment, these formulations / compositions are free of phosphonate compounds.

[0152] In a more preferred embodiment, the complexing agent (building agent) is selected from amino polycarboxylic acids, particularly MGDA and GLDA. As used herein, the term "MGDA" includes, but is not limited to, methylglycine diacetic acid, α-alanine diacetic acid, N-(1-carboxyethyl)-iminodiacetic acid, and N,N-bis(carboxymethyl)-DL-alanine, including the free acid form and the corresponding salt, preferably an alkali metal salt, particularly a trisodium salt. As used herein, the term "GLDA" includes, but is not limited to, glutamic acid diacetic acid, L-glutamic acid-N,N-diacetic acid, and N,N-bis(carboxymethyl)-L-glutamate, including the free acid form and the corresponding salt, preferably an alkali metal salt, particularly a tetrasodium salt.

[0153] While higher MGDA or GLDA concentrations are possible based on the total weight of the formulation, it is preferred in textile detergents when MGDA, particularly up to 25 wt.%, especially 0.2 to 5 wt.%, preferably 0.25 to 3 wt.%, and even more preferably 0.5 to 2 wt.%, is used, preferably trisodium MGDA (MGDA-Na3). Even more preferred is the use of GLDA, preferably tetrasodium GLDA (GLDA-Na4), at 0.2 to 5 wt.%, preferably 0.25 to 3 wt.%, and even more preferably 0.5 to 2 wt.%, based on the total weight of the formulation.

[0154] In automatic dishwasher detergents, the amount of MGDA or GLDA is preferably 2.0 to 40 wt.%, particularly preferably 5.0 to 30 wt.%, especially 8.0 to 25 wt.%, and very particularly preferably 10.0 to 20 wt.%, based on the total weight of the formulation. Preferably, trisodium MGDA is used at these amounts.

[0155] The solid formulations according to the present invention preferably contain at least one water-soluble and / or water-insoluble, organic and / or inorganic detergent builder. Water-soluble organic detergent builders include the aforementioned organic detergent builders.

[0156] In addition to the aforementioned water-soluble organic detergent builders, the formulations of the present invention may further contain inorganic water-soluble detergent builders. In particular, alkali metal silicates, alkali metal carbonates, alkali metal bicarbonates, alkali metal phosphates, and / or sesquicarbonates, which may exist in their basic, neutral, or acidic sodium or potassium salt forms, can be used as water-soluble inorganic detergent builder materials. A small amount of calcium carbonate may optionally also be included in the solid textile detergent.

[0157] Suitable alternatives include, for example, water-soluble crystalline and / or amorphous alkali metal silicates. Alkali metal silicates that can be used as builders in formulations according to the invention preferably have a molar ratio of alkali metal oxide to SiO2 of less than 0.95, particularly 1:1.1 to 1:12, and can exist in amorphous or crystalline form. Preferred alkali metal silicates are sodium silicates, particularly amorphous sodium silicates, with a Na2O:SiO2 molar ratio of 1:2 to 1:2.8. As crystalline silicates, they can exist alone or in mixture with amorphous silicates, preferably using the general formula Na2Si. x O 2x+1× y H2O crystalline layered silicates, where x, called the modulus, is a number from 1.9 to 22, particularly from 1.9 to 4, and y is a number from 0 to 33, with a preferred value of x being 2, 3, or 4. Preferred crystalline lamellar silicates are those in which x takes the value of 2 or 3 in the above general formula. In particular, β- and δ-disilicates (Na2Si2O5× yH2O) are preferred. Nearly anhydrous crystalline alkali metal silicates of the above general formula, where x is a number from 1.9 to 2.1, and produced from amorphous alkali metal silicates, may also be used in the formulations according to the invention. In another embodiment of the formulation according to the invention, crystalline sodium silicate lamellar silicates having a modulus of 2 to 3 are used, such as those prepared from sand and soda. In another embodiment of the formulation according to the invention, crystalline sodium silicate having a modulus in the range of 1.9 to 3.5 is used. In formulations containing amorphous and crystalline alkali metal silicates, the weight ratio of amorphous alkali metal silicate to crystalline alkali metal silicate is preferably 1:2 to 2:1, particularly 1:1 to 2:1. The crystalline lamellar silicates described above are sold by Clariant GmbH under the trade name Na-SKS, for example, Na-SKS-1 (Na2Si...). 22 O 45 × x H2O, kenyaite), Na-SKS-2 (Na2Si 14 O 29 × x H2O, magadiite), Na-SKS-3 (Na2Si8O 17 (× x H2O) or Na-SKS-4 (Na2Si4O9× x H2O, macatite). Among them, Na-SKS-5 (α-Na2Si2O5), Na-SKS-7 (β-Na2Si2O5, natrosilite), Na-SKS-9 (NaHSi2O5× 3 H2O), Na-SKS-10 (NaHSi2O5× 3 H2O, kanemite), Na-SKS-11 (t-Na2Si2O5), and Na-SKS-13 (NaHSi2O5), but Na-SKS-6 (δ-Na2Si2O5) is particularly suitable. In one embodiment of the formulation according to the invention, a particulate compound made from crystalline lamellar silicates and citrates, crystalline lamellar silicates and the above-described (co)polymerized polycarboxylic acids, or alkali metal silicates and alkali metal carbonates, is used, for example, commercially available under the trade name Nabion® 15. This water-soluble inorganic building block material is preferably included in the formulation according to the invention in an amount of 1 to 20 wt.%, particularly 5 to 15 wt.%, based on the total weight of the formulation. Carbonates (and bicarbonates), especially sodium carbonate, are also important as water-soluble inorganic building blocks.

[0158] Alkali metal carbonates, particularly sodium carbonate (baking soda), are preferred detergent builders in automatic dishwasher detergents. Typical amounts are in the range of 5 to 50 wt.%, preferably 10 to 40 wt.%, and particularly 15 to 30 wt.%, based on the total weight of the formulation in each case.

[0159] The formulations according to the present invention are preferably free of phosphate builders, i.e., contain less than 1 wt.% based on the total weight of the formulation, and preferably without any intentionally added phosphate builders.

[0160] The formulations according to the invention may also contain water-insoluble building blocks. Crystalline or amorphous water-dispersible alkali metal aluminosilicates, in amounts up to 50 wt.%, preferably not exceeding 40 wt.%, particularly 3 to 20 wt.%, especially preferably 1 to 15 wt.%, based on the total weight of the formulation, are particularly used as water-insoluble inorganic building blocks. Preferably, crystalline sodium aluminosilicates of detergent quality, particularly zeolite A, zeolite P, zeolite MAP, and optionally zeolite X, are used, either alone or in mixtures, for example, in the co-crystallization of zeolite A and X (Vegobond® AX, a commercial product of Condea Augusta SpA). Amounts close to the said upper limit are preferred for solid particulate formulations. Suitable aluminosilicates, in particular, do not have particles larger than 30 µm and preferably consist of at least 80 wt.% particles smaller than 10 µm. The calcium-binding capacity of the aluminosilicates, as determined according to DE 2412837 A1, is generally in the range of 100 to 200 mg CaO per gram.

[0161] In a preferred embodiment, the formulation according to the invention comprises a builder system containing at least one builder, preferably in an amount of 0.5 to 50 wt.%, more preferably 0.5 to 20 wt.%, particularly preferably 0.5 to 10 wt. wt.% (based on the total weight of the formulation), wherein the detergent builder is selected from polycarboxylic acids such as citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, succinic acid, and carboxymethyl inulin or their salts; monomers and polymeric amino polycarboxylic acids such as glycine diacetic acid, methylglycine diacetic acid (MGDA), glutamic acid diacetic acid (GLDA), hyponitrotriacetic acid, iminodisuccinates such as ethylenediamine-N,N'-disuccinate (EDDS) and hydroxyiminodisuccinate, ethylenediaminetetraacetic acid and polyaspartic acid or their salts; polyphosphonic acids such as aminotris(methylenephosphonic acid), ethylenediaminetetra(methylenephosphonic acid), lysine tetra(methylenephosphonic acid), diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) and 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or their salts; polymeric hydroxy compounds such as dextrin; and mixtures thereof.

[0162] In a preferred embodiment, the formulation according to the invention, preferably a textile detergent, contains, in each case, based on the total weight of the formulation, (i) at least 0.0000001 wt.% of at least one peptide according to the invention (ii) 0 to 10 wt.%, preferably 1 to 4 wt.%, of citric acid and / or citrate, preferably alkali metal citrate, (iii) 0 to 40 wt.%, preferably 0 to 15 wt.%, more preferably 1 to 3 wt.%, of an alkali metal carbonate, preferably sodium carbonate. (iv) 0 to 20 wt.%, preferably 3 to 10 wt.%, of alkali metal silicates. (v) 0 to 10 wt.%, preferably 0.5 to 2 wt.%, of phosphonic acid and / or alkali metal phosphonates, particularly preferably HEDP and / or DTPMP. (vi) 0 to 10 wt.%, preferably 0.5 to 3 wt.%, of amino polycarboxylic acid, preferably MGDA and / or GLDA.

[0163] In other preferred embodiments, the formulation according to the invention is preferably an automatic dishwasher detergent, which in each case contains based on the total weight of the formulation. (i) at least 0.0000001 wt.% of at least one peptide according to the invention (ii) 0 to 20 wt.%, preferably 1.0 to 15.0 wt.%, of citric acid and / or citrate, preferably alkali metal citrate, (iii) 0 to 40 wt.%, preferably 5 to 30 wt.%, more preferably 10 to 25 wt.%, of an alkali metal carbonate, preferably sodium carbonate. (iv) 0 to 20 wt.%, preferably 3 to 10 wt.%, of alkali metal silicates. (v) 0 to 10 wt.%, preferably 0.5 to 8 wt.%, of phosphonic acid and / or alkali metal phosphonates, particularly preferably HEDP and / or DTPMP, and / or (vi) 0 to 25 wt.%, preferably 5.0 to 20.0 wt.%, of amino polycarboxylic acid, preferably MGDA and / or GLDA.

[0164] Possible peroxide compounds suitable for formulations according to the invention include, in particular, peracids or peracid salts of organic peroxides, such as salts of phthalimide perhexanoic acid, perbenzoic acid, or diperdodecanoic acid, hydrogen peroxide, and inorganic salts that release hydrogen peroxide under washing conditions, including perborates, percarbonates, persilicates, and / or persulfates such as peroxymonosulfate, and hydrogen peroxide inclusion complexes such as H₂O₂-urea adducts. Hydrogen peroxide can also be produced by an enzymatic system, i.e., oxidases and their substrates. If solid peroxide compounds are intended to be used, they can be used in powder or granule form, and can also be coated in a manner known per se. Peroxide compounds can be added to washing liquids either on their own or in formulations containing them, which in principle can contain all conventional washing, cleaning, or disinfecting components. Alkali metal percarbonates or alkali metal perborate monohydrates are particularly preferred. If the formulation according to the invention contains peroxides, they are preferably present in an amount of up to 50 wt.%, particularly 5 to 30 wt.%, more preferably 0.1 to 20 wt.%, based on the total weight of the formulation in each case.

[0165] Compounds that produce aliphatic peroxycarboxylic acids and / or optionally substituted perbenzoic acids under hydrolytic conditions, preferably with 1 to 10 carbon atoms, particularly 2 to 4 carbon atoms, can be used as bleaching activators in formulations. Suitable substances are those with O- and / or N-acyl groups and / or optionally substituted benzoyl groups bearing a specified number of carbon atoms. Preferred are polyacylated alkylene diamines, particularly tetraacetylethylenediamine (TAED); acylated triazine derivatives, particularly 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT); acylated glycourea, particularly tetraacetylglycourea (TAGU); N-imides, particularly N-nonanoylsuccinimide (NOSI); acylated phenol sulfonates or carboxylates or their sulfonic or carboxylic acids, particularly nonanoyloxybenzenesulfonate or isonanoyloxybenzenesulfonate or lauroyloxybenzenesulfonate (NOBS or isoNOBS or LOBS), 4-(2-decanoyloxyethoxycarbonyloxy)-benzenesulfonate (DECOBS) or decanoyloxybenzoic acid. Salts (DOBA); carboxylic anhydrides, especially phthalic anhydrides; acylated polyols, especially triacetin, ethylene glycol diacetate, 2,5-diacetoxy-2,5-dihydrofuran and enol esters, and acetylated sorbitol and mannitol or mixtures thereof (SORMAN); acylated sugar derivatives, especially pentaacetyl glucose (PAG), pentaacetylfructose, tetraacetylxylose and octaacetyllactone; acetylated, optionally N-alkylated glucosamines and gluconic acid lactones; N-acylated lactams, such as N-benzoylcaprolactam; nitriles from which perimides are formed, especially aminoacetonitrile derivatives having quaternized nitrogen atoms; and / or oxygen-transferring sulfonamides and / or acylhydrazones. Hydrophilically substituted acyl acetals and acyl lactams are also preferred. Combinations of conventional bleaching activators may also be used. Such bleaching activators may be present, particularly in the presence of the aforementioned hydrogen peroxide-releasing bleaching agents, in conventional amounts, preferably 0.5 to 10 wt.%, particularly 1 to 8 wt.% (based on the total weight of the formulation), but preferably not at all when percarboxylic acid is used as the sole bleaching agent.

[0166] In addition to or in place of conventional bleaching activators, sulfonamides and / or bleaching-enhancing transition metal salts or transition metal complexes can also be included as so-called bleaching catalysts in solid formulations, particularly textile detergents.

[0167] Suitable anti-ashing agents or detergency active ingredients (detergent polymers), particularly for textile detergents, are cellulose ethers, such as carboxymethyl cellulose, methyl cellulose, hydroxyalkyl cellulose, and mixed cellulose ethers, such as methyl hydroxyethyl cellulose, methyl hydroxypropyl cellulose, and methyl carboxymethyl cellulose. Sodium carboxymethyl cellulose, hydroxypropyl methyl cellulose, and mixtures thereof, and optionally mixtures thereof with methyl cellulose, are preferred. Commonly used detergency active ingredients include copolyesters containing dicarboxylic acid units, alkylene glycol units, and polyalkylene glycol units. In formulations according to the invention, the proportion of anti-ashing agents and / or detergency active ingredients is generally no more than 2 wt.%, preferably 0.5 to 1.5 wt.%, and particularly preferably 0.5 to 2 wt.% (based on the total weight of the formulation).

[0168] For example, derivatives of diaminostilbene disulfonic acid or their alkali metal salts can be included as optical brighteners in textile detergents, particularly for textiles made of cellulosic fibers (e.g., cotton). Suitable examples include salts of 4,4'-bis(2-anilino-4-morpholino-1,3,5-triazinyl-6-amino)stilbene-2,2'-disulfonic acid or compounds with similar structures, wherein the morpholino group has a diethanolamine, methylamine, or 2-methoxyethylamine. Furthermore, substituted 4,4'-stilbene-biphenyl type brighteners, such as 4,4'-bis-(4-chloro-3-sulfostyleno)-biphenyl, can be present. Mixtures of brighteners can also be used. For polyamide fibers, 1,3-diaryl-2-pyrazoline type brighteners, such as 1-(p-sulfonylaminophenyl)-3-(p-chlorophenyl)-2-pyrazoline, and compounds with similar structures are particularly suitable. The content of optical brighteners or brightener mixtures in the formulation is generally no more than 1 wt.%, preferably 0.05 to 0.5 wt.% (based on the total weight of the formulation). In a preferred embodiment of the invention, the formulation does not contain such active ingredients.

[0169] Conventional foam modifiers that can be used in formulations according to the invention include, for example, polysiloxane-silicic acid mixtures, wherein the finely fragmented silicic acid contained therein is preferably silanized or otherwise hydrophobically modified. Polysiloxanes can consist of linear compounds and cross-linked polysiloxane resins and mixtures thereof. Other defoamers are paraffinic hydrocarbons, particularly microcrystalline waxes and paraffins with melting points above 40°C, saturated fatty acids, or soaps having particularly 20 to 22 carbon atoms, such as sodium behenate, and alkali metal salts of monoalkyl and / or dialkyl phosphates, wherein each alkyl chain has 12 to 22 carbon atoms. Preferably, defoamers with C... 16-18 Alkyl monoalkyl phosphate and / or dialkyl phosphate. The proportion of foam regulator is preferably 0.2 to 2 wt.%, particularly preferably not more than 1 wt.% (based on the total weight of the formulation).

[0170] To set the desired pH, the formulations according to the invention may contain system-compatible and environmentally friendly acids, particularly citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid, and / or adipic acid, but also include inorganic acids, particularly sulfuric acid or alkali metal hydrogen sulfates, or bases, particularly ammonium hydroxide or alkali metal hydroxides, preferably sodium hydroxide. These types of pH adjusters are preferably included in the formulations according to the invention in an amount preferably not greater than 10 wt.%, particularly 0.5 to 6 wt.%, and especially preferably 0.3 to 2 wt.%, based on the total weight of the formulation.

[0171] The formulation according to the invention has a pH in a 1 wt.% solution in deionized water at 20°C ranging from about 6 to about 11.5, preferably from about 7 to about 11, more preferably from about 7.5 to about 10.5, and particularly preferably from about 8 to about 10.

[0172] As an additional component, the formulations according to the invention may contain organic solvents. The addition of organic solvents has beneficial effects on the enzyme stability and cleaning properties of these formulations. Preferred organic solvents are derived from the group consisting of monohydric or polyhydric alcohols, alkanolamines, or glycol ethers. Solvents are preferably selected from ethanol, n-propanol or isopropanol, butanol, ethylene glycol, propylene glycol, butanediol, glycerol, diethylene glycol, propylene glycol diethylene glycol, butyl diethylene glycol, hexanediol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, diethylene glycol ethyl ether, propylene glycol methyl ether, propylene glycol ethyl ether, propylene glycol propyl ether, dipropylene glycol methyl ether, dipropylene glycol ethyl ether, methoxytriethylene glycol, ethoxytriethylene glycol, butoxytriethylene glycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol tert-butyl ether, and mixtures of these solvents. The organic solvents are preferably present in a weight ratio of 0.1 to 10 wt.%, more preferably 0.2 to 8.0 wt.%, and even more preferably 0.5 to 5.0 wt.% of the total weight of the formulation according to the invention. A particularly preferred organic solvent, which is particularly effective in stabilizing detergents, is glycerol and 1,2-propanediol. The liquid formulation preferably contains at least one polyol, preferably from the group consisting of glycerol and 1,2-propanediol, preferably in an amount of 0.1 to 10 wt.%, more preferably 0.2 to 8.0 wt.%, and more preferably 0.5 to 5.0 wt.% based on the total weight of the formulation. Other preferred organic solvents are organic amines and alkanolamines. The formulation according to the invention preferably contains these amines in an amount of 0.1 to 10 wt.%, preferably 0.2 to 8.0 wt.%, and more preferably 0.5 to 5.0 wt.% (based on the total weight of the formulation). Ethanolamine is a particularly preferred alkanolamine.

[0173] Furthermore, the formulations according to the invention (particularly for automatic dishwashers) may contain a bleaching catalyst. Usable bleaching catalysts include, but are not limited to, bleaching-enhancing transition metal salts and transition metal complexes, preferably Mn, Fe, Co, Ru, or Mo complexes, particularly those derived from manganese and / or cobalt salts and / or complexes, especially cobalt (amine) complexes, cobalt (acetate) complexes, cobalt (carbonyl) complexes, chlorides of cobalt or manganese, manganese sulfate, and complexes of manganese with 1,4,7-trimethyl-1,4,7-triazacyclononane (Mn3-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (Mn4-TACN).

[0174] Automatic dishwasher detergents containing 0.001 to 1 wt.%, preferably 0.01 to 0.1 wt.%, of bleaching catalyst, preferably Mn complexes, especially complexes of manganese with 1,4,7-trimethyl-1,4,7-triazacyclononane (Mn3-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (Mn4-TACN) are preferred.

[0175] The formulations according to the invention may contain hydrolases or other enzymes at concentrations suitable for the potency of the formulation. Therefore, formulations further comprising one or more enzymes represent another embodiment of the invention. All enzymes that can exhibit catalytic activity in the formulations according to the invention, particularly those selected from proteases, lipases, amylases, cellulases, hemicellulases, mannanases, tanninases, xylanases, xanthan gumases, xyloglucanases, β-glucosidases, pectins, carrageenans, hydrolases, oxidases, or redox enzymes and mixtures thereof, are preferably used as enzymes. The enzyme is advantageously expressed in units of 1 x 10⁻⁶ based on the total weight of the active protein and the formulation. -8 It is included in the formulation in an amount of up to 5 wt.%. Preferably, it is incrementally increased based on the total weight of the active protein and the formulation, with each enzyme in a quantity of 1 x 10⁻⁶. -7 The enzyme is included in the formulation according to the invention in amounts of up to 3 wt.%, 0.00001 to 1 wt.%, 0.00005 to 0.5 wt.%, 0.0001 to 0.1 wt.%, and particularly preferably 0.0001 to 0.05 wt.%. Particularly preferably, the enzyme exhibits synergistic cleaning properties against a specific stain or dirt, i.e., the enzymes included in the formulation composition mutually assist each other in terms of cleaning performance.

[0176] In a preferred embodiment, the formulation according to the invention contains at least one enzyme, and preferably at least two, three, four or five enzymes, preferably selected from proteases, amylases, cellulases, mannanases, pectic acid lyases and mixtures thereof, with a total content of 0.01 to 10 wt.%, preferably 0.1 to 8 wt.%, particularly preferably 0.2 to 6 wt.% (based on the total weight of the active protein and the formulation).

[0177] Examples of proteases are derived from Bacillus amyloliquefaciens (Bambusa amyloliquefaciens). Bacillus amyloliquefaciens Bacillus subtilis protease BPN′ and Bacillus licheniformis ( Bacillus licheniformis Carlsberg, protease PB92, subtilisin 147 and 309, and Bacillus tarda ( Bacillus lentusThe proteases of *Bacillus subtilis* DY, and the enzymes Thermitase, Proteinase K, and proteases TW3 and TW7, are narrowly related to subtilases but no longer related to *Bacillus subtilis* proteases. *Bacillus subtilis* proteases Carlsberg are available from Novozymes in developmental form under the trade name Alcalase®. *Bacillus subtilis* proteases 147 and 309 are marketed by Novozymes under the trade names Esperase® and Savinase®, respectively. Protease variants derived from *Bacillus tarda* DSM 5483, such as those described in WO 95 / 23221, WO 92 / 21760, WO 2013 / 060621, and EP 3660151, are also mentioned. Other suitable proteases include, for example, enzymes available from Novozymes under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase®, Progress Uno 101L®, and Ovozyme®; enzymes available from Danisco / DuPont under the trade names Purafect®, Purafect® OxP, Purafect® Prime, Excellase®, and Properase®, Preferenz P100®, and Preferenz P300®; enzymes available from BASF under the trade name Lavergy pro 104 LS®; enzymes available from Advanced Biochemicals Ltd. under the trade name Protosol®; enzymes available from Wuxi Snyder Bioproducts Ltd. under the trade name Wuxi®; enzymes available from Amano Pharmaceuticals Ltd. under the trade names Proleather® and Protease P®; and enzymes available from Kao Corp. under the name Proteinase K-16. It is especially preferred to use Bacillus griseus (B. griseus) Bacillus gibsonii ) and Bacillus pumilus ( Bacillus pumilus The protease of , disclosed in WO2008 / 086916, WO 2007 / 131656, WO 2017 / 215925, WO 2021 / 175696 and WO 2021 / 175697.

[0178] Examples of amylase are from Bacillus licheniformis , Bacillus amyloliquefaciens Or thermophilic lipophilic bacillus ( Bacillus stearothermophilusα-Amylase, and particularly its improved applications in detergents and cleaning agents. Bacillus licheniformis The enzyme is available from Novozymes under the name Termamyl® and from Danisco / DuPont under the name Purastar® ST. This α-amylase is available under the trade names Duramyl® and Termamyl® ultra (both from Novozymes), Purastar® OxAm (Danisco / DuPont), and Keistase® (Daiwa Seiko Inc.). Bacillus amyloliquefaciens The α-amylase is marketed by Novozymes under the name BAN®, and derivative variants of α-amylase from Bacillus stearothermophilus are also available from Novozymes under the names BSG® and Novamyl®. Others of particular note for this purpose are from... Bacillus sp. α-Amylase from A 7-7 (DSM 12368) and from Bacillus mucilaginosus ( Bacillus agaradherens Cyclodextrin glucan transferase (CGTase) from DSM 9948. Fusion products of all the mentioned molecules can also be used. Additionally, those from Aspergillus niger (… Aspergillus niger ) and Aspergillus oryzae ( A. oryzae The development of α-amylase products, which are available from Novozymes under the trade name Fungamyl®, is also suitable. Other commercially available products that may be advantageously used are, for example, Amylase-LT® and Stainzyme® or Stainzyme® ultra or Stainzyme® plus, and Amplify™ 12L or Amplify Prime™ 100L or Amplify Prime™ 120L, the latter also from Novozymes, and the PREFERENZ S® series from Danisco / DuPont, including, for example, PREFERENCE S100®, PREFERENCE S1000® or PREFERENCE S210®. Variants of these enzymes obtained through point mutations may also be used.

[0179] Suitable cellulases include those derived from bacteria or fungi. Chemically modified or protein-engineered mutants are also included. Suitable cellulases are those derived from the genus *Bacillus* (…). Bacillus ), Pseudomonas spp. Pseudomonas ), genus *Pythium* Humicola Fusarium ( ) Fusarium ), genus *Cladosporium* ( Thielavia ), genus Apocynum ( AcremoniumCellulases, such as those derived from thermophilic humic molds (… Humicola insolens ), thermophilic hygrophytes ( Myceliophthora thermophila ) and Fusarium oxysporum ( Fusarium oxysporum Fungal cellulases. Particularly suitable cellulases are alkaline or neutral cellulases with color-protecting properties. Examples of cellulases having endoglucanase activity (EC 3.2.1.4) are described in WO 2002 / 099091, such as those with amino acid sequences having at least 97% identity with positions 1 to 773 of SEQ ID NO:2 of WO 2002 / 099091. Another example may comprise GH44-xyglucanase, such as xyglucanase having at least 60% identity with positions 40 to 559 of SEQ ID NO:2 of WO 2001 / 062903. Other examples of cellulases include GH45 cellulases described in WO 96 / 29397. Commercially available cellulases include Celluzyme™, Carezyme™, Carezyme Premium™, Celluclean™ (e.g., Celluclean™ 5000L to Celluclean™ 4000T), Celluclean Classic™, Cellusoft™, Endolase®, Renozyme® and Whitezyme™ (Novozymes A / S), Clazinase™ and Puradax HA™ (Genencor International Inc.), KAC-500 (B)™ (Kao Corporation), Revitaranz™ 1000, Revitaranz™ 2000 and Revitaranz™ 3000 (DuPont), as well as Ecostone® and Biotouch® (AB Enzymes).

[0180] Suitable mannanases are, for example, Bacillus subtilis ( Bacillus subtilis Endo-β-mannanase, Bacillus sp. I633 endo-β-mannanase, Bacillus sp. AAI12 endonuclease-β-mannanase, Bacillus sp. AA349 endonuclease, Bacillus mucosa-agar NCIMB 40482 endonuclease, Bacillus halophilus ( Bacillus halodurans Endo-β-mannanase, Bacillus clausti ( Bacillus clausii Endo-β-mannanase, Bacillus licheniformis Endo-β-mannanase, thermophilic humic mold endo-β-mannanase and pyrolytic cellulosic bacteria strains ( Caldocellulosiruptor sp. Endo-β-mannanases (e.g., US 6060299, WO 99 / 64573, US 6566114 and WO 99 / 64619).

[0181] Pectate lyases suitable for detergents and cleaning agents are described, for example, in WO 2003 / 095638 or WO 2015 / 121133. Examples of suitable pectin-degrading enzymes also include enzymes and enzyme preparations available from Novozymes under the trade names Gamanase®, PektinexAR®, X-Pect®, or Pectaway®; enzymes available from AB Enzymes under the trade names Rohapect UF®, Rohapect TPL®, Rohapect PTE100®, Rohapect MPE®, Rohapect MA plus HC, Rohapect DA12L®, Rohapect 10L®, and Rohapect B1L®; and enzymes available from Diversa Corp. under the trade name Pyrolase®.

[0182] The peptides, proteins, and enzymes described herein are preferably mature peptides, proteins, or enzymes, i.e., catalytically active molecules without a signal peptide and / or propeptide. Unless otherwise stated, the given sequences also refer to the corresponding mature (processed) peptides, proteins, or enzymes.

[0183] In various embodiments of the invention, the corresponding peptide, protein, or enzyme is a free peptide, protein, or enzyme. This means that the peptide, protein, or enzyme can directly interact with all components of the formulation, and if the formulation is a liquid formulation, the peptide, protein, or enzyme is in direct contact with the solvent of the formulation (e.g., water). In other embodiments, the formulation may contain peptides, proteins, or enzymes that form interaction complexes with other molecules or contain a “capsule.” In this case, a single peptide, protein, or enzyme molecule, or multiple molecules thereof, can be separated from other formulation components by surrounding structures. Such separating structures can be generated by, but are not limited to, vesicles such as micelles or liposomes. However, the surrounding structures can also be viral particles, bacterial cells, or eukaryotic cells. In various embodiments, the formulation may contain *Bacillus pumilus* expressing peptides, proteins, or enzymes (…). Bacillus pumilus (or Bacillus subtilis cells, or cell culture supernatant of these cells.)

[0184] In the context of this invention, "characterized" means that the peptide, protein, or enzyme has one or more substitutions (or deletions or insertions) shown, i.e., it contains the (shown) substitution (or deletion or insertion) at the corresponding position, i.e., at least at the shown position there is no other mutation or deletion, such as by fragmentation of the peptide, protein, or enzyme. In various embodiments, the peptide, protein, and / or enzyme described herein has a sequence of the corresponding reference sequence that, except for the explicitly mentioned substitutions, i.e., except for the substituted positions, is 100% identical to the corresponding reference sequence.

[0185] The identity of nucleic acid or amino acid sequences is determined through sequence comparison. This sequence comparison is based on the BLAST algorithm, which is established and commonly used in the art (Altschul et al., Basic local alignment search tool, J. Mol. Biol., 1990, 215, 403-410, and Altschul et al., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic AcidsRes., 1997, 25, 3389-3402) and is performed in principle by assigning similar nucleotides or amino acid sequences within the nucleic acid or amino acid sequence to each other. The tabular assignment of relevant positions is called alignment. Another algorithm available in the art is the FASTA algorithm. Sequence comparison (alignment), especially multiple sequence comparison, is created using computer programs. Commonly used methods include the Clustal series (Chenna et al., Multiple sequence alignment with the Clustalseries of programs, Nucleic Acid Res., 2003, 31, 3497-3500), T-Coffee (Notredame et al., T-Coffee: A novel method for multiple sequence alignments, J. Mol. Biol., 2000, 302, 205-217), or programs based on these methods or algorithms. Sequence alignment can also be performed using the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with its specified standard parameters, whose AlignX module for sequence alignment is based on ClustalW, or using Clone Manager 10 (which performs sequence alignment at the amino acid level using the BLOSUM 62 scoring matrix). Unless otherwise stated, sequence identity indicated herein is determined using the BLAST algorithm.

[0186] This comparison can also draw conclusions about the similarity between the compared sequences. It is usually given as a percentage identity, that is, the proportion of identical nucleotide or amino acid residues at the same or corresponding positions in the alignment. In the case of amino acid sequences, the broader concept of homology considers conserved amino acid exchanges, i.e., amino acids with similar chemical activities, as these typically perform similar chemical activities within polypeptides, proteins, or enzymes. Therefore, the similarity of the compared sequences can also be expressed as percentage homology or percentage similarity. Identity and / or homology information can be provided for the entire polypeptide or gene or only for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are thus defined by matches in the sequence. Such regions typically have the same function. They can be small and contain only a few nucleotides or amino acids. Such small regions typically perform essential functions for the overall activity of the peptide, protein, or enzyme. Therefore, it may be appropriate to associate sequence matches only with individual (optionally small) regions. However, unless otherwise stated, the identity or homology information in this application refers to the entire length of the specific nucleic acid or amino acid sequence indicated.

[0187] In the context of this invention, indicating that the amino acid position corresponds to the position of the numerical marker in SEQ ID NO:1 means that in the alignment as defined above, the corresponding position is associated with the position of the numerical marker in SEQ ID NO:1.

[0188] For descriptions involving substitutions (amino acid exchanges) at exactly one amino acid position, the following conventions apply: First, the naturally occurring amino acid is referred to in its internationally used single-letter code form, followed by the relevant sequence position, and finally the inserted amino acid. Multiple substitutions within the same polypeptide chain are separated by slashes. "130D / V" thus means that position 130 has been mutated to D or V. In the case of insertion, the additional amino acid is named according to its sequence position. In the case of deletion, the deleted amino acid is replaced with a symbol (e.g., an asterisk or dash) or indicated by Δ before the corresponding position. For example, P9T describes the substitution of proline at position 9 by threonine, P9TH describes the insertion of histidine after threonine at position 9, and P9* or ΔP9 describes the deletion of proline at position 9. This nomenclature is known to those skilled in the art of enzyme technology.

[0189] Those skilled in the art can use currently known methods, such as chemical synthesis or polymerase chain reaction (PCR), combined with standard methods of molecular biology and / or protein chemistry, to produce corresponding nucleic acids or even complete genes based on known DNA and / or amino acid sequences. Such methods are known, for example, from Sambrook, J., Fritsch, EF and Maniatis, T. 2001. Molecular cloning: a laboratory manual, 3rd Edition, Cold Spring Laboratory Press.

[0190] Furthermore, the peptides, proteins, enzymes, and / or other components of the formulation contained herein can be encapsulated in a substance that is impermeable to the peptides, proteins, or enzymes at room temperature or under anhydrous conditions, but becomes permeable under the conditions of application of the formulation. Therefore, one such embodiment of the invention is characterized by encapsulating the peptides, proteins, or enzymes in a substance that is impermeable to the peptides, proteins, or enzymes at room temperature or under anhydrous conditions. Additionally, the detergent or cleaning agent itself can be packaged in a container, preferably a breathable container, from which it is released shortly before use or during washing.

[0191] In the formulations described herein, the peptide, protein, or enzyme to be used may be further packaged together with accompanying substances (e.g., from fermentation). In liquid formulations, the peptide, protein, or enzyme is preferably used as a liquid formulation of the peptide, protein, or enzyme.

[0192] Peptides, proteins, or enzymes are typically not provided in pure protein form, but rather in stable, storable, and transportable formulations. These pre-packaged formulations include, for example, solid formulations obtained by granulation, extrusion, or lyophilization, or, particularly in the case of liquid or gel formulations, solutions of peptides, proteins, or enzymes that are advantageously concentrated as much as possible, have a low water content, and / or are supplemented with stabilizers or other adjuvants.

[0193] Alternatively, peptides, proteins, or enzymes can be encapsulated in solid and liquid dosage forms, for example by spray drying or extrusion of a peptide, protein, or enzyme solution with a preferred natural polymer, or in capsule form, such as those in which the peptide, protein, or enzyme is encapsulated in a solidified gel, or in core-shell types, where the enzyme-containing core is covered by a protective layer impermeable to water, air, and / or chemicals. Other active ingredients such as stabilizers, emulsifiers, pigments, bleaching agents, or dyes can be additionally applied to the outer layer. Such capsules are applied using methods known per se, such as by shaking or spheronization or in a fluidized bed process. Advantageously, such particles are low in dust due to the application of a polymerizing film-forming agent, for example, and are storage stable due to the encapsulation.

[0194] In addition, two or more peptides, proteins or enzymes can be packaged together, so that a single particle contains multiple enzyme activities.

[0195] Peptides, proteins, or enzymes can also be incorporated into water-soluble membranes, such as those used in unit-sized packaging of detergents and cleaning agents. Such membranes allow the peptides, proteins, or enzymes to be released upon contact with water. As used herein, "water-soluble" refers to a membrane structure that is preferably completely water-soluble. Preferably, such a membrane is composed of (completely or partially hydrolyzed) polyvinyl alcohol (PVA).

[0196] The formulations according to the invention may contain one or more reversible enzyme inhibitors / stabilizers. The formulations according to the invention may contain reversible enzyme inhibitors / stabilizers at a concentration of 0.1 to 2 wt.%, preferably 0.3 to 1.5 wt.% (based on the total weight of the formulation). If several inhibitors / stabilizers are contained, this information refers to the total concentration. These may be particularly selected from polyols (e.g., glycerol or 1,2-ethylene glycol), benzoamide hydrochloride, borax, boric acid, boric acid or its salts or esters or derivatives (especially phenylboronic acid derivatives or 4-formylphenylboronic acid (4-FPBA)), antioxidants, specific peptide compounds, and combinations thereof.

[0197] In a preferred embodiment, the formulation according to the invention is a detergent and / or cleaning agent containing at least one fat-binding peptide as described herein and at least one enzyme with hydrolytic activity against ester bonds, preferably selected from lipases and esterases, particularly esterases with fat-decomposing activity, especially lipases.

[0198] In a preferred embodiment, the formulation according to the invention is a detergent and / or cleaning agent comprising at least one fat-binding peptide described herein and at least one lipase, wherein the lipase is selected from: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in increments of at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38.

[0199] In a preferred embodiment, the formulation according to the invention is a detergent and / or cleaning agent consisting of at least two phases, wherein at least one fat-binding peptide is contained in the first phase, and the at least one enzyme having hydrolytic activity against ester bonds, preferably selected from lipases and esterases, particularly esterases having fat-decomposing activity, especially lipases, is contained in the second phase.

[0200] In a preferred embodiment, the formulation according to the invention is a detergent and / or cleaning agent consisting of at least two phases, wherein the at least one fat-binding peptide is contained in the first phase, and the at least one lipase is contained in the second phase, wherein the lipase is selected from: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) At at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in increments of at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38.

[0201] In a preferred embodiment, the formulation according to the invention is a textile detergent, preferably a multiphase textile detergent. The textile detergent according to the invention is particularly suitable for textiles made of plastics and / or having a plastic content (blended fabrics) and / or made of natural fibers such as cotton. Preferably, the textiles comprise or are made of polyester (PES), polyethylene (PE), polypropylene (PP), polyurethane (PU), polystyrene (PS), polyvinyl chloride (PVC), polycarbonate (PC), polyamide (PA), polyphenylene ether, polyphenylene sulfide, polyoxymethylene (POM), polymethyl methacrylate (PMA), polyethylene terephthalate (PET), polybutylene terephthalate (PBT), polytetrafluoroethylene (PTFE), polyhydroxyalkanoates (PHA), polyhydroxybutyrate (PHB), polyimide (P... I) Fabrics composed of polylactide (PLA), polyvinylidene fluoride (PVDF), polyetherketone (PEK), and / or copolymers or blends thereof, even more preferably polyester (PES), polyethylene (PE), polypropylene (PP), polystyrene (PS), copolymers thereof, or blends thereof, preferably having at least 10%, preferably at least 20%, more preferably at least 30%, particularly preferably at least 40%, very particularly preferably at least 50%, especially at least 60%, for example, cotton / polyester blends with 65% or 70% polyester content, or pure polyester or copolymers thereof. The term "blended fabric" or "blended textile" refers to textiles with plastic content, preferably textiles made of at least one natural fiber and at least one plastic fiber (plastic content). In particular, blended fabrics or blended textiles are composed of cotton and at least one plastic, especially polyester. In a preferred embodiment, textiles having plastic content or plastic blends or blended textiles have at least 10%, preferably at least 20%, more preferably at least 30%, particularly preferably at least 40%, very particularly preferably at least 50%, especially at least 60%, for example, 65% or 70% plastic content.

[0202] In a preferred embodiment, the formulation is a cleaner for hard surfaces, particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., cutlery or pots) or glass.

[0203] Preferably, the peptides according to the invention, particularly when used in detergents and / or cleaning agents according to the invention, achieve detergency, particularly degreasing and / or degreasing effects, especially due to binding / adhesion to at least one greasy and / or oily stain, preferably greasy, on textiles (particularly composed of or made of cotton, polyester, and mixtures thereof) and / or hard surfaces (particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass). Therefore, the detergents and / or cleaning agents are preferably used as detergents in the washing process, particularly in machine washing or hand washing. The peptides described herein, when used in detergents and / or cleaning agents, not only improve cleaning performance on greasy and / or oily stains but also have detergency, particularly degreasing and / or degreasing effects. Therefore, they represent biodegradable alternatives to detergency polymers. Thus, these peptides are particularly suitable for detergents and cleaning agents and can contribute to improved cleaning performance. Furthermore, they can help reduce or completely eliminate synthetic and chemical substances, such as those in detergents and / or cleaning agents, by providing biodegradable alternatives. They also help stabilize other ingredients.

[0204] In this context, it is particularly preferred that the peptide according to the invention is surface-active and achieves stain removal, particularly degreasing and / or degreasing effect, by binding / adhering to at least one grease-containing and / or oil-containing, preferably grease-containing stains, on textiles (particularly composed of or made of cotton, polyester and mixtures thereof) and / or hard surfaces (particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastics), metal (e.g., tableware or pots) or glass), said surface activity as determined in Example 4.

[0205] In a particularly preferred embodiment, in the detergents and / or cleaning agents according to the invention, the peptides described herein result in improved cleaning performance on at least one grease- and / or oil-containing stain on textiles (particularly those containing or composed of cotton, polyester, and mixtures thereof) and / or hard surfaces (particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metals (e.g., cutlery or pots) or glass). The improved cleaning performance is preferably based on the synergistic interaction between the peptides and esterases according to the invention. The improved cleaning performance is particularly preferably based on the synergistic interaction between the peptides and lipases according to the invention.

[0206] Preferably, the improved cleaning performance of the detergents and / or cleaning agents according to the invention is based on the interaction of an enzyme with hydrolytic activity against ester bonds (preferably selected from lipases and esterases, especially esterases with fat-decomposing activity, particularly lipases) with a peptide according to the invention, said peptide binding to at least one grease- and / or oil-containing stain, preferably grease-containing stain, on textiles (particularly composed of or consisting of cotton, polyester, and mixtures thereof). Particularly preferred is that the improved cleaning performance of the detergents and / or cleaning agents according to the invention is based on the interaction of a lipase with a peptide according to the invention, said peptide binding to at least one grease- and / or oil-containing stain, preferably grease-containing stain, on textiles (particularly composed of or consisting of cotton, polyester, and mixtures thereof).

[0207] Preferably, the improved cleaning performance of the detergents and / or cleaning agents according to the invention is based on the interaction of an enzyme with hydrolytic activity against ester bonds (preferably selected from lipases and esterases, especially esterases with fat-decomposing activity, particularly lipases) with a peptide according to the invention, which binds to at least one grease- and / or oil-containing stain, preferably grease-containing stain, on a hard surface (particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass). Particularly preferred is that the improved cleaning performance of the detergents and / or cleaning agents according to the invention is based on the interaction of a lipase with a peptide according to the invention, which binds to at least one grease- and / or oil-containing stain, preferably grease-containing stain, on a hard surface (particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass).

[0208] Preferably, the peptides according to the invention have detergency, particularly degreasing and / or degreasing effects, especially on at least one greasy and / or oily stain on textile surfaces (particularly those containing or composed of cotton, polyester, and mixtures thereof) and / or hard surfaces (particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass). In particular, through the presence of the peptides, the peptides bind to at least one greasy stain on textile and / or hard surfaces, thereby releasing these surfaces from the stain.

[0209] Particularly preferred is that the peptide according to the invention is surface-active and has detergency, particularly degreasing and / or degreasing effects, especially with respect to at least one greasy and / or oily stain on textile surfaces (particularly those containing or composed of cotton, polyester, and mixtures thereof) and / or hard surfaces (particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass), the surface activity being determined as described in Example 4. In particular, through the presence of the peptide, which is surface-active and binds to at least one greasy stain on textile and / or hard surfaces, thereby releasing these stains from the surface, the surface activity being determined as described in Example 4.

[0210] One possible mechanism for the degreasing effect is that the peptides described herein can adsorb onto solid grease, thereby softening the grease film. This surfactant-like behavior makes it easier to remove the grease film during the cleaning process. The softened grease can be removed (by a coiling mechanism) and / or rinsed away. This mechanism can be explained by the surface-active behavior of the peptides according to the invention, the surface activity of which was determined as described in Example 4. An example of such a peptide is, for example, the peptide having SEQ ID NO:29.

[0211] Another possible mechanism is based on the peptides described herein, particularly the non-surface-active peptides according to the invention, forming a stable layer on the oily layer. Through this functionalization of the oily surface or binding to oily stains on the surface, other degreasing and / or oil-dissolving substances or molecules, especially lipases, become more accessible to the oily layer.

[0212] Therefore, the peptides according to the invention also allow for the removal of greasy stains at lower temperatures, such as about 15°C, about 20°C, or about 30°C. This enables the formulation of high-performance detergents and / or cleaning agents that exhibit good cleaning performance against at least one type of greasy stain, even at low temperatures, such as about 15°C, about 20°C, or about 30°C. In a preferred embodiment, this effect is also based on interaction with lipases. Improved grease removal, in addition to the hydrolysis of fat molecules by lipases, also improves the removal of decomposition products, thereby reducing or even preventing the accumulation or retention of decomposition products on surfaces. This reduces odor formation, particularly lowering the risk of unpleasant odors caused by lipase decomposition products.

[0213] All the facts, subjects, and embodiments described above also apply to the subject matter of this invention. Therefore, reference is made here to the disclosure at the relevant points, and it is noted that this disclosure also applies to the formulations described above according to the invention.

[0214] Another subject of the invention is a method for cleaning textiles, particularly those containing or composed of cotton, polyester, and mixtures thereof, and / or for cleaning hard surfaces, particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, characterized in that an agent according to the invention is used in at least one method step.

[0215] In a preferred embodiment, in the first step, at least one peptide according to the invention is brought into contact with the article to be washed or rinsed, and in the second step, at least one enzyme with hydrolytic activity against ester bonds, preferably selected from lipases and esterases, particularly esterases with fat-decomposing activity, especially lipases, is brought into contact with the article to be washed or rinsed.

[0216] In a preferred embodiment, in the first step, at least one peptide is brought into contact with the article to be washed or rinsed, and in the second step, at least one lipase is brought into contact with the article to be washed or rinsed. The peptides mentioned therein are selected from a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3 Selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or b) A peptide having an amino acid sequence identity of at least 80%, and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%, with one of the amino acid sequences listed in SEQ ID NOs: 1-31; and The lipase mentioned therein is selected from (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in sequence over its entire length at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38, preferably 100%.

[0217] In various embodiments, the above method is characterized by being carried out at a temperature of about 5°C to about 100°C, preferably about 10°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, and very particularly preferably about 20°C.

[0218] This includes both manual and machine methods, with machine methods being preferred because they allow for more precise control, such as regarding the amount used and the contact time. Methods for cleaning textiles are generally characterized by the application of various cleaning active substances to the material to be cleaned in multiple process steps, followed by washing off after a set time of contact, or by treating the material to be cleaned in other ways with a detergent or a solution or dilution of that formulation. The method preferably involves machine washing, particularly in a washing machine, or hand washing. The peptides described herein preferably function as anti-fouling and / or detergency active ingredients.

[0219] This invention also includes a dishwasher method. The cleaning agent according to the invention can be dispensed into the cleaning liquid, for example, through a dispensing chamber in the door or through an additional dispensing container inside the dishwasher. Alternatively, the cleaning agent can be applied directly to the dirty dishes or one of the interior walls of the dishwasher, such as the inside of the door. The method according to the invention is performed inside a commercially available dishwasher. In the case of a dishwasher, the cleaning program can typically be selected and determined by the user before the washing method begins. The dishwasher cleaning program used in the method according to the invention includes at least one washing cycle. According to the invention, a cleaning program preferably includes further washing or rinsing cycles, such as a pre-rinse cycle and / or a rinsing cycle. The method according to the invention is particularly preferably used as part of a cleaning program that includes an optional pre-rinse cycle, a washing cycle, and a rinsing cycle. The method according to the invention is preferably used in conjunction with a cleaning program in which the liquid is heated during the washing cycle.

[0220] Alternative embodiments of this subject matter are also represented by methods for treating textile raw materials or for textile care, wherein the formulations or peptides according to the invention become active in at least one method step. Preferably, the method is used for textile raw materials, fibers, or textiles containing natural components; particularly preferred is the method for textile raw materials, fibers, or textiles containing wool or silk.

[0221] The present invention also relates to the use of the formulations according to the invention for cleaning textiles, particularly textiles containing or composed of cotton, polyester and mixtures thereof, and / or hard surfaces, particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metals (e.g., tableware or pots) or glass, preferably at a temperature range of about 10°C to about 80°C, more preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, and very particularly preferably in the temperature range of about 20°C.

[0222] This invention also relates to the use of the peptide described herein in detergents and / or cleaning agents according to the invention, preferably lipase-containing detergents and / or cleaning agents, for improving the cleaning performance of the formulation against at least one type of grease- and / or oil-containing stain. The peptides mentioned therein are selected from a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3 Selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or b) A peptide having an amino acid sequence identity of at least 80%, and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%, with one of the amino acid sequences listed in SEQ ID NOs: 1-31; and The lipase mentioned therein is selected from (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in sequence, preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38. The application is preferably in the temperature range of about 10°C to about 80°C, more preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, and very particularly preferably about 20°C.

[0223] The present invention also relates to the use of the peptides according to the invention as detergency, particularly degreasing and / or oil-removing active ingredients in detergents and / or cleaning agents, preferably lipase-containing detergents and / or cleaning agents. The peptides mentioned therein are selected from a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3Selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or b) A peptide having an amino acid sequence identity of at least 80%, and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%, with one of the amino acid sequences listed in SEQ ID NOs: 1-31; and The lipase mentioned therein is selected from (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in sequence, preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38. The application is preferably in the temperature range of about 10°C to about 80°C, more preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, and very particularly preferably about 20°C.

[0224] All facts, topics, and embodiments described with respect to the peptides and formulations according to the invention also apply to these topics of the invention. Therefore, explicit reference is made herein to the disclosure at the corresponding points, wherein it is indicated that such disclosure also applies to the methods and uses according to the invention.

[0225] Preferred implementation scheme 1. A detergent and / or cleaning agent, comprising (A) at least one peptide, wherein the peptide is selected from... a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 )q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3 Selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or b) A peptide having an amino acid sequence identity of at least 80%, and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%, with one of the amino acid sequences listed in SEQ ID NOs: 1-31; and (B) At least one enzyme that has hydrolytic activity against ester bonds, preferably selected from lipases and esterases, especially esterases with lipolytic activity, and particularly preferably lipases.

[0226] 2. The formulation according to item 1, wherein the peptide according to item 1a) (i) The total charge is 0 to +4, or (ii) If r ≥ 4, the total charge is 0 to +4, or (iii) If r < 4, the total charge is +1 to +4, preferably +2 or +3.

[0227] 3. The formulation according to item 1 or 2, wherein in the peptide according to item 1a), if o = 1, p = 0, 1 or 2, q = 2 and r = 4, then the sequence (X) 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s Equal to Z 1 Z 2 Z 3 [(Z 4 ) u Z 5 Z 6 ]3(Z 7 ) v , in Z 1 As defined in Project 1, X 2 And selected from R, H and K, with R preferred, Z 2 Z 3 Z 5 and Z 6 As defined in Project 1, X 4 And selected from A, L, and V, with A and L being preferred. Z 4 As defined in Project 1, X 3 And selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with F, R, E, A, Q, and W preferred. u is 1 or 2. Z 7 As defined in Project 1, X 5 And selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V. v is defined as s in Project 1 and is an integer from 0 to 4.

[0228] 4. The formulation according to Project 3, wherein (i) If u = 1, Z 4 Selected from R, E, and Q, or (ii) If u = 2, (Z 4 )2 is selected from FR, FE, AR, WE, WR and AQ.

[0229] 5. The formulation according to item 3 or 4, wherein (i) The peptide contains at least one motif selected from RAL and RLA, preferably RAL, and wherein the sequence is preferably located at the N-terminal amino acid at positions 1-3; and / or (ii) The peptide contains at least one motif selected from EAL and ELA, preferably EAL, and wherein the motif is preferably not located in the N-terminal amino acids at positions 1-4; and / or (iii) The peptide contains at least one motif selected from QAL and QLA, preferably QAL; and / or (iv) The peptide contains at least one of the motifs RAL and QAL or EAL, preferably both; and / or (v) The peptide contains at least one, preferably two or three, RAL motifs; and / or (vi) The peptide contains at least two RAL motifs and at least one of QAL or EAL, preferably both.

[0230] 6. The formulation according to item 1 or 2, wherein in the peptide according to item 1a), if o = 1, p = 3-6, q = 1 or 2 and r = 2, then the sequence (X) 2 ) o [(X 3 ) p (X 4 ) q ] r Equal to Z 11 (Z 12 )6Z 13 Z 14 (Z 15 ) w Z 16 , in Z 11 As defined in Project 1, X 2 And selected from R, H and K, Z 12 As defined in Project 1, X 3 And selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, preferably A, N, C, Q, G, I, L, M, F, P, S, T, W, Y, and V, more preferably M, I, S, T, N, V, and F. Z 13 Z 14 Z 16 As defined in Project 1, X 4 And selected from A, L, and V, with A and L being preferred. Z 15 As defined in Project 1, X 3And selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with R, K, E, S, Q, and N being preferred. w is an integer from 3 to 6.

[0231] 7. The formulation according to item 6, wherein (i) Z 13 Z 14 Selected from AL and LA, with AL preferred; and / or (ii) (Z 15 ) w Where w = 3-6, and contains a sequence comprising at least one positively charged amino acid (R, H, or K); and / or (iii) (Z 15 ) w Where w = 3-6, comprising motifs selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, more preferably RQN; and / or (iv) Z 16 Choose from A and L, with A being the preferred option.

[0232] 8. The formulation according to any one of items 1 to 7, wherein the peptide has an amino acid sequence that is 80% and preferably increasing at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% identical to one of the amino acid sequences listed in SEQ ID NOs: 1-32, preferably SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, more preferably SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0233] 9. The formulation according to any one of items 1 to 8, wherein the lipase is selected from: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and Optionally (ii) at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in sequence over its entire length at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38, preferably 100%.

[0234] 10. A detergent and / or cleaning agent, comprising (A) At least one peptide, wherein the peptide is selected from peptides having an amino acid sequence having at least 80% and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31; and (B) At least one enzyme that has hydrolytic activity against ester bonds, preferably selected from lipases and esterases, especially esterases with lipolytic activity, and particularly preferably lipases.

[0235] 11. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:1; and (B) At least one lipase.

[0236] 12. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:2; and (B) At least one lipase.

[0237] 13. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:3; and (B) At least one lipase.

[0238] 14. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:4; and (B) At least one lipase.

[0239] 15. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:5; and (B) At least one lipase.

[0240] 16. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:6; and (B) At least one lipase.

[0241] 17. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:7; and (B) At least one lipase.

[0242] 18. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:8; and (B) At least one lipase.

[0243] 19. A detergent and / or cleaning agent comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:9; and (B) At least one lipase.

[0244] 20. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:10; and (B) At least one lipase.

[0245] 21. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:11; and (B) At least one lipase.

[0246] 22. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:12; and (B) At least one lipase.

[0247] 23. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:13; and (B) At least one lipase.

[0248] 24. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:14; and (B) At least one lipase.

[0249] 25. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:15; and (B) At least one lipase.

[0250] 26. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:16; and (B) At least one lipase.

[0251] 27. A detergent and / or cleaning agent comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:17; and (B) At least one lipase.

[0252] 28. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:18; and (B) At least one lipase.

[0253] 29. A detergent and / or cleaning agent comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:19; and (B) At least one lipase.

[0254] 30. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:20; and (B) At least one lipase.

[0255] 31. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:21; and (B) At least one lipase.

[0256] 32. A detergent and / or cleaning agent comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:22; and (B) At least one lipase.

[0257] 33. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:23; and (B) At least one lipase.

[0258] 34. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:24; and (B) At least one lipase.

[0259] 35. A detergent and / or cleaning agent comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:25; and (B) At least one lipase.

[0260] 36. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:26; and (B) At least one lipase.

[0261] 37. A detergent and / or cleaning agent comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:27; and (B) At least one lipase.

[0262] 38. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:28; and (B) At least one lipase.

[0263] 39. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:29; and (B) At least one lipase.

[0264] 40. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:30; and (B) At least one lipase.

[0265] 41. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:31; and (B) At least one lipase.

[0266] 42. The formulation according to any one of items 1 to 41, wherein the lipase is selected from: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in sequence over its entire length at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38, preferably 100%.

[0267] 43. A detergent and / or cleaning agent, comprising (A) at least one peptide having the same amino acid sequence as shown in SEQ ID NO:1; and (B) At least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0268] 44. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:2; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0269] 45. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:3; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0270] 46. ​​A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:4; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0271] 47. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:5; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0272] 48. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:6; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0273] 49. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:7; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0274] 50. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:8; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0275] 51. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:9; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0276] 52. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:10; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0277] 53. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:11; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0278] 54. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:12; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0279] 55. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:13; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0280] 56. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:14; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0281] 57. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:15; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0282] 58. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:16; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0283] 59. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:17; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0284] 60. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:18; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0285] 61. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:19; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering of SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0286] 62. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:20; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0287] 63. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:21; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0288] 64. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:22; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0289] 65. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:23; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0290] 66. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:24; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0291] 67. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:25; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0292] 68. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:26; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0293] 69. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:27; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0294] 70. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:28; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0295] 71. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:29; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0296] 72. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:30; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0297] 73. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:31; and (B) at least one lipase, wherein the lipase is a lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO:33, and in each case, based on the numbering in SEQ ID NO:33, (i) having amino acid substitutions T231R and N233R at positions corresponding to positions 231 and 233, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0298] 74. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:1; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0299] 75. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:2; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0300] 76. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:3; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0301] 77. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:4; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0302] 78. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:5; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0303] 79. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:6; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0304] 80. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:7; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0305] 81. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:8; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0306] 82. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:9; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0307] 83. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:10; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0308] 84. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:11; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0309] 85. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:12; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0310] 86. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:13; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0311] 87. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:14; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0312] 88. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:15; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0313] 89. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:16; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0314] 90. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:17; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0315] 91. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:18; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0316] 92. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:19; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0317] 93. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:20; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0318] 94. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:21; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0319] 95. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:22; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0320] 96. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:23; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0321] 97. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:24; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0322] 98. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:25; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0323] 99. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:26; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0324] 100. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:27; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0325] 101. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:28; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0326] 102. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:29; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0327] 103. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:30; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0328] 104. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:31; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33 over its entire length.

[0329] 105. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:1; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0330] 106. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:2; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0331] 107. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:3; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0332] 108. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:4; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0333] 109. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:5; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0334] 110. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:6; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0335] 111. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:7; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0336] 112. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:8; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0337] 113. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:9; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0338] 114. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:10; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0339] 115. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:11; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0340] 116. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:12; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0341] 117. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:13; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0342] 118. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:14; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0343] 119. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:15; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0344] 120. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:16; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0345] 121. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:17; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0346] 122. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:18; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0347] 123. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:19; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0348] 124. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:20; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0349] 125. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:21; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0350] 126. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:22; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0351] 127. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:23; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0352] 128. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:24; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0353] 129. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:25; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0354] 130. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:26; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0355] 131. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:27; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0356] 132. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:28; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0357] 133. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:29; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0358] 134. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:30; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0359] 135. A detergent and / or cleaning agent comprising: (A) at least one peptide having an amino acid sequence identical to that shown in SEQ ID NO:31; and (B) at least one lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0360] 136. The formulation according to any one of items 74 to 104, wherein the lipase has lipolytic activity and comprises an amino acid sequence that is 100% identical in its entire length to the amino acid sequence shown in SEQ ID NO:33.

[0361] 137. The formulation according to any one of items 105 to 135, wherein the lipase has lipolytic activity and comprises an amino acid sequence that is 100% identical in its entire length to the amino acid sequence shown in SEQ ID NO:34.

[0362] 138. The formulation according to any one of items 1 to 137, wherein the peptide binds to an oily surface or a surface coated with oil or having at least one oily and / or greasy stain, and said surface is preferably selected from hard surfaces, more preferably comprising or composed of ceramics (e.g., porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamel surfaces, wood, laminate, linoleum and mixtures thereof, especially preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, and / or textiles, more preferably comprising or composed of textiles of cotton, polyester, polyamide, polypropylene and mixtures thereof, especially preferably cotton, polyester and mixtures thereof, wherein said adhesion is determined as described in Example 2.

[0363] 139. The formulation according to any one of items 1 to 138, wherein the peptide is surface-active.

[0364] 140. The formulation according to any one of items 1 to 138, wherein the peptide is not surface-active.

[0365] 141. The formulation according to any one of items 1 to 139, wherein the peptide is surface-active, and wherein the surface activity is determined by the bubble pressure method as described herein.

[0366] 142. A formulation according to any one of items 1 to 138 or 140, wherein the peptide is not surface-active, and wherein the surface activity is determined by the bubble pressure method as described herein.

[0367] 143. The formulation according to any one of items 1 to 139 or 141, wherein the peptide is surface-active, and wherein the surface activity is determined as described in Example 4.

[0368] 144. The formulation according to any one of items 1 to 138, 140 or 142, wherein the peptide is not surface-active, and wherein the surface activity is determined as described in Example 4.

[0369] 145. The formulation according to any one of items 1 to 144, wherein the formulation is preferably selected from textile detergents, automatic dishwasher detergents, hand dishwashing detergents and hard surface cleaners.

[0370] 146. The formulation according to any one of items 1 to 144, wherein the formulation has at least two spatially separated compartments, wherein the peptide is contained in a first compartment and the at least one lipase is contained in a second compartment.

[0371] 147. The formulation according to any one of items 1 to 146, wherein the formulation has a pH in a 1 wt.% solution in deionized water at 20°C in the range of about 6 to about 11.5, preferably about 7 to about 11, more preferably about 7.5 to about 10.5, and particularly preferably about 8 to about 10.

[0372] 148. A method for cleaning textiles, particularly textiles containing or composed of cotton, polyester and mixtures thereof, and / or for cleaning hard surfaces, particularly tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, characterized in that a detergent or cleaning agent according to any one of items 1 to 147 is used in at least one method step.

[0373] 149. The method according to item 148, wherein in a first step, at least one peptide is brought into contact with the article to be washed or rinsed, and in a second step, at least one lipase is brought into contact with the article to be washed or rinsed.

[0374] 150. The method according to item 148 or 149, wherein the method is carried out in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, and very particularly preferably about 20°C.

[0375] 151. The formulation according to any one of items 1 to 147 is used for cleaning textiles, particularly textiles containing or composed of cotton, polyester and mixtures thereof, and / or for cleaning hard surfaces, particularly tableware (preferably made of ceramic such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass.

[0376] 152. The use of a peptide in a lipase-containing detergent and / or cleaning agent according to any one of items 1 to 147 for improving the cleaning performance of said formulation against at least one grease- and / or oil-containing stain, preferably an oil-containing stain, wherein said peptide is selected from... a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3 Selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or (b) A peptide having an amino acid sequence that is at least 80% and preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31.

[0377] 153. The use of a peptide in a lipase-containing detergent and / or cleaning agent according to any one of items 1 to 147 for improving the cleaning performance of the formulation against at least one grease- and / or oil-containing stain, preferably an oil-containing stain, wherein the peptide is selected from peptides comprising an amino acid sequence identical to one of the amino acid sequences listed in SEQ ID NOs: 1-31.

[0378] 154. Use of peptides in detergents and / or cleaning agents, preferably lipase-containing detergents and / or cleaning agents according to any one of items 1 to 147, as detergency, particularly degreasing and / or oil-removing active ingredients in formulations, wherein said peptides are selected from... a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3Selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or (b) A peptide having an amino acid sequence identity of at least 80%, and preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%, with respect to one of the amino acid sequences listed in SEQ ID NOs: 1-31.

[0379] 155. The use of a peptide in detergents and / or cleaning agents, preferably lipase-containing detergents and / or cleaning agents according to any one of items 1 to 147, as a detergency, particularly degreasing and / or oil-removing active ingredient in the formulation, wherein the peptide is selected from peptides comprising an amino acid sequence identical to one of the amino acid sequences listed in SEQ ID NOs: 1-31.

[0380] 156. The use according to any one of items 151 to 155, wherein the lipase is selected from: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in sequence over its entire length at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38, preferably 100%.

[0381] 157. The use according to any one of items 151 to 156, wherein the lipase is selected from lipases having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length, and in each case based on the numbering of SEQ ID NO: 33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) At at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T.

[0382] 158. The use according to any one of items 151 to 157, wherein the lipase is selected from: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO: 33 over its entire length; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:34 over its entire length.

[0383] 159. The use according to any one of items 151 to 158, wherein the lipase is selected from lipases having lipolytic activity and comprising an amino acid sequence having 100% identity with the amino acid sequence shown in SEQ ID NO:33 throughout its entire length.

[0384] 160. The use according to any one of items 151 to 158, wherein the lipase is selected from lipases having lipolytic activity and comprising an amino acid sequence having 100% identity with the amino acid sequence shown in SEQ ID NO:34 throughout its entire length.

[0385] 161. The use according to any one of items 151 to 160, wherein the temperature range is from about 10°C to about 80°C, preferably from about 15°C to about 60°C, more preferably from about 15°C to about 45°C, particularly preferably from about 20°C to about 30°C, and very particularly preferably from about 20°C.

[0386] Example Example 1: Peptide sequence The peptides in Table 2 are prepared by chemical synthesis.

[0387] Table 2: Peptide Names and Related Amino Acid Sequences

[0388] Example 2: Testing the adhesion of peptides to lipid substrates. In the first experiment, the adhesion of various peptides to oily stains on textiles was measured using the fluorescent amine method. Fluoroamine, a protein dye, is a fluorescent dye used to quantify trace amounts of proteins and peptides in solution. The fluorescent amine reagent reacts rapidly with primary amines.

[0389] The following pre-contaminated textile samples were used (from CFT, Center For Testmaterials): C-FF CS46, used frying oil, cotton (frying oil on the cotton). P-FF PS46, used frying oil, polyester (frying oil on polyester) CO2, olive oil with carbon black and thickener, cotton (olive oil on the cotton). PO PO2, olive oil with carbon black and thickener, polyester (olive oil on polyester) CS CS32, sebum and carbon black, cotton (sebum on cotton). PS PS32, sebum and carbon black, polyester (sebum on polyester) For the study, three textile samples (each approximately 10 mm in diameter) were placed twice into the wells of a 48-well microplate. 0.2 mL of peptide solution (0.02 mg / mL, dissolved in distilled water) was added to the wells of the first plate, and 0.2 mL of distilled water was added to the wells of the second plate. Wells without textile samples served as controls. The microplates were incubated at 20°C with gentle shaking (750 rpm, Titramax) for 1 hour. After incubation, 50 µL of the supernatant from each well was transferred to the wells of a black 96-well microplate. 17 µL of fluorescein solution (3 mg / mL, dissolved in DMSO; fluorescein, from AcrosOrganics) was added and mixed at 20°C for 15 minutes. The fluorescence of the samples in the 96-well plate was measured using a biophotometer (Ex 260 nm, Em 465 nm). Since the fluorescence response is linearly dependent on the peptide concentration, the percentage of peptide adhesion to the test material could be determined based on the final and initial fluorescence values.

[0390] The results are shown in Table 3. Higher values ​​indicate better adhesion of the peptide to the corresponding surface. Values ​​of 40% to 59% indicate moderate adhesion, 60% to 79% indicate good adhesion, and values ​​above 79% indicate very good adhesion. Values ​​with a difference ≥ 5% are considered significant.

[0391] Table 3: Adhesion Results

[0392] All peptides P1 to P31 exhibit good to very good adhesion to at least one grease- and / or oil-containing stain on polyester and / or cotton textiles. Peptide P32, which is not of this invention, did not exhibit adhesion to grease- and / or oil-containing stains.

[0393] Example 3: Determining the degreasing effect The degreasing effect was studied using a quartz crystal microbalance with dissipation monitoring (QCM-D). This surface-sensitive method allows for in-situ monitoring of the adsorption and desorption processes of materials or substances (and associated processes such as swelling) on ​​the sensor surface at nanogram resolution. The sensor used for this purpose consists of a thin quartz crystal disk surrounded by two metal electrodes (with thin gold layers on both sides). Due to the piezoelectric properties of quartz, it can be mechanically deformed when an external voltage is applied (depending on the crystal cut and the sign of the voltage). When an alternating voltage is applied, the quartz sensor begins to oscillate. At a specific frequency (resonant frequency f), the quartz sensor resonates. Since the resonant frequency depends on the thickness of the disk, measuring the change of the resonant frequency over time can infer the mass or layer thickness changes of the aforementioned process. In addition to the change in resonant frequency Δf, the change in dissipation ΔD (energy loss) is also measured. This parameter describes the energy loss of the oscillating system due to the viscoelastic properties of the adsorbed or desorbed material film. By simultaneously measuring Δf and ΔD, a viscoelastic model can be created. In the simple case, i.e., for a rigid, thin, uniformly distributed film firmly bonded to the surface of a quartz crystal, the mass change Δm resulting from the adsorption and desorption processes can be calculated solely from the frequency change Δf (Sauerbrey equation; see, for example, Snabe et al. (2003), Lag phase and hydrolysis mechanisms of triacylglycerol film lipolysis, Chemistry and Physics of Lipids, 125: 69-82; QSense analysis documentation and manufacturer instructions are available at: https: / / www.biolinscientific.com / qsense / instruments / qsense-pro#knowledge).

[0394] method: The quartz sensor preparation for the quartz crystal microbalance (QSense Analyzer, QSense Flow module QFM 401, ex. QSense®) was conducted by cleaning the quartz sensor at 75°C with a hydrogen peroxide-ammonia-Millipore aqueous solution (ratio 1:1:5), and then measuring the fundamental frequency and overtones or dissipation values ​​of the cleaned quartz sensor in air at 20°C (termination criterion: the frequency and dissipation values ​​remain constant over time; that is, the frequency and dissipation changes over time are recorded until the system stabilizes at a stable frequency and / or dissipation).

[0395] After cleaning, the quartz sensor was coated with a model grease solution (1% tridecylamine dissolved in toluene) by spin coating. Spin coating is a method known to those skilled in the art, allowing the application of very thin substrate layers with thicknesses of several nanometers or millimeters (see, for example, Olesen et al., Revealing Detergent Efficiency and Mechanism by Real-Time Measurement Using a Novel and Tailored QCM-D methodology, Tenside Surf. Det. 53 (2016) 5: 488-494). Subsequently, the fundamental and overtone frequencies or dissipations of the grease-coated quartz sensor were measured in air.

[0396] Subsequently, the measurement cell was first filled with Millipore water, and the fundamental and overtone frequencies or dissipations (baseline) of the grease-coated quartz sensor were measured in Millipore water at 20°C.

[0397] Then, the peptide solution (peptide P2) was introduced at a flow rate of 50 µl / min, and the fundamental or overtone frequency or dissipation of the grease-coated quartz sensor in the peptide solution was measured over time (stop criterion: the frequency or dissipation value remained constant over time).

[0398] The measurement cell was then briefly rinsed with Millipore water (50 µl / min). Lipase solution (Lipex Evity 200 L, from Novozymes) was then passed through at a flow rate of 50 µl / min, and the fundamental or overtone frequency or dissipation of the grease-coated quartz sensor in the peptide solution was measured over time (stop criterion: frequency or dissipation value remains constant over time).

[0399] To restore the sensor, the measurement cell was rinsed with a 2% aqueous surfactant solution after the measurement was completed.

[0400] Evaluate: The Sauerbrey equation can be used to determine the average amount of grease applied to the sensor based on the frequency difference between the coated and uncoated sensors, according to the QCM-D test results in air (the average value is taken for all oscillation modes, i.e., the average value of the fundamental frequency and each overtone).

[0401] (Sauerbrey equation) Δm: per cm 2 Quality changes Δf: Change in resonant frequency n: Number of oscillation modes (fundamental frequency or overtone) C: Mass sensitivity constant; Peptide P2 was used as an example peptide and tested at different concentrations. At a peptide concentration of 0.3 mg / L, the average mass / cm of the applied lipid layer was calculated according to the Sauerbrey equation. 2 2880 ng / cm 2 .

[0402] Based on the measured frequency values ​​over time, the reaction time for removing grease / coatings from the sensor can be determined. The reaction time is calculated as the difference between the time of maximum frequency change (when the peptide has completely bound to the grease layer) and the time when the frequency change begins after the addition of lipase (when the lipase releases the grease layer from the sensor).

[0403] The results are as follows Figure 1 As shown in Table 4.

[0404] Table 4: Degreasing reaction time

[0405] It can be seen that when using the combination of peptides and lipases according to the present invention, fats dissolve faster.

[0406] This effect also Figure 1 The diagram in the middle shows... Figure 1 An example of the time curve for the QCM-D measurement described above is shown.

[0407] The various method steps are marked below the X-axis ("Rinsing" = introducing Millipore water at a flow rate of 50 µl / min; "Peptide Adsorption" = introducing a peptide solution at a flow rate of 50 µl / min; "Oil Removal by Lipase" = introducing a lipase solution at a flow rate of 50 µl / min). Curves depicting the changes in resonant frequency and dissipation over time are plotted. The "Δf lipase" curve shows the resonant frequency change of the test device where only lipase acts on the oil on the sensor (comparative example). The "Δf lipase + peptide" curve shows the resonant frequency change of the test device where the peptide first adheres to the oil layer on the sensor, and then the lipase subsequently acts on it (an example according to the invention). The "ΔD lipase" or "ΔD lipase + peptide" curves show the dissipation changes of their respective test devices. Curves for test devices without peptides are plotted at a later time, as the peptide adhesion step is clearly missing here.

[0408] The change in frequency value (Δf) is explained as follows: A value of Δf < 0 indicates that the sensor becomes heavier, meaning that material is adsorbed onto it; in this case, peptides are adsorbed onto the lipid layer. The larger the value, the greater the mass of peptides bound to the lipid layer on the sensor.

[0409] A value of Δf > 0 means the sensor becomes lighter, i.e., material detaches from it, in this case, a layer of grease. The larger the value, the more fat mass detaches from the sensor.

[0410] A value of 0 means that the quality of the sensor does not change (in this case, the quality of a grease-coated sensor).

[0411] Initially, by adjusting the mass of the added adhesive peptide, the frequency (Δf) dropped below the baseline (Δf = 0), indicating that the peptide adhered to or adsorbed onto the grease applied to the sensor. In subsequent processes, even during rinsing with Millipore water, the frequency (Δf) remained stable for several hours, indicating that the peptide had stably adhered or adsorbed and was not washed away by the water.

[0412] After introducing the lipase solution, a strong frequency change (Δf) above the baseline was observed. This increase in frequency indicates that the lipid layer is being removed from the sensor.

[0413] After a certain period of time, the frequency change (Δf) remained stable, meaning that all the grease had been removed and there was no further deposition.

[0414] When comparing the curve "Δf lipase" and the curve "Δf lipase + peptide", it can be clearly seen that the curve "Δf lipase + peptide" shows a steeper curve, that is, the combination according to the present invention shows a faster oil removal effect than using lipase alone (comparative example).

[0415] The aforementioned QCM-D measurement also corresponds to phenomena observable to the naked eye. The presence of an grease layer can be identified before the coated quartz sensor comes into contact with the peptide and lipase, or with the lipase alone. After measurement, the grease layer is completely removed, and the gold layer of the sensor is visible again. This also demonstrates that the combination of peptide and lipase according to the present invention can remove grease and / or oily stains adhering to surfaces.

[0416] Example 4: Determining Surface Activity The dynamic surface tension of surfactants or molecules with surfactant-like properties in liquids was measured using a SITA science line t100 laboratory tensiometer (from SITA Messtechnik GmbH, Dresden). Dynamic surface tension provides information, in particular, about surfactant kinetics and is therefore a measure of the surface activity of surfactants and other molecules. In this example, dynamic surface tension was determined based on the bubble pressure method. For this purpose, a certain volumetric flow rate of air was introduced into the liquid to be tested through a capillary tube, generating bubbles within it. The dynamic surface tension could then be inferred from the pressure curve of bubble formation using the Young-Laplace equation.

[0417] First, the laboratory tensiometer Science Line T100 was calibrated using distilled water. Once a constant value of 72.7 mN / m was measured at different bubble lifetimes (72.7 mN / m corresponds to the reference value for water at 20°C, source: https: / / www.sita-messtechnik.de / wissen / oberflaechenspannung), measurements of the sample liquid could begin. To do this, the capillary was immersed in the sample liquid, and measurements were started at different bubble lifetimes. The following parameters varied in the sample liquid being measured: pH = 5.5 (aqueous solution) or 8.0 (10 mM TRIS-HCl buffer) c KCl = 0 mM; 5 mM; 50 mM c 肽 = 0-10 µM (P2, P4) T = 22 ℃ Figure 2 The dynamic surface tension curves for the control (TRIS (pH 8.0) + 50 mM KCl) and peptides P2 and P4 (10 µm each dissolved in TRIS (pH 8.0) + 50 mM KCl) are shown. Curves for other parameters are not shown here, but appear similar. It is clear that the dynamic surface tension remains constant throughout the bubble lifetime, indicating that peptides P2 and P4 are not surface-active.

[0418] Example 5: Exemplary Detergent and Cleaning Agent Formulations The combination of at least one peptide and at least one lipase according to the present invention can be used in various detergent and cleaning agent compositions and achieve their effects.

[0419] Table 5 Liquid Detergent Formulations

[0420] Table 6 Solid Detergents

[0421] Table 7 Dual-phase solid-state dishwasher detergents

[0422] Table 8 Solid Automatic Dishwasher Detergents

[0423] Table 9 Single-phase liquid detergents for automatic dishwashers

[0424] Table 10 Two-Phase Liquid Automatic Dishwasher Detergent with Compartments

[0425] A specific enzyme phase and a specific alkali phase are added at a 1:1 weight ratio, with a total weight of 30g, directly added from a double-chamber bottle into the feeding chamber of an automatic dishwasher.

[0426] Table 11 Multiphase liquid cleaning compound preparations (suitable for automatic dispensing, preferably for use in independent compartments of dishwashers)

[0427] Table 12 Hard Surface Cleaners

[0428] * pH = 10 was achieved by adding NaOH. Table 13 Handwashing Dishwashing Detergent

[0429] Table 14 Hard Surface Cleaners (Preferred for Glass Cleaning)

[0430] The composition also contains additional amine oxide and a fatty alcohol ethoxylate...

Claims

1. A detergent and / or cleaning agent, comprising (A) at least one peptide, wherein the peptide is selected from... a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or b) A peptide having an amino acid sequence identity of at least 80%, and preferably increasing to at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100%, with one of the amino acid sequences listed in SEQ ID NOs: 1-31; (B) At least one enzyme that has hydrolytic activity against ester bonds, preferably selected from lipases and esterases, especially esterases with lipolytic activity, and particularly preferably lipases.

2. The formulation according to claim 1, wherein in the peptide according to claim 1a), if o = 1, p = 0, 1 or 2, q = 2 and r = 4, then the sequence (X) 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s Equal to Z 1 Z 2 Z 3 [(Z 4 ) u Z 5 Z 6 ]3(Z 7 ) v , in Z 1 Defined as X in claim 1 2 And selected from R, H and K, with R preferred, Z 2 Z 3 Z 5 and Z 6 Defined as X in claim 1 4 And selected from A, L, and V, with A and L being preferred. Z 4 Defined as X in claim 1 3 And selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with F, R, E, A, Q, and W preferred. u is 1 or 2. Z 7 Defined as X in claim 1 5 And selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V. v is defined as s in claim 1 and is an integer from 0 to 4.

3. The formulation according to claim 1, wherein in the peptide according to claim 1a), if o = 1, p = 3-6, q = 1 or 2 and r = 2, then the sequence (X) 2 ) o [(X 3 ) p (X 4 ) q ] r Equal to Z 11 (Z 12 )6Z 13 Z 14 (Z 15 ) w Z 16 , in Z 11 Defined as X in claim 1 2 And selected from R, H and K, Z 12 Defined as X in claim 1 3 And selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, preferably A, N, C, Q, G, I, L, M, F, P, S, T, W, Y, and V, more preferably M, I, S, T, N, V, and F. Z 13 Z 14 Z 16 Defined as X in claim 1 4 And selected from A, L, and V, with A and L being preferred. Z 15 Defined as X in claim 1 3 And selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with R, K, E, S, Q, and N being preferred. w is an integer from 3 to 6.

4. The formulation according to any one of claims 1 to 3, wherein the peptide has an amino acid sequence that is 80% and preferably increasing at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% identical to one of the amino acid sequences listed in SEQ ID NOs: 1-32, preferably SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, and more preferably one of the amino acid sequences listed in SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29.

5. The formulation according to any one of claims 1 to 4, wherein the lipase is selected from: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO:

33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in sequence over its entire length at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38, preferably 100%.

6. The formulation according to any one of claims 1 to 5, wherein the peptide binds to an oily surface or an oil-coated surface or a surface having at least one oily and / or greasy stain, and the surface is preferably selected from hard surfaces, more preferably surfaces comprising or composed of ceramics (e.g., porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamel surfaces, wood, laminate, linoleum and mixtures thereof, especially preferably tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass, and / or textiles, more preferably textiles comprising or composed of cotton, polyester, polyamide, polypropylene and mixtures thereof, especially preferably cotton, polyester and mixtures thereof, wherein the adhesion is determined as described in Example 2.

7. The formulation according to any one of claims 1 to 6, wherein the formulation is preferably selected from textile detergents, automatic dishwasher detergents, hand dishwashing detergents, and hard surface cleaners.

8. The formulation according to any one of claims 1 to 7, wherein the formulation has at least two spatially separated compartments, wherein the peptide is contained in the first compartment, and the at least one enzyme having hydrolytic activity against ester bonds, preferably selected from lipases and esterases, particularly lipases having lipolytic activity, especially preferably lipases, is contained in the second compartment.

9. A method for cleaning textiles, particularly textiles containing or composed of cotton, polyester, and mixtures thereof, and / or for cleaning hard surfaces, especially tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., cutlery or pots) or glass, characterized in that... The detergent or cleaning agent according to any one of claims 1 to 8 is used in at least one method step.

10. The method according to claim 9, wherein in the first step, at least one peptide is contacted with the article to be washed or rinsed, and in the second step, at least one enzyme having hydrolytic activity against ester bonds, preferably selected from lipases and esterases, particularly esterases having fat-decomposing activity, especially lipases, is contacted with the article to be washed or rinsed.

11. The method according to claim 9 or 10, wherein the method is carried out in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, and very particularly preferably about 20°C.

12. The formulation according to any one of claims 1 to 8 is used for cleaning textiles, particularly textiles containing or composed of cotton, polyester and mixtures thereof, and / or for cleaning hard surfaces, particularly tableware (preferably made of ceramics such as porcelain or stoneware and plastic), metal (e.g., tableware or pots) or glass.

13. The use of a peptide in a lipase-containing detergent and / or cleaning agent according to any one of claims 1 to 8 for improving the cleaning performance of the detergent and / or cleaning agent against at least one grease-containing and / or oil-containing stain, preferably an oil-containing stain, wherein the peptide is selected from... a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3 selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or (b) A peptide having an amino acid sequence that is at least 80% and preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31.

14. Use of peptides in detergents and / or cleaning agents, preferably lipase-containing detergents and / or cleaning agents according to any one of claims 1 to 8, as a detergency, particularly degreasing and / or oil-removing active ingredient in formulations, wherein said peptides are selected from... a) A peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the amino acid sequence of the peptide has the following sequence in the N-to-C-terminal direction. (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t in X 1 The numerator is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y, and V, with G, I, S, and W being preferred, and G and I being even more preferred. X 2 Selected from R, H, and K, with R and K being preferred. X 3 selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 Selected from A, L, and V, with A and L preferred. X 5 Selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, and V, with A, R, E, and L preferred. m and t are each 0 or 1, where m + t = 0 or 1. n and o are each 0 or 1. p is an integer from 0 to 9. q is an integer between 0 and 2. r is an integer from 1 to 4. s is an integer from 0 to 4; and / or (b) A peptide having an amino acid sequence that is at least 80% and preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31.

15. The use according to any one of claims 13 to 14, wherein the lipase is selected from: (a) A lipase having lipolytic activity and comprising an amino acid sequence having at least 70% and preferably increasing at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity over its entire length with the amino acid sequence shown in SEQ ID NO: 33, and in each case based on the numbering of SEQ ID NO:

33. (i) At positions corresponding to positions 231 and 233, there are amino acid substitutions T231R and N233R, and (ii) Optionally, at at least one position corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255, and 256, there is at least one amino acid substitution selected from D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A, and P256T; and / or (b) A lipase having lipolytic activity and comprising an amino acid sequence, the amino acid sequence having at least 70% and increasing in sequence over its entire length at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%, preferably 100%, identity with the amino acid sequence shown in SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38, preferably 100%.

16. The use according to any one of claims 12 to 15, wherein the temperature range is from about 10°C to about 80°C, preferably from about 15°C to about 60°C, preferably from about 15°C to about 45°C, particularly preferably from about 20°C to about 30°C, and very particularly preferably from about 20°C.

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