Washing and cleaning agents with improved cleaning performance on greasy soils

Abstract

The invention relates to a washing and / or cleaning agent comprising at least one peptide, at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, more preferably lipase, and optionally at least one salt, wherein the peptide is suitable for adhesion to a surface containing fat and / or oil, or to a surface coated with fat and / or oil, or to a surface provided with at least one layer of fat and / or oil, wherein the surface consists of hard surfaces, more preferably surfaces containing or consisting of ceramic (e.g., porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum, and mixtures thereof, more preferably tableware (preferably made of ceramic such as porcelain or stoneware, as well as plastic), metal (e.g.,The invention relates to methods for cleaning hard surfaces and / or textiles, as well as the use of such peptides and agents for improving the cleaning performance on at least one type of greasy and / or oily soiling.

Description

[0001] The invention relates to a washing and / or cleaning agent comprising at least one peptide, at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, more preferably lipase, and optionally at least one salt, wherein the peptide is suitable for adhesion to a surface containing fat and / or oil, or to a surface coated with fat and / or oil, or to a surface provided with at least one layer of fat and / or oil, wherein the surface consists of hard surfaces, more preferably surfaces containing or consisting of ceramic (e.g., porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum, and mixtures thereof, more preferably tableware (preferably made of ceramic such as porcelain or stoneware, as well as plastic), metal (e.g.,The invention relates to methods for cleaning hard surfaces and / or textiles, as well as the use of such peptides and agents for improving the cleaning performance on at least one type of greasy and / or oily soiling.

[0002] Peptides that bind specifically to or interact with oxide surfaces such as metal surfaces, as well as peptides that bind specifically to plastic surfaces, have already been described (WO 2014 / 072313 A1, WO 2023 / 110572 A1). However, adhesive peptides are also of interest for many other surfaces, particularly for functionalizing such surfaces or imparting other desired properties.

[0003] It is known to use so-called "functional polymers" in detergents and / or cleaning agents, such as "soil release polymers" in detergents to improve the removal of dirt from textiles, or "soil repellent polymers" in detergents to prevent / reduce dirt adhesion to textiles. These soil release polymers (SRPs) are water-soluble or water-dispersible polycondensates based on dicarboxylic acids and diols or cellulose ethers. SRPs can positively influence the washability of oils and greases from textiles. Typical SRPs are based, for example, on copolymers of polyester and polyethers, including terephthalates, such as polypropylene terephthalate. However, these polymers are not biodegradable. Therefore, there is a need for alternative or improved, especially biodegradable, SRPs for use in detergents and / or cleaning agents, and / or alternatives to them.

[0004] Dispersing polymers, used in machine dishwashing detergents to prevent or reduce soil buildup, perform similar functions. These are typically (co-)polymeric polycarboxylates, such as poly(meth-)acrylates or polymers containing sulfonic acid groups based on (meth)acrylic acid. However, the biodegradability of such polymers is currently limited, so alternative, readily biodegradable alternatives are being sought for dishwashing applications.

[0005] Grease and / or oil stains on hard surfaces and / or textiles are among the most stubborn types of soiling and are not easily removed. Conventional washing and / or cleaning processes remove such stains by first liquefying the grease with the washing and / or cleaning temperature, usually between approximately 40°C and 60°C, and then loosening it from the surface with surfactants contained in the washing and / or cleaning agents (the "roll-up mechanism"). The detached, liquefied grease molecules are then carried away by mechanical forces during the washing and / or rinsing process. Additionally or alternatively, grease and / or oil stains can be removed by esterases, lipolytic enzymes, or lipases. In this process, the enzyme breaks down the grease and / or oils, and the resulting breakdown products are then washed away.However, the use of lipases after washing leaves an unpleasant odor on the washed items, especially textiles, because the lipase is adsorbed by the fabric and continues to hydrolyze fatty acid esters to low molecular weight fatty acids. These low molecular weight fatty acids are then perceived due to their unpleasant odor. The intensity of the odor can vary depending on the nature of the textile. Therefore, there is currently no satisfactory alternative for removing grease and / or oil stains at low temperatures, i.e., below 40°C, particularly around 20°C or 30°C, because fats do not liquefy, or only insufficiently liquefy, at temperatures below approximately 30°C or 40°C.

[0006] The inventors have discovered and developed special peptides that are surprisingly suitable for adhesion to greasy and / or oily surfaces, as described herein, enabling the removal of at least one greasy and / or oily soiling from surfaces and thus improving the cleaning performance of washing and / or cleaning agents containing them on at least one greasy and / or oily soiling. Furthermore, the inventors have found that, in particular, the combination of a lipase and at least one peptide according to the invention leads to improved removal of at least one greasy and / or oily soiling from a surface. The inventors have also found that, in particular, the combination of a lipase and at least one peptide according to the invention, in the presence of a salt, leads to improved removal of at least one greasy and / or oily soiling from a surface.

[0007] Within the scope of the present invention, "fatty and / or oily surface" is understood to mean a surface that contains or consists of fats and / or oils, and / or a surface that is coated with fats and / or oils, and / or a surface that is contaminated with at least one fatty and / or oily deposit. Within the scope of the present invention, "fat" or "fats" are understood to mean macromolecules formed from glycerol and fatty acids, in addition to mono- and diglycerides, in particular the so-called triacylglycerols or triglycerides in which three fatty acids are bonded to the glycerol. According to the invention, all known fatty acids with 8 to 36, preferably 10 to 24, carbon atoms, both mono- and polyunsaturated and saturated fatty acids, are further included. Within the scope of the present invention, "oil" or "oils" are understood to mean liquid or non-liquid substances at room temperature.The term "fatty and / or oily soiling" refers to free-flowing, fat-like substances that do not mix with water. The invention encompasses both synthetic and bio-based fats and / or oils. Within the scope of the present invention, "fatty and / or oily soiling" refers to soiling on a surface, particularly a hard surface and / or textile surface, that contains or consists of a fat and / or oil. Examples of typical fatty and / or oily soiling include food and food residue soiling, such as vegetable fats (e.g., coconut oil), animal fats (e.g., butter, clarified butter), cooking oils (e.g., olive oil, sunflower oil, rapeseed oil), frying fat, mayonnaise, margarine, deep fryer fat, meat fat (e.g., beef tallow, pork fat, lard), including burnt-on food residue, and / or synthetic fats and / or oils, such as...Mineral oil(s) and / or greases, motor oil, bicycle chain oil, pigmented fats, pigmented oils, and / or fats and / or oils from personal care products, such as lipstick, make-up, lotion, cream, and / or body oil deposits, such as sebum. In preferred embodiments, the greasy surface contains or consists of a grease that is solid at room temperature. In preferred embodiments, the grease-coated surface is coated with a grease that is solid at room temperature. In preferred embodiments, the surface provided with at least one greasy contaminant is provided with or contaminated with at least one solid grease; that is, preferably, the at least one greasy contaminant contains or consists of a grease that is solid at room temperature.

[0008] Within the scope of the present invention, the surface containing grease and / or oil and / or the surface coated with grease and / or oil and / or the surface provided with at least one greasy and / or oily soiling is preferably selected from hard surfaces and / or textiles.

[0009] Preferably, the surface containing grease and / or oil and / or the surface coated with grease and / or oil and / or the surface provided with at least one greasy and / or oily soiling is a hard surface containing or consisting of ceramic (e.g. porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, lacquered and enamelled surface, wood, laminate, linoleum and mixtures thereof, especially preferably tableware (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0010] Preferably, a surface containing grease and / or oil, or a surface coated with grease and / or oil, or a surface bearing at least one greasy and / or oily soiling, is a textile surface. The term "textile surface," as used herein, is synonymous with the term "textile" or "textiles." The term "textile" or "textiles," as used herein, refers to 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., garments and other articles). The textile or fabric may be in the form of knitted fabrics, woven fabrics, denim, nonwovens, felts, yarns, and terry cloth. The textile may be cellulose-based, such as...Natural cellulose fibers such as cotton, flax / linen, jute, ramie, sisal, or coconut fibers, or artificially produced cellulose fibers (e.g., from wood pulp) such as viscose / rayon, cellulose acetate fibers (Tricell), lyocell, or mixtures thereof. The textile or fabric may also consist of non-cellulose fibers, e.g., natural polyamides such as wool, camel, cashmere, mohair, rabbit, and silk, or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene, and spandex / elastane, or mixtures thereof, as well as mixtures of cellulose and non-cellulose fibers. Examples of blends include blends of cotton and / or rayon / viscose 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, ramie, flax / linen, jute, cellulose acetate fibers, lyocell).The fabric can be conventional washable laundry, e.g., soiled household linen. When the terms "fabric" or "garment" are used, they should also encompass the broader term "textiles." Preferably, textiles containing or consisting of cotton, polyester, polyamide, polypropylene, and mixtures thereof are preferred; cotton, polyester, or mixtures thereof are particularly preferred.

[0011] The invention particularly preferably relates to hard surfaces and / or textiles that are provided with at least one greasy and / or oily soiling, i.e., are grease-stained, wherein the hard surfaces are preferably selected from dishes (preferably ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, and the textiles contain or consist of cotton, polyester and mixtures thereof.

[0012] Through the adhesion of substrate-specific peptides to fatty and / or oily surfaces, in particular fatty surfaces as defined herein, i.e., in particular to at least one fatty and / or oily soiling on a surface (as described herein), preferably selected from hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, and textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, functional groups can be selectively bound to the fatty and / or oil molecules on the surface. This can result in substrate-specific removal of the fatty and / or oily soiling.Peptides according to the invention, which bind specifically to fats and / or oils, preferably solid fats, or to greasy and / or oily soiling, preferably greasy soiling, on surfaces, can thus be used to selectively remove these fats and / or oils, in particular solid fats, from the surface.

[0013] In particularly preferred embodiments, the peptides according to the invention enable the improvement of the cleaning performance of washing and / or cleaning agents on at least one greasy and / or oily soiling of a surface, wherein the surface is selected from hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, in particular containing or consisting of cotton, polyester and mixtures thereof.

[0014] The invention therefore relates in a first aspect to a washing and / or cleaning agent comprising (A) at least one peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5, and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably from -1.5 to +1.5, particularly preferably from -1.1 to +1.1, and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably from -2.0 to +2.0, particularly preferably from -1.8 to +1.0; and (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably of 7.0 to 11.0, more preferably of 7.5 to 10.5, and particularly preferably of 8.0 to 10.0.

[0015] In preferred embodiments, the peptide in the composition according to the invention has an amino acid sequence that is 80% and increasingly 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% identical to one of the amino acid sequences listed in SEQ ID NOs: 1-31, 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 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, especially preferred SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0016] In preferred embodiments, the at least one enzyme exhibiting hydrolytic activity on an ester bond is a lipase, wherein the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:32, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical.

[0017] In preferred embodiments, the at least one salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts, and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0018] Particularly preferred is the at least one salt selected from alkali metal salts with an inorganic counterion; alkali metal halides are especially preferred, in particular those selected from lithium chloride, sodium chloride, potassium chloride and mixtures thereof.

[0019] In preferred embodiments, the peptide binds to a fatty surface, a surface coated with grease, or a surface contaminated with at least one fatty and / or oily substance, wherein the surface is preferably selected from hard surfaces, more preferably containing or consisting of ceramic (e.g., porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum, and mixtures thereof, particularly preferably tableware (preferably made of ceramic such as porcelain or stoneware, as well as plastic), metal (e.g., cutlery or pots), or glass, and / or textiles, more preferably containing or consisting of cotton, polyester, polyamide, polypropylene, and mixtures thereof, particularly preferably cotton, polyester, and mixtures thereof, wherein the adhesion is determined as described in Example 2.

[0020] In further aspects, the invention relates to preferred embodiments of the aforementioned means as described herein.

[0021] Further aspects of the invention relate to • Method for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, wherein in at least one process step a washing and / or cleaning agent as described herein is used; • Method for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, wherein in a first step the at least one peptide is brought into contact with the items to be washed or rinsed and in a second step the at least one lipase is brought into contact with the items to be washed or rinsed; • A method for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, wherein it is carried out in a temperature range of about 10°C to about 60°C, preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C; • Use of any agent described herein for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass; • Use of a peptide described herein in a washing and / or cleaning agent to improve the cleaning performance of the washing and / or cleaning agent on at least one greasy and / or oily soiling, preferably greasy soiling; • Use of a peptide described herein in a washing and / or cleaning agent as a dirt-removing, in particular grease- and / or oil-removing, active ingredient in a washing or cleaning agent; • Use in a temperature range of about 10°C to about 60°C, preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0022] These and other aspects, features, and advantages of the invention will become apparent to the person skilled in the art upon studying the following detailed description and claims. Each feature from one aspect of the invention can be incorporated into any other aspect of the invention. Furthermore, it is understood that the examples contained herein are intended to describe and illustrate the invention, but do not limit it, and in particular, the invention is not limited to these examples.

[0023] Unless otherwise stated, all percentages are weight percent (wt%), based on the total weight of the respective composition or agent.

[0024] Numeric ranges specified in the format "from x to y" include the stated values. If multiple preferred numeric ranges are specified in this format, it is understood that all ranges resulting from the combination of the different endpoints are also included.

[0025] "At least one," as used herein, means one or more, i.e., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or more. When referring to an ingredient, the statement refers to the type of ingredient and not the absolute number of molecules. Thus, "at least one peptide," for example, means at least one type of peptide, i.e., it may refer to one type of peptide or a mixture of several different peptides. When used with weight specifications, the statement refers to all compounds of the specified type contained in a product, i.e., the product typically does not contain any further compounds of that type beyond the specified amount of the relevant compounds.

[0026] “Approximately” or “about”, as used herein in reference to numerical values, means the corresponding value ±10%, preferably ±5%.

[0027] The term “washing and cleaning agent” or “washing or cleaning agent”, as used herein, is synonymous with the term “agent” and refers to a composition for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, as explained in the description.

[0028] Unless explicitly stated otherwise, the term "room temperature" within the scope of the invention is understood to mean 20°C at 1013 mbar.

[0029] "Liquid," as used herein, includes liquids and gels as well as pasty compositions. It is preferred that the liquid compositions are free-flowing and pourable at room temperature, but it is also possible that they exhibit a yield point.

[0030] A substance, e.g. a composition or a means, is, according to the definition of the invention, solid if it is in the solid state of matter at 20°C and 1,013 mbar.

[0031] A substance, e.g., a composition or an agent, is liquid according to the definition of the invention if it exists in the liquid state at 20°C and 1,013 mbar. Liquid also includes gel-like states.

[0032] In the context of the present invention, the term “N-terminus” or “N-terminal” typically describes the end of the amino acid chain of a peptide which has a free amino group.

[0033] In the context of the present invention, the term “C-terminus” or “C-terminal” typically describes the end of the amino acid chain of a peptide which has a free carboxyl group.

[0034] In the context of this invention, the expression “in N- to C-terminal orientation” refers to an amino acid sequence in which the order of the amino acids is described starting from the N-terminus and moving towards the C-terminus.

[0035] When reference is made herein to various interconnected or individual amino acid sequences, these are always shown in an N- to C-terminal orientation, unless otherwise stated. Furthermore, the individual amino acids or amino acid sequences are linked to each other via peptide bonds, unless otherwise stated.

[0036] In the context of this invention, "adhesion" or "adhesive" refers to an interaction between a peptide and a surface, enabling the peptide to adhere to the surface. Thus, the term "adhesion-mediating" denotes the ability, under suitable conditions (i.e., typically non-denaturing conditions), to interact with and / or adhere to various surfaces, such as textile surfaces, particularly those containing or consisting of cotton, polyester, and mixtures thereof, or hard surfaces, such as, in particular, tableware (preferably ceramic such as porcelain or stoneware, as well as plastic), metal (e.g., cutlery or pots), or glass. "Fat-binding peptides," as used herein, means that the peptide binds to fat, for example, to at least one fatty and / or oily contaminant on a surface.In preferred embodiments, the binding affinity is greater than that of a reference sequence or reference molecule that does not possess adhesion-promoting properties. The fat-binding peptides described herein preferably exhibit 10-fold, and more preferably 20-fold, 50-fold, or 100-fold higher adhesion to a given surface than a reference molecule (peptide according to SEQ ID NO:32). In the context of this invention, the term "binding" preferably refers to "covalent bonds" between the peptide and a surface.A peptide is, in particular, a fat-binding peptide within the meaning of the invention if, in a method according to Example 2, the ability of the peptide to adhere to a fat- and / or oil-containing surface and / or to a surface coated with fat and / or oil and / or to at least one fat- and / or oil-containing contaminant on a surface is demonstrated, wherein the binding affinity is greater than that of a reference molecule (peptide according to SEQ ID NO:32).

[0037] The present invention is based on the inventors' surprising discovery that specific peptides, as described herein, bind to surfaces containing grease and / or oil, enabling the removal of at least one greasy and / or oily soiling from surfaces and thus improving the cleaning performance of the washing and / or cleaning agents they contain on at least one greasy and / or oily soiling. Furthermore, the inventors found that, in particular, the combination of an enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, especially esterase with lipolytic activity, and particularly preferably lipase, and the peptide according to the invention leads to improved removal of at least one greasy and / or oily soiling from a surface.This is surprising insofar as it has not previously been described that peptides according to the invention can remove greasy and / or oily soiling from a surface, i.e., exhibit cleaning performance on at least one greasy and / or oily soiling, nor that peptides according to the invention can improve the cleaning performance of an enzyme that has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipases. Furthermore, it was surprisingly found that the presence of at least one salt further enhances the cleaning performance of the combination of peptide and lipase.

[0038] The invention therefore relates in a first aspect to a washing and / or cleaning agent comprising (A) at least one peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt.% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, more preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0.

[0039] In a second aspect, the invention relates to a washing 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 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably from -1.5 to +1.5, particularly preferably from -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably from -2.0 to +2.0, particularly preferably from -1.8 to +1.0; and / or b) 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 peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r ( X 5) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence that has at least 80% and increasingly 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; (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably of 7.0 to 11.0, more preferably of 7.5 to 10.5, and particularly preferably of 8.0 to 10.0.

[0040] The peptide definitions a), b) and c) are to be understood as alternative or complementary.

[0041] In the context of the present invention, a "peptide" is understood to be a preferably linear polymer composed of amino acids, preferably the 20 proteinogenic L-amino acids, comprising up to 100 amino acids linked together by peptide bonds. According to the invention, the peptides have an amino acid sequence of 4 to 50 amino acids. In the context of this invention, the amino acids are indicated by a single-letter code, e.g., "C" in the sequence (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t for a cysteine ​​residue. It is further clear that, unless otherwise stated, the amino acids in any amino acid sequence disclosed herein are linked by peptide bonds and, unless otherwise stated, the sequence is listed in an N- to C-terminal orientation. Table 1: Proteinogenic amino acids Single-letter code Three-letter code amino acid A Ala Alanine R Arg Arginine N Asn Asparagin D Asp Aspartic acid C Cys Cysteine Q Gln Glutamine E Glu Glutamic acid G Gly Glycine H His Histidine I Island Isoleucine L Leu Leucin K Lys Lysine M Met Methionine F Phe Phenylalanine P Per Proline S Ser Serine T Thr Threonine W Trp Tryptophan Y type Tyrosine V Val Valin

[0042] 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 typically uncharged, i.e., neutral amino acids. When reference is made herein to an “arbitrary” amino acid, this usually refers to any of the 20 naturally occurring proteinogenic amino acids (Table 1).

[0043] Unless otherwise specified, the amino acids are typically L-amino acids. In alternative embodiments, the peptide may also consist of D-amino acids, although it may be preferred that D- and L-amino acids do not occur simultaneously within the peptides described herein. In various embodiments, such an arbitrary amino acid encompasses all of the aforementioned amino acids.

[0044] In various embodiments, the peptide has a theoretically calculable total charge (hereinafter referred to as total charge) from 0 to +12, e.g., 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 amino acids in the peptide that, in addition to the C- or N-terminus, can form a negative or positive charge in a side chain, in particular R, K, H, D, and E, and results from the sum of these (theoretically possible) negative and positive charges, whereby one (theoretically possible) positive charge and one negative charge cancel each other out. A peptide with two R residues and one E residue would thus have a total charge of +1. In preferred embodiments, the total charge of the peptide is 0 to +4.

[0045] In various embodiments, the peptide exhibits (a1) has a total charge of 0 to +4, or (a2) if r ≥ 4, has a total charge of 0 to +4, or (a3) if r < 4 has a total charge of +1 to +4, preferably +2 or +3.

[0046] In various embodiments (b) the N-terminus comprising the first 1-5 amino acids carries a net positive charge; and / or (c1) the C-terminus comprising the last 1-5 amino acids has a net negative charge such that the net charge of the first 1-5 amino acids at the N-terminus and the last 1-5 amino acids at the C-terminus together is greater than or equal to 0, preferably greater than 0, or (c2) the C-terminus comprising the last 1-5 amino acids has a neutral net charge such that the net charge of the first 1-5 amino acids at the N-terminus and the last 1-5 amino acids at the C-terminus together is greater than 0, preferably greater than 1, or (c3) the C-terminus comprising the last 1-5 amino acids has a net positive charge such that the net charge of the first 1-5 amino acids at the N-terminus and the last 1-5 amino acids at the C-terminus together is greater than 0, preferably greater than 1.

[0047] All of the aforementioned characteristics can be realized individually or in any combination.

[0048] The feature that the peptide has a net positive charge at the N-terminus comprising the first 1-5 amino acids means that the N-terminal 1-5 amino acids contain more positively charged than negatively charged amino acids. In various embodiments, this feature is fulfilled, for example, when the N-terminal 1-5 amino acids contain one or two positively charged amino acids, i.e., H, K, or R, preferably K or R, even more preferably R, and no negatively charged amino acids, such as E or D. If the N-terminus contains a negatively charged amino acid, the number of positively charged amino acids must be at least two for the net charge to remain positive.

[0049] The feature that the peptide has a net negative charge at the C-terminus comprising 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 (D and E) must be greater than the number of positively charged amino acids. In various embodiments, this feature is fulfilled, for example, when the C-terminal 1-5 amino acids (i.e., within the last 5 amino acids at the C-terminus) contain 1 or 2 negatively charged amino acids (D or E) and no positively charged amino acids (H, K, or R). An example of such a C-terminal sequence would be EAL or a double sequence of this motif.

[0050] The characteristic that the peptide has a neutral net charge at the "C-terminus comprising the last 1-5 amino acids" means that the number of charged amino acids must be 0 or the number of negatively and positively charged amino acids must be equal.

[0051] The isoelectric point (IEP, pH) i or pl) is the pH value at which the number of positive and negative charges of an amphoteric molecule, in this case the peptide, is exactly equal on average. At this pH value (in an aqueous solution), the respective peptide is externally neutral, i.e., isoelectric.

[0052] The peptides according to the invention have an isoelectric point in the range of 5.0 to 15.0. Preferred peptides have an isoelectric point of 6.0 to 13.0, particularly preferably of 6.5 to 12.0. This has the advantage that the adhesion of the peptides to the fatty surface is particularly stable and the interaction of the peptides with the lipases is also improved.

[0053] A peptide is preferred which has an isoelectric point in the range of 5.0 to 15.0 and is selected from the peptides according to SEQ ID NO: 1 to 31. Preferred peptides have an isoelectric point of 6.0 to 13.0, particularly preferably of 6.5 to 12.0.

[0054] If the pH of the aqueous solution containing the peptide is above its isoelectric point, the peptide has a negative charge. If the pH of the aqueous solution containing the peptide is below its isoelectric point, the peptide has a positive charge.

[0055] In addition to the aforementioned total charge, which results from the theoretical calculation of the sum of the negative and positive amino acids (i.e., the sum of amino acids that can form a negative or positive charge in a side chain in addition to the C- or N-terminus), whereby one positive and one negative charge cancel each other out, there is also the pH-dependent charge value of a peptide.

[0056] This pH-dependent charge value of the peptide is determined by the actual pKa values ​​of the amino acid residues, which can form a negative or positive charge.

[0057] In a further embodiment of the present invention, the peptide according to the invention therefore has a charge value at pH 8 of -3 to +3. A peptide having a charge value at pH 8 of -3 to +3 and selected from the peptides according to SEQ ID NO: 1 to 31 is preferred. A particularly preferred peptide has a charge value at pH 8 of -1.0 to +2.0. A most particularly preferred peptide has a charge value at pH 8 of -1.0 to +2.0 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30.

[0058] According to a particularly preferred embodiment, the peptide has a charge value of -0.75 to +1.5 at pH 8. Most preferably, the peptide has a charge value of -0.75 to +1.5 at pH 8 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30.

[0059] Furthermore, an embodiment of the present invention is characterized in that the peptide according to the invention has a charge value of -3.0 to +3.0 at pH 9. A peptide having a charge value of -3 to +3 at pH 9 and selected from the peptides according to SEQ ID NO: 1 to 31 is preferred. A particularly preferred peptide has a charge value of -1.5 to +1.5 at pH 9. It is most preferred if the peptide has a charge value of -1.5 to +1.5 at pH 9 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30.

[0060] According to a particularly preferred embodiment, a peptide is particularly preferred which has a charge value of -1.1 to +1.1 at pH 9. Most preferably, the peptide has a charge value of -1.1 to +1.1 at pH 9 and is selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30.

[0061] In a further embodiment of the present invention, the peptides according to the invention have a charge value at pH 10 of -3 to +3. A peptide having a charge value at pH 10 of -3 to +3 and selected from the peptides according to SEQ ID NO: 1 to 31 is preferred. Particularly preferred peptides have a charge value at pH 10 of -2.0 to +2.0. Most preferred is a peptide having a charge value at pH 10 of -2.0 to +2.0 and selected from the peptides according to SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30.

[0062] Peptides exhibiting a charge value of -1.8 to +1.0 at pH 10 are particularly preferred. A peptide with a charge value of -1.8 to +1.0 at pH 10 selected from the peptides listed under SEQ ID NO: 1, 2, 3, 4, 6, 7, 8, 9, 10, 11, 12, 13, 14, 17, 22, 25, 27, 29, 30 is especially preferred.

[0063] Particularly preferred peptides have a) an isoelectric point of 6.0 to 13.0, particularly preferably 6.5 to 12.0, and b) a charge value of -1.0 to +2.0 at pH 8 and / or a charge value of -1.5 to +1.5 at pH 9 and / or a charge value of -2.0 to +2.0 at pH 10. Most particularly preferred peptides have a) an isoelectric point of 6.5 to 12.0 and b) a charge value of -0.75 to +1.5 at pH 8 and / or a charge value of -1.5 to +1.5 at pH 9 and / or a charge value of -1.8 to +1.0 at pH 10.

[0064] The isoelectric point and charge values ​​can be calculated using the Henderson-Hasselbalch equation, as described in Kozlowski, LP, “IPC - Isoelectric Point Calculator”. Biol Direct 11, 55 (2016), https: / / doi.org / 10.1186 / s13062-016-0159-9. The pKa values ​​used in the calculation were disclosed in Grimsley GR, Scholtz JM, Pace CN. “A summary of the measured pK values ​​of the ionizable groups in folded proteins”. Protein Sci. 2009 Jan;18(1):247-51. doi: 10.1002 / pro.19. PMID: 19177368; PMCID: PMC2708032.

[0065] The isoelectric points and charge values ​​at pH 8.0, pH 9.0 and pH 10.0 resulting from these calculations for the peptides explicitly disclosed herein are given in Table 2.

[0066] In various embodiments, the peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence. (C) m (X 1 ) n (X2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4.

[0067] In various embodiments, in a peptide, when o = 1, p = 0, 1 or 2, q = 2 and r = 4, the sequence (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s equal Z 1 Z 2 Z 3 [(Z 4 ) u Z 5 Z 6 ]3(Z 7 ) v , where Z 1 like X 2 The above is defined and selected from R, H and K, preferably R. Z 2 , Z 3 , Z 5 and Z 6 like X 4 The above defined and selected are from A, L and V, preferably A and L. Z 4 like X 3 The above is defined 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 F, R, E, A, Q and W. u 1 or 2 is, Z 7 like X 5 The above is defined 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 above and is an integer from 0 to 4. In various embodiments (i) if u = 1, Z 4 selected from R, E and Q, or (ii) if u = 2, (Z 4 )2 selected from FR, FE, AR, WE, WR and AQ. In various embodiments, the peptide comprises (i) at least one motif selected from RAL and RLA, preferably RAL, wherein this sequence is preferably located in the N-terminal amino acids at positions 1-3; and / or (ii) at least one motif selected from EAL and ELA, preferably EAL, wherein this motif is preferably not located in the N-terminal amino acids of positions 1-4; and / or (iii) at least one motif selected from QAL and QLA, preferably QAL; and / or (iv) the RAL motif and at least one of QAL or EAL, preferably both; and / or (v) at least one, preferably two or three, RAL motif(s); and / or (vi) the motif RAL at least twice and at least one of QAL or EAL, preferably both.

[0068] 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 exhibits a net positive charge, but also comprises amino acids with a particularly high α-helix-forming potential. In various embodiments, the R residue can also be replaced by K; however, the N-terminal R residue is particularly preferred.

[0069] In various embodiments, the peptide comprises amino acids with a high α-helix-forming potential, wherein these amino acids are selected from E, A, L, M, Q, K, R, F, I, H, Wund D, more preferably E, A, L, M, Q, K, R, F, I and H, more preferably E, A, L, M, Q, K, R and H.

[0070] In various embodiments, the peptide consists of at least 50% and increasingly preferably 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 a high α-helix-forming potential, wherein these amino acids are preferably selected from E, A, L, M, Q, K, R, F, I, H, W and D, further preferably E, A, L, M, Q, K, R, F, I and H, particularly preferably E, A, L, M, Q, K, R and H.

[0071] In various forms, the peptide forms a helical secondary structure, in particular an α-helix structure with an α-helix content of preferably at least 70% and increasingly 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% or 99%. The use of the motif AL or LA in the amino acid sequence of the peptide according to the invention can contribute to the stability of the helical structure because these amino acids have a high α-helix potential.

[0072] In various embodiments, in a peptide, when o = 1, p = 3-6, q = 1 or 2 and r = 2, the sequence (X 2 ) o [(X 3 ) p (X 4 ) q ] r equal Z 11 (Z 12 )6Z 13 Z 14 (Z 15 ) w Z 16 , where Z 11 like X 2The above is defined and selected from R, H and K. Z 12 like X 3 The above is defined 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 like X 4 The above defined and selected are from A, L and V, with A and L being preferred. Z 15 like X 3 The above is defined 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 R, K, E, S, Q and N. w is an integer from 3 to 6.

[0073] In various embodiments, a peptide (i) is Z 13 Z 14 selected from AL and LA, preferably AL; and / or (ii) includes (Z 15 ) wwith w = 3-6 a sequence that includes at least one positively charged amino acid (R, H or K); and / or (iii) includes (Z 15 ) w with w = 3-6 a motif selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, further preferably RQN; and / or (iv) is Z 16 selected from A and L, preferably A.

[0074] In various embodiments, the peptide can have a high proportion of hydrophobic amino acids selected from A, L, F, W, V, M, I and P, in particular A, L, F, W, V, M and I.

[0075] In various embodiments, the peptide has an amino acid sequence that is 10 to 24 amino acids in length, e.g. 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular 12 to 18 amino acids.

[0076] In various embodiments, the peptide has the amino acid cysteine ​​(C) at its C-terminus. In other embodiments, the peptide has the amino acid cysteine ​​at its N-terminus. This amino acid, via its free sulfhydryl group, can enable coupling to other molecules, structures, or substrates. This amino acid therefore serves as a linkage site but is typically not involved in the desired adhesive effect.

[0077] In preferred embodiments, the peptide has an amino acid sequence that has at least 80% and increasingly 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.

[0078] In preferred embodiments, 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).

[0079] In preferred embodiments, the peptide has a sequence that is represented in SEQ ID NO: 1-31, particularly preferably SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29, most preferably SEQ ID NO: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0080] In preferred embodiments, the peptide has an amino acid sequence of 10 to 24 amino acids, e.g. 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular 10 to 18 amino acids, and has an isoelectric point of 5.0 to 15, preferably 6.0 to 13.0, in particular preferably 6.5 to 12.0, and / or a charge value at pH 8 of -3.0 to +3.0, preferably -1.0 to +2.0, in particular preferably -0.75 to +1.5; and / or a charge value at pH 9 from -3.0 to +3.0, preferably from -1.5 to +1.5, particularly preferably from -1.1 to +1.1 and / or a charge value at pH 10 from -3.0 to +3.0, preferably from -2.0 to +2.0, particularly preferably from -1.8 to +1.0.

[0081] In preferred embodiments, the peptide has an amino acid sequence that has at least 80% and increasingly 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, and has an isoelectric point of 5.0 to 15, preferably 6.0 to 13.0, particularly preferably 6.5 to 12.0, and / or a charge value at pH 8 of -3.0 to +3.0, preferably -1.0 to +2.0, particularly preferably -0.75 to +1.5; and / or a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0.

[0082] In preferred embodiments, the peptide has an amino acid sequence that is 10 to 24 amino acids in length, e.g.11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular 12 to 18 amino acids, wherein the amino acid sequence has at least 80% and increasingly 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 mentioned in SEQ ID NOs: 1-31, and has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably 6.5 to 12.0, and / or a charge value at pH 8 of -3.0 to +3.0, preferably -1.0 to +2.0, particularly preferably -0.75 to +1.5; and / or a charge value at pH 9 of -3.0 to +3.0, preferably -1.5 to +1.5, particularly preferably -1.1 to +1.1 and / or a charge value at pH 10 of -3.0 to +3.0, preferably -2.0 to +2.0, particularly preferably -1.8 to +1.0.

[0083] Preferred peptides according to the invention bind to a surface containing fat and / or oil and / or to a surface coated with fat and / or oil and / or to a surface provided with at least one layer of fat and / or oil, wherein the surface is preferably made of hard surfaces, more preferably surfaces containing or consisting of ceramic (e.g. porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably tableware (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, i.e. the peptides have the ability under suitable conditions, i.e.Peptides that typically adhere to surfaces under non-denaturing conditions exhibit adhesive properties. Such adhesion / binding of the peptide can occur directly via the terminal N- or C-terminal group. Alternatively or additionally, such adhesion / binding of the peptide can also occur via further functional groups bound at the N- and / or C-terminal level. Furthermore, the peptide can be stably associated at the N- and / or C-terminal level and / or via suitable side chains, covalently and / or via similar suitable binding mechanisms, under the desired application conditions, with a carrier substance, in particular a fatty and / or oily surface and / or a surface coated with fatty and / or oil and / or a surface contaminated with at least one fatty and / or oily deposit, as described herein.

[0084] Preferred peptides according to the invention bind to fatty and / or oily surfaces, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass. Preferred peptides according to the invention bind to fatty surfaces, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0085] Preferred peptides according to the invention bind to surfaces coated with fat and / or oil, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass. Preferred peptides according to the invention bind to surfaces coated with fat, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably tableware (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0086] Preferred peptides according to the invention bind to at least one fatty and / or oily soiling on a surface, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass. Preferred peptides according to the invention bind to at least one fatty soiling on a surface, in particular textiles, preferably containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0087] In particularly preferred embodiments, the peptides according to the invention bind to at least one fatty and / or oily, preferably fatty, soiling on textiles. In particularly preferred embodiments, the peptides according to the invention bind to at least one fatty and / or oily, preferably fatty, soiling on textiles, wherein the textile contains or consists of cotton, polyester, or mixtures thereof.

[0088] Good adhesion to textile surfaces, especially textile surfaces made of synthetic fibers, such as polyester-containing textiles, can be achieved, for example, by a peptide with a pronounced helical structure (especially α-helix structure) and / or a high arginine content, especially at one of the termi.

[0089] Preferred peptides exhibiting good to very good adhesion to at least one fatty and / or oily, preferably fatty, soiling on polyester textiles have an amino acid sequence that has at least 80% and increasingly preferably 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 peptides listed in SEQ ID NO: 1, 3, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 16, 17, 18, 19, 20, 21, 22, 25. Further preferred peptides exhibiting good to very good adhesion to at least one fatty and / or oily, preferably fatty, soiling on polyester textiles have an amino acid sequence identical to one of the amino acid sequences specified in SEQ ID NO: 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 fatty and / or oily, preferably fatty, soiling on polyester textiles have an amino acid sequence identical to one of the amino acid sequences listed in SEQ ID NO: 1, 3, 7, 8, 9, 10, 11, 12, 13, 17, 19, 20, 21, 25, 26, 27, 29, 31. Most particularly preferred peptides exhibiting good to very good adhesion to at least one fatty and / or oily, preferably fatty, soiling on polyester textiles have an amino acid sequence identical to one of the amino acid sequences listed in SEQ ID NO: 8, 10, 21, 25, 26.

[0090] Preferred peptides exhibiting good to very good adhesion to at least one fatty and / or oily, preferably fatty, soiling on cotton textiles have an amino acid sequence that has at least 80% and increasingly preferably 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 peptides listed in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17, 18, 19, 20, 22. Further preferred peptides exhibiting good to very good adhesion to at least one fatty and / or oily, preferably fatty, soiling on cotton textiles have an amino acid sequence identical to one of the amino acid sequences listed in SEQ ID NO: 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 fatty and / or oily, preferably fatty, soiling on cotton textiles have an amino acid sequence identical to one of the amino acid sequences specified in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 17, 18, 19, 20, 23, 24, 25, 26, 27, 29. Particularly preferred peptides that exhibit good to very good adhesion to at least one fatty and / or oily, preferably fatty, soiling on cotton textiles have an amino acid sequence identical to one of the amino acid sequences specified in SEQ ID NO: 1, 3, 4, 6, 7, 8, 9, 10, 12, 13, 23, 26, 27.

[0091] In particularly preferred embodiments, peptides according to the invention bind to at least one fatty and / or oily, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, e.g. fatty and / or oily soiling on dishes, pots, cutlery (metal) or glass.

[0092] Preferred peptides exhibiting good to very good adhesion to at least one fatty and / or oily, preferably greasy, soiling on hard surfaces, particularly dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, have an amino acid sequence that exhibits at least 80% and increasingly preferably 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 specified in SEQ ID NO:1-31. Further preferred peptides exhibiting good to very good adhesion to at least one fatty and / or oily, preferably greasy, soiling on hard surfaces, especially dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g.cutlery or pots) or glass, exhibit an amino acid sequence identical to one of the amino acid sequences listed in SEQ ID NO: 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. Particularly preferred peptides exhibiting good to very good adhesion to at least one fatty and / or oily, preferably greasy, soiling on hard surfaces, especially dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, have an amino acid sequence identical to one of the amino acid sequences specified in SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 17, 19, 20, 21, 22, 23, 25, 26, 27, 28, 29.Particularly preferred peptides that exhibit good to very good adhesion to at least one fatty and / or oily, preferably greasy, soiling on hard surfaces, especially dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, have an amino acid sequence that is identical to one of the amino acid sequences specified in SEQ ID NO: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0093] Methods for determining adhesion are known to those skilled in the art, and all suitable methods can be applied. Further methods are described in the examples.

[0094] If the peptide used according to the invention is coupled to at least one other (macro)molecule, it can also be referred to as a peptide derivative. The peptide used according to the invention is then derivatized. In such embodiments, the peptide can act as an adhesion tag, which causes the binding of a molecule coupled to it to the desired surface. Such molecules can also be referred to as conjugates.

[0095] In some embodiments, the peptides used according to the invention, which may, for example, have the amino acid cysteine ​​at the N- or C-terminal for coupling purposes, are coupled (functionally modified) with biotin, preferably at a suitable amino acid of the chain and / or at the N- and / or C-terminal.

[0096] It is also possible that the peptide used according to the invention is part of a protein or polypeptide. Such proteins and polypeptides can, for example, be produced recombinantly as fusion proteins. In such embodiments, the peptide according to the invention is localized either at the N- or C-terminus to mediate the adhesion of the entire molecule to a surface. In such embodiments, the peptide thus also acts as an adhesion tag.

[0097] All of the aforementioned features and embodiments can be implemented individually or in any combination.

[0098] Furthermore, the peptide used according to the invention can also be at least one subunit (module) of a larger peptide or polypeptide, wherein the polypeptide can comprise a multimer of the sequences described herein, e.g., 1 to 30 repeats, more preferably 2 to 15 repeats, and particularly preferably 2 to 10 repeats, e.g., 2, 3, 4, 5, or 6 repeats of the peptide. The polypeptide can comprise or consist of such multimers. In this context, the term "polypeptide" refers in particular to peptides comprising 100 or more amino acids. The term "larger peptides" preferably refers to peptides with at least 40 amino acids, unless otherwise specified.

[0099] In various embodiments, the peptide used according to the invention is a peptide or polypeptide (multimer) comprising two or more of the peptides as described herein. In various embodiments, the two or more peptides can be linked together by at least one spacer, preferably comprising or consisting of 1 to 10 amino acid residues, in particular 2, 3 or 4 amino acid residues, preferably selected from the group consisting of G, P, I, A and S or combinations thereof, in particular GPI or GAS. In such embodiments, the individual peptides are optionally linked linearly to one another via peptide bonds, possibly also via a spacer.

[0100] The at least one peptide according to the invention can be in aqueous solution. In various embodiments, the peptide content of the solution is preferably 0.00001 to 10 parts by weight of peptide per 100 parts by weight of water, e.g., 0.00001 to 10 wt.%, preferably 0.0001 to 7.5 wt.%, more preferably 0.001 to 5 wt.%, in each case based on the total weight of the solution.

[0101] The inventive compositions increasingly preferably contain the peptides according to the invention in an amount of 1 × 10 each. -8 up to 10 wt%, from 0.00001 to 5 wt%, from 0.00005 to 2.5 wt%, from 0.0001 to 1.5 wt%, 0.001 to 0.75 wt% based on active protein and total weight of the product.

[0102] The means according to the invention contain, in addition to the at least one peptide according to the invention, at least one enzyme which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase.

[0103] Enzymes that exhibit hydrolytic activity at an ester bond are enzymes capable of hydrolytically cleaving esters into an alcohol and an acid (saponification). They are therefore called hydrolases.

[0104] Lipases are enzymes that catalyze the hydrolysis of ester bonds in lipid substrates, particularly in fats and oils. Lipases therefore constitute a group of esterases. They are generally versatile enzymes that accept a wide variety of substrates, such as aliphatic, alicyclic, bicyclic, and aromatic esters, thioesters, and activated amines. Lipases are effective, for example, against grease residues in laundry by catalyzing their hydrolysis (lipolysis). Lipases with broad substrate spectra are particularly useful where inhomogeneous raw materials or substrate mixtures need to be processed, such as in detergents and cleaning agents, since soiling can consist of fats and oils with varying structures. The lipases used in detergents and cleaning agents known from the prior art are usually of microbial origin and generally come from bacteria or fungi.Lipases are produced by suitable microorganisms of the genera Thermomyces, Bacillus, Pseudomonas, Acinetobacter, Micrococcus, Humicola, Trichoderma, or Trichosporon using well-known biotechnological methods, e.g., by transgenic expression hosts of the genera Bacillus or by filamentous fungi.

[0105] Generally, only selected lipases are suitable for use in liquid surfactant preparations. Many lipases do not exhibit sufficient catalytic performance or stability in such preparations. Furthermore, the use of lipases results in an unpleasant odor on washed items, especially textiles, after the washing process. This is because the lipase is absorbed by the textiles and continues to hydrolyze fatty acid esters to low molecular weight fatty acids. These low molecular weight fatty acids are then perceived due to their unpleasant odor. The intensity of the odor can vary depending on the nature of the textile.

[0106] Examples of suitable lipases include, for example, lipase from Thermomyces, e.g., from T. lanuginosus (formerly Humicola lanuginosa), as described in EP 0258068 and EP 0305216; lipase from strains of Pseudomonas (some of which are now renamed Burkholderia), e.g., P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. sp. strain SD705, P. wisconsinensis; Streptomyces lipases of the GDSL type; lipase from Thermobifida fusca; lipase from Geobacillus stearothermophilus; lipase from Bacillus subtilis; and lipase from Streptomyces griseus and S. pristinaespiralis. Preferred lipases include, for example, those originally obtained from or further developed from Humicola lanuginosa (Thermomyces lanuginosus), in particular those with one or more of the following amino acid substitutions starting from the aforementioned lipase at positions D96L, T213R and / or N233R, especially T213R and N233R.Preferred commercial lipase products include Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A / S), Lumafast (Genencor / DuPont) and Lipomax (Gist-Brocades).

[0107] Methods for determining lipase activity are familiar to those skilled in the art of enzyme technology and are routinely used by them (see, e.g., Bruno Stellmach, "Methods of Determining Enzymes for Pharmacy, Food Chemistry, Technology, Biochemistry, Biology, Medicine," Steinkopff Verlag Darmstadt, 1988, pp. 172ff). In this method, lipase-containing samples are added to an olive oil emulsion in water containing an emulsifier and incubated at 30°C and pH 9.0. This releases fatty acids. These are then continuously titrated with 0.01 N sodium hydroxide solution using an autotitrator for 20 minutes, maintaining a constant pH ("pH-stat titration"). The lipase activity is determined based on the sodium hydroxide consumption and reference to a reference lipase sample. An alternative test for determining the lipolytic activity of the lipases according to the invention is an optical measurement method, preferably a photometric method.The appropriate test involves the lipase-dependent cleavage of the substrate para-nitrophenol butyrate (pNP-butyrate). This is cleaved by lipase into para-nitrophenolate and butyrate. The presence of para-nitrophenolate can be determined at 405 nm using a photometer, such as the Tecan Sunrise device, and the XFLUOR software, thus allowing conclusions to be drawn about the enzymatic activity of the lipase.

[0108] In a preferred embodiment, an agent according to the invention comprises at least one lipase selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 consisting of T231R-N233R, P208N-T231R-N233R, F211N-T231R-N233R, T231 R-N233R-P253N, N33Q-G91Q-E210Q-I255A, N33Q-G91Q-E210Q-T231R-N233R-1255A, D96E-T231R-N233R, N33Q-D96E-T231R-N233R, N33Q-D111A-T231R-N233R, N33Q-T231R-N233R-P256T, N33Q-G38A-G91T-G163K-T231R-N233R-D254S, N33Q-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-N33Q-G38A-G91T-D96E-D111AG163K-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-D254S-P256T, G163K-T231R-N233R-D254S, D27R-N33Q-G38A-G91T-D96E-G163K-T231R-N233R-D254S-P256T, D27R-G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96EG163K-T231R-N233R-D254S, D27R-G163K-T231R-N233R-D254S, D27R-G38A-G91T-D96E-D111AG163K-T231R-N233R-D254S, D27R-G38A-G91T-D96E-G163K-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-D96E-G163K-T231R-N233R-D254S, D27R-D96E-D111A-G163K-T231R-N233R-D254S-P256T D27R-G38A-D96E-G163K-T231R-N233R-D254S-P256T, D111A-G163K-T231R-N233R-D254S-P256T, D111A-T231R-N233R, D111A-T231R-N233R-D254S-P256T, D27R-D96E-D111A-G163K- T231 R-N233R, D27R-D96E-D111A- T231 R-N233R, D27R-N33Q-G38A-D96E-D111A-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K-E210Q-T231R-N233R-D254S-P256T, D27R-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R, D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R-P256T, D96E-D111A-T231R-N233R, D96E-D111A-T231R-N233R-D254S,D96E-D111A-T231R-N233R-D254S-P256T, D96E-D111A-T231R-N233R-P256T, D96E-G163K-T231R-N233R-D254S-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-N233R, G91T-T231R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231R-N233R-D254S-P256T, T231R-N233R-D254S-P256T and T231R-N233R-P256T existing group selected; and / or, (c) a lipase having lipolytic activity and comprising an amino acid sequence that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical; and / or (d) a lipase having lipolytic activity and comprising an amino acid sequence that is identical over its entire length to at least 70% and increasingly preferably 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%, 99% or 100%, preferably 100%, to the amino acid sequence specified in SEQ ID NO:33; and / or (e) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:34 over its entire length to at least 70% and increasingly preferably 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%, 99% or 100%, preferably 100%; and / or (f) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:35 over its entire length to at least 70% and increasingly preferably 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%, 99% or 100%, preferably 100%; and / or (g) a lipase having lipolytic activity and comprising an amino acid sequence that is identical over its entire length to at least 70% and increasingly preferably 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%, 99% or 100%, preferably 100%, to the amino acid sequence specified in SEQ ID NO:36; and / or (h) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:37 over its entire length to at least 70% and increasingly preferably 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%, 99% or 100%, preferably 100%; and / or (i) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:38 over its total length to at least 70% and increasingly preferably 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%, 99% or 100%, preferably 100%.

[0109] In a further preferred embodiment, an agent according to the invention comprises at least one lipase selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, having at least one amino acid substitution selected from the group consisting of 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 consisting of T231R-N233R, P208N-T231 R-N233R, F211N-T231R-N233R, T231 R-N233R-P253N, N33Q-G91 Q-E2100-I255A, N33Q-G91 Q-E21 OQ-T231 R-N233R-1255A, D96E-T231R-N233R, N33Q-D96E-T231R-N233R, N33Q-D111A-T231R-N233R, N33Q-T231R-N233R-P256T, N33Q-G38A-G91T-G163K-T231R-N233R-D254S, N33Q-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-N33Q-G38A-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-N33Q-G38A-G91T-D96E-D111AG163K-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-D254S-P256T, G163K-T231R-N233R-D254S, D27R-N33Q-G38A-G91T-D96E-G163K-T231R-N233R-D254S-P256T, D27R-G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96EG163K-T231R-N233R-D254S, D27R-G163K-T231R-N233R-D254S, D27R-G38A-G91T-D96E-D111AG163K-T231R-N233R-D254S, D27R-G38A-G91T-D96E-G163K-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-D96E-G163K-T231R-N233R-D254S, D27R-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-G38A-D96E-G163K-T231R-N233R-D254S-P256T, D111A-G163K-T231R-N233R-D254S-P256T, D111A-T231R-N233R, D111A-T231R-N233R-D254S-P256T, D27R-D96E-D111A-G163K-T231 R-N233R, D27R-D96E-D111A-T231 R-N233R, D27R-N33Q-G38A-D96E-D111A-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K-E210Q-T231R-N233R-D254S-P256T, D27R-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R, D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R-P256T,D96E-D111A-T231R-N233R, D96E-D111A-T231R-N233R-D254S, D96E-D111A-T231R-N233R-D254S-P256T, D96E-D111A-T231R-N233R-P256T, D96E-G163K-T231R-N233R-D254S-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-N233R, G91T-T231R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231R-N233R-D254S-P256T, T231R-N233R-D254S-P256T and T231R-N233R-P256T existing group selected; and / or (c) a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:34 over its entire length to at least 70% and increasingly preferably 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%, 99% or 100%, preferably 100%; and / or (d) a lipase,exhibits lipolytic activity and comprises an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:34 over its entire length to at least 70% and increasingly preferably 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%, 99% or 100%, preferably 100%.

[0110] In a particularly preferred embodiment, an agent according to the invention comprises at least one lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its total length to at least 70% and increasingly preferably 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%, 99% or 100%, preferably 100%.

[0111] In a particularly preferred embodiment, a means according to the invention comprises at least one lipase having lipolytic activity and comprising an amino acid sequence that is 100% identical over its total length to the amino acid sequence specified in SEQ ID NO:33.

[0112] In a particularly preferred embodiment, an agent according to the invention comprises at least one lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its total length to at least 70% and increasingly preferably 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% and, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, having at least one amino acid substitution selected from the group consisting of 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 group consisting of T231R-N233R, P208N-T231 R-N233R, F211N-T231R-N233R, T231 R-N233R-P253N, N33Q-G91 Q-E210Q-I255A, N33Q-G91 Q-E210Q-T231R-N233R-I255A, D96E-T231R-N233R, N33Q-D96E-T231 R-N233R, N33Q-D111A-T231R-N233R, N33Q-T231R-N233R-P256T, N33Q-G38A-G91T-G163K-T231R-N233R-D254S, N33Q-G38AG91T-D96E-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-G91 T -D96E-D111 A-G163K- T231 R-N233R-D254S,D27R-G38A-G91T-D96E-D111AG163K-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-P256T, D96E-G163K-T231R-N233R-D254S, D27R-G163K-T231R-N233R-D254S, D27R-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S, D27R-G38A-G91T-D96E-G163K-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-D96E-G163K-T231R-N233R-D254S, D27R-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-G38A-D96E-G 163K- T231 R-N233R-D254S-P256T, D111A-G163K-T231R-N233R-D254S-P256T, D111A-T231R-N233R, D111A-T231R-N233R-D254S-P256T, D27R-D96E-D111A-G163K-T231R-N233R, D27R-D96E-D111A-T231R-N233R, D27R-N33Q-G38A-D96E-D111A-T231 R-N233R-D254S-P256T, D27R-G38A-D96E-D1 1 1A-G163K-E210Q-T231R-N233R-D254S-P256T, D27R-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R, D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R-P256T,D96E-D111A-T231R-N233R, D96E-D111A-T231R-N233R-D254S, D96E-D111A-T231R-N233R-D254S-P256T, D96E-D111A-T231R-N233R-P256T, D96E-G163K-T231R-N233R-D254S-P256T, D96E-T231R-N233R-D254S-P256T, D96E-T231R-N233R-P256T, G38A-D96E-D111A-T231R-N233R, The existing group G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, G91T-D96E-D111A-T231R-N233R, G91T-D96E-T231R-N233R, G91T-T231R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231R-N233R-D254S-P256T, T231R-N233R-D254S-P256T and T231R-N233R-P256T has been selected.

[0113] In a particularly preferred embodiment, a composition according to the invention comprises at least one lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its total length to at least 70% and increasingly preferably 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% and, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) at at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 consisting of T231R-N233R, P208N-T231 R-N233R, F211N-T231R-N233R, T231 R-N233R-P253N, N33Q-G91 Q-E210Q-I255A, N33Q-G91 Q-E210Q-T231R-N233R-I255A, D96E-T231R-N233R, N33Q-D96E-T231R-N233R, N330-D111A-T231R-N233R, N33Q-T231R-N233R-P256T, N33Q-G38A-G91T-G163K-T231R-N233R-D254S, N33Q-G38A-G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-N330-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-D254S-P256T, G163K-T231 R-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-G91T-D96E-G163K-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-D96E-G163K-T231R-N233R-D254S, D27R-D96E-D111A-G163K-T231R-N233R-D254S-P256T, D27R-G38A-D96E-G163K-T231R-N233R-D254S-P256T, D111A-G163K-T231R-N233R-D254S-P256T, D111A-T231R-N233R, D111A-T231R-N233R-D254S-P256T, D27R-D96E-D111AG163K-T231R-N233R, D27R-D96E-D111A-T231R-N233R, D27R-N33Q-G38A-D96E-D111A-T231R-N233R-D254S-P256T, D27R-G38A-D96E-D111A-G163K-E210Q-T231R-N233R-D254S-P256T, D27R-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R, D96E-D111A-G163K-T231R-N233R-D254S-P256T, D96E-D111A-G163K-T231R-N233R-P256T, D96E-D111A-T231R-N233R, D96E-D111A-T231R-N233R-D254S,D96E-D111A-T231R-N233R-D254S-P256T, D96E-D111A-T231R-N233R-P256T, D96E-G163K-T231R-N233R-D254S-P256T, D96E-T231R-N233R-D254S-P256T, D96E-T231R-N233R-P256T, G38A-D96E-D111A-T231R-N233R, G91T-D96E-D111A-G163K-T231R-N233R-D254S-P256T, The existing group G91T-D96E-D111A-T231R-N233R, G91T-D96E-T231R-N233R, G91T-T231R-N233R-D254S-P256T, N33Q-D96E-D111A-G163K-T231R-N233R-D254S-P256T, T231R-N233R-D254S-P256T and T231R-N233R-P256T has been selected.

[0114] In preferred embodiments, the composition according to the invention contains at least one salt. In preferred embodiments, the composition contains at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, and particularly preferably about 1 to about 2 wt.%, based on the active substance and the total weight of the composition.

[0115] In preferred embodiments, the at least one salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0116] In preferred embodiments, the composition according to the invention contains at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on the active substance and total weight of the composition, wherein the at least one salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0117] In preferred embodiments, the at least one salt is selected from lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof.

[0118] In preferred embodiments, the composition according to the invention contains at least one salt selected from alkali metal salts with inorganic counterions, particularly preferably alkali metal halides, in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on the active substance and total weight of the composition.

[0119] In further preferred embodiments, compositions according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on the active substance and total weight of the composition, wherein the at least one salt is selected from lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof.

[0120] In particularly preferred embodiments, the at least one salt is selected from lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate and mixtures thereof.

[0121] In particularly preferred embodiments, compositions according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on active substance and total weight of the composition, wherein the at least one salt is selected from lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate and mixtures thereof.

[0122] In further particularly preferred embodiments, the at least one salt is selected from lithium chloride, sodium chloride, potassium chloride and mixtures thereof.

[0123] In further particularly preferred embodiments, compositions according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on active substance and total weight of the composition, wherein the at least one salt is selected from lithium chloride, sodium chloride, potassium chloride and mixtures thereof.

[0124] In particularly preferred embodiments, the at least one salt is selected from sodium chloride, potassium chloride and mixtures thereof.

[0125] In particularly preferred embodiments, compositions according to the invention contain at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, particularly preferably about 1 to about 2 wt.%, based on the active substance and total weight of the composition, wherein the at least one salt is selected from sodium chloride, potassium chloride and mixtures thereof.

[0126] Within the scope of the invention, cleaning performance is understood to mean the ability of a means to partially or completely remove existing soiling, in particular the brightening performance of one or more soilings on textiles and / or hard surfaces. Within the scope of the invention, both the means itself and the washing and / or cleaning solution formed by this means possess a respective cleaning performance.

[0127] The term "washing or cleaning solution" refers to the working solution containing the washing or cleaning agent that acts on textiles, fabrics, or surfaces, particularly dishes or household surfaces, and thus comes into contact with the soiling present on these items. The washing or cleaning solution is typically created when the washing or cleaning process begins and the agent is diluted with water, for example, in a washing machine, dishwasher, or other suitable container.

[0128] The composition of the washing or cleaning agents according to the invention, as well as the quantities of the ingredients, depends on the respective intended use, and the trained person is generally familiar with suitable dosages of these components and can obtain them from the relevant technical literature.

[0129] The washing and / or cleaning agents according to the invention include all conceivable types of washing or cleaning agents, both concentrates and undiluted agents, for use on a commercial scale, in washing machines, or for hand washing or cleaning. These include, for example, detergents for textiles, carpets, or natural fibers, for which the term "washing agent" is used. They also include, for example, dishwashing detergents for dishwashers (machine dishwashing detergents) or manual dishwashing detergents, or cleaners 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. This includes, in addition to manual and machine dishwashing detergents, scouring agents, glass cleaners, toilet fresheners, etc.The washing and cleaning agents within the scope of the invention also include washing aids that are added to the actual detergent during manual or machine textile washing to achieve an additional effect. Furthermore, washing and cleaning agents within the scope of the invention also include textile pre- and post-treatment agents, i.e., agents with which the garment is brought into contact before the actual washing, e.g., to loosen stubborn stains, and also agents that, in a step following the actual textile washing, impart further desirable properties to the laundry, such as a pleasant feel, wrinkle resistance, or low static charge. Fabric softeners are among the latter. This also includes agents for use in (semi-)automated washing or cleaning systems, such as robotic mops or wet vacuum cleaners.

[0130] The washing and / or cleaning agents according to the invention, which may be in the form of powdered or granular solids, in compacted or post-compacted particle form, as homogeneous solutions or suspensions, may contain all known ingredients commonly found in such agents. In particular, the agents according to the invention may contain surfactants, builders, complexing agents, polymers, glass corrosion inhibitors, corrosion inhibitors, bleaching agents such as peroxygen compounds, bleach activators or bleach catalysts, water-miscible organic solvents, enzyme stabilizers, sequestrants, electrolytes, pH regulators, and / or other auxiliary substances such as optical brighteners, anti-graying agents, color transfer inhibitors, foam regulators, as well as colorants and fragrances.Advantageous ingredients of the composition according to the invention are disclosed in the international patent application WO 2009 / 121725, beginning on page 5, penultimate paragraph, and ending on page 13 after the second paragraph. This disclosure is expressly incorporated by reference and its content is included in the present patent application.

[0131] The inventive compositions increasingly preferably contain the peptides according to the invention in an amount of 1 × 10 each. -8 up to 10 wt%, from 0.00001 to 5 wt%, from 0.00005 to 2.5 wt%, from 0.0001 to 1.5 wt%, 0.001 to 0.75 wt% based on active protein and total weight of the product.

[0132] The protein concentration can be determined using known methods, e.g., the BCA method (bicinchoninic acid; 2,2'-bicinolyl-4,4'-dicarboxylic acid) or the biuret method (Gornall et al., J. Biol. Chem., 1948, 177, 751-766). The determination of the active protein concentration can be carried out by titration of the active sites using a suitable irreversible inhibitor and determination of the residual activity (Bender et al., J. Am. Chem. Soc., 1966, 88, 24, 5890-5913). Furthermore, those skilled in the art in peptide and protein technology are aware of a multitude of suitable methods for determining the peptide or protein concentration that can be applied within the scope of this invention.

[0133] Further embodiments include all solid, powdered, liquid, gel-like, or pasty dosage forms of the composition according to the invention, which may optionally consist of several phases and may be in compressed or uncompressed form. The composition may be in the form of a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, more specifically 500 g / l to 900 g / l or 600 g / l to 850 g / l. Solid dosage forms of the composition also include extrudates, granules, tablets, or pouches. Alternatively, the composition may also be liquid, gel-like, or pasty, e.g., in the form of a non-aqueous liquid detergent or a non-aqueous paste, or in the form of an aqueous liquid detergent or a water-containing paste. Liquid compositions are generally preferred. Furthermore, the composition may be in the form of a single-component system. Such compositions consist of one phase. Alternatively, a composition may also consist of several phases.Such a remedy is therefore divided into several components.

[0134] When compositions according to the invention are in liquid form, they preferably contain more than 20 wt.%, preferably 30 to 90 wt.% and preferably 40 to 80 wt.% water based on their total weight.

[0135] The composition according to the invention can contain one or more surfactants, in particular anionic surfactants, non-ionic surfactants and mixtures thereof, but also cationic, zwitterionic and / or amphoteric surfactants. The composition preferably contains 0.5 to 70 wt.% surfactant. In textile detergents, 35 to 60 wt.% and more preferably 40 to 55 wt.% surfactant, based on the total weight of the composition, is preferably used; in preferred embodiments, the composition preferably contains 3 to 35 wt.%, and more preferably 5 to 30 wt.%, surfactant, based on the total weight of the composition.

[0136] Suitable anionic surfactants are, in particular, soaps and those containing sulfate or sulfonate groups with preferably alkali ions as cations. Usable soaps are preferably the alkali salts of saturated or unsaturated C₆H ... 12-18 -Fatty acids. Such fatty acids can also be used in a partially neutralized form. Useful sulfate-type surfactants include the salts of the sulfuric acid half-esters of C. 12-18 Fatty alcohols and the sulfation products of the aforementioned nonionic surfactants with a low degree of ethoxylation. Usable sulfonate-type surfactants include, for example, C 9-14 -Alkylbenzenesulfonates, alkanesulfonates derived from C 12-18 -Alkanes can be obtained, for example, by sulfochlorination or sulfoxidation followed by hydrolysis or neutralization, C 12-18-Olefin sulfonates, which are formed by the reaction of corresponding monoolefins with sulfur trioxide, mixtures of alkene and hydroxyalkane sulfonates, disulfonates, such as those obtained from C 12-18 -Monoolefins with terminal or internal double bonds are obtained by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acidic hydrolysis of the sulfonation products, as well as α-sulfofaticial esters (ester sulfonates) that are formed by the sulfonation of fatty acid methyl or ethyl esters, e.g. α-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids.

[0137] Preferably, the composition, in particular a textile detergent, comprises 2 to 55 wt.%, preferably 3 to 35 wt.%, of anionic surfactant based on the total weight of the composition. Most preferably, the composition comprises 3 to 25 wt.% of alkylbenzenesulfonate. Furthermore, the composition may preferably contain other anionic surfactants, in particular alkyl ether sulfates, as well as non-ionic surfactants, in particular fatty alcohol alkoxylates. These may then constitute the remaining surfactants.

[0138] Suitable alkylbenzenesulfonates are preferably selected from linear or branched alkylbenzenesulfonates of formula R' and R" where R' and R" are independent of H or alkyl and together contain 6 to 19, preferably 7 to 15, and particularly 9 to 13 carbon atoms. Sodium dodecylbenzylsulfonate is a particularly preferred representative.

[0139] The alkali and especially the sodium salts of the sulfuric acid half-esters of C are called alk(en)yl sulfates. 12-18-Fatty alcohols, e.g. from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or the C 10-20 Oxo alcohols and those half-esters of secondary alcohols of these chain lengths are preferred. Also preferred are alk(en)yl sulfates of the aforementioned chain length, which contain a synthetic, petrochemical-based, straight-chain alkyl group and exhibit analogous degradation behavior to the corresponding compounds based on fatty chemical raw materials. For washing-related purposes, the C 12-16 -Alkyl sulfates and C 12-15 -Alkyl sulfates as well as C 14-15 -Alkyl sulfates preferred.

[0140] Also the sulfuric acid monoesters of the straight-chain or branched C ethoxylated with 1 to 6 mol of ethylene oxide. 7-21 -Alcohols, such as 2-methyl-branched C 9-11 -Alcohols with an average of 3.5 mol ethylene oxide (EO) or C 12-18 Fatty alcohols with 1 to 4 EO are suitable.

[0141] Suitable alkyl ether sulfates are, for example, compounds of the formula R. 1 -O-(AO) n -SO3 - X + In this formula, R stands for... 1 for a linear or branched, substituted or unsubstituted alkyl group, preferably for a linear, unsubstituted alkyl group, preferably for a fatty alcohol group. Preferred groups R' are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl groups and mixtures thereof, with the representatives with an even number of carbon atoms being preferred. Particularly preferred groups R 1 are derived from C 12-18 -Fatty alcohols, e.g., coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol, or C 10-20-Oxo alcohols. AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably for an ethylene oxide group. The index n stands for an integer from 1 to 50, preferably from 1 to 20, and particularly from 2 to 10. Most preferably, n stands for the numbers 2, 3, 4, 5, 6, 7, or 8. X + stands for a monovalent cation or the nth part of an n-valent cation, preferably the alkali metal ions and among them Na + or K + , where Na + is extremely preferred. Further cations X + can be selected from NH4 + , ½ Zn 2+ , ½ Mg 2+ , ½ Ca 2+ , ½ Mn 2+ and their mixtures.

[0142] In various embodiments, the alkyl ether sulfate can be selected from fatty alcohol ether sulfates of the formula with k = 11 to 19, n = 2, 3, 4, 5, 6, 7 or 8. Particularly preferred representatives are Na-C 12-14Fatty alcohol ether sulfates with 2 EO (k = 11-13, n = 2). The stated degree of ethoxylation represents a statistical average, which may be a whole number or a fraction for a specific product. The stated degrees of alkoxylation represent statistical averages, which may be a whole number or a fraction for a specific product. Preferred alkoxylates / ethoxylates exhibit a narrow range of homologs (nreoxylates).

[0143] For cold washing performance, it has proven advantageous if the agents additionally contain soap(s). Preferred agents are therefore characterized by the fact that they contain soap(s). Suitable are saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid, and behenic acid, as well as, in particular, soap mixtures derived from natural fatty acids, e.g., coconut, palm kernel, or tallow fatty acids.

[0144] A class of preferably used non-ionic surfactants, which are used either as the sole non-ionic surfactant or in combination with other non-ionic surfactants, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably with 1 to 4 C atoms in the alkyl chain, in particular fatty acid methyl esters.

[0145] Another class of nonionic surfactants that can be used advantageously are the alkyl polyglycosides (APGs). Suitable alkyl polyglycosides satisfy the general formula RO(G) z, where R represents a linear or branched, particularly 2-position methyl-branched, saturated or unsaturated, aliphatic residue with 8 to 22, preferably 12 to 18, carbon atoms, and G is the symbol representing a glucose unit with 5 or 6 carbon atoms, preferably glucose. The degree of glycosylation z is between 1 and 4, preferably between 1 and 2, and particularly between 1.1 and 1.4. Linear alkyl polyglycosides are preferably used, i.e., alkyl polyglycosides in which the polyglycosyl residue is a glucose residue and the alkyl residue is an n-alkyl residue.

[0146] Non-ionic surfactants of the amine oxide type, e.g., N-cocosalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and fatty acid alkanolamides may also be suitable. The amount of these non-ionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, and in particular not more than half of it.

[0147] Suitable amphoteric surfactants are, for example, betaines of the formula (R iii )(R iv )(R v )N + CH2COO - , in the R iii an alkyl group, possibly interrupted by heteroatoms or heteroatom groups, with 8 to 25, preferably 10 to 21 C atoms and R iv as well as R v Alkyl groups of the same or different types with 1 to 3 carbon atoms, in particular C 10-18 -Alkyldimethylcarboxymethyl betaine and C 11-17 -Alkylamidopropyldimethylcarboxymethylbetaine.

[0148] Suitable cationic surfactants include, among others, the quaternary ammonium compounds of the formula (R vi )(R vii )(R viii )(R ix )N + X - , in the R vi to R ix for four identical or different, in particular two long-chain and two short-chain, alkyl groups and X -Examples of suitable cationic surfactants include an anion, particularly a halide ion, such as didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride, and mixtures thereof. Other suitable cationic surfactants are quaternary surfactants, especially those with a sulfonium, phosphonium, iodonium, or arsonium group, which are also known as antimicrobial agents. By using quaternary surfactants with antimicrobial properties, the product can be formulated to have antimicrobial activity, or its existing antimicrobial effect, if present due to other ingredients, can be enhanced.

[0149] Suitable nonionic surfactants are, in particular, alkyl glycosides and ethoxylation and / or propoxylation products of alkyl glycosides or linear or branched alcohols, each with 8 to approximately 18 carbon atoms in the alkyl moiety and 3 to 20, preferably 4 to 10, alkyl ether groups. Furthermore, corresponding ethoxylation and / or propoxylation products of N-alkylamines, vicinal diols, fatty acid esters, and fatty acid amides, which correspond to the aforementioned long-chain alcohol derivatives with respect to the alkyl moiety, as well as of alkylphenols with 5 to 12 carbon atoms in the alkyl group, are also suitable.

[0150] As nonionic surfactants, particularly in textile detergents, preferably alkoxylated, advantageously ethoxylated, especially primary alcohols with preferably 8 to 18 carbon atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol are used, in which the alcohol residue may be linear or preferably methyl-branched at the 2-position, or may contain linear and methyl-branched residues in the mixture, as is usually the case in oxo alcohol residues. However, alcohol ethoxylates with linear residues from alcohols of native origin with 12 to 18 carbon atoms, e.g., from coconut, palm, tallow, 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 12-14 -Alcohols with 3 EO or 4 EO, C 9-11 -Alcohol with 7 EO, C 13-15 -Alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C 12-18 -Alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C12-14 -Alcohol with 3 EO and C 12-18 Alcohol with 5 EO. The stated degrees of ethoxylation represent statistical averages, which may be whole or fractional numbers for a specific product. Preferred alcohol ethoxylates exhibit a narrow range of homologs (NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples include tallow fatty alcohols with 14 EO, 25 EO, 30 EO, or 40 EO.

[0151] For dishwashing detergents, the use of nonionic surfactants, as explained below, is particularly suitable. The detergents therefore contain, in particular, one or more nonionic surfactants. The weight fraction of the total weight of the detergent is preferably 0.5 to 30 wt.%, more preferably 1.0 to 20 wt.%, and more preferably 1.5 to 15 wt.%.

[0152] Examples of nonionic surfactants that can be used either 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 with 1 to 4 carbon atoms in the alkyl chain. Nonionic surfactants of the amine oxide type, e.g., N-cocosalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and fatty acid alkanolamides can also be suitable. The amount of these nonionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, and in particular not more than half of it. Such surfactants are also used, in particular, in hand dishwashing detergents. Other suitable surfactants are the polyhydroxy fatty acid amides known as PHFAs.However, low-foaming non-ionic surfactants are preferably used in dishwashing detergents, in particular alkoxylated, especially ethoxylated, low-foaming non-ionic surfactants. The detergents preferably contain non-ionic surfactants from the group of alkoxylated alcohols. Non-ionic surfactants with a melting point above room temperature are particularly preferred. Non-ionic surfactants with a melting point above 20°C, preferably above 25°C, particularly preferably between 25°C and 60°C, and especially between 26.6°C and 43.3°C, are particularly preferred. Surfactants to be used preferably come from the group of alkoxylated non-ionic surfactants, in particular the ethoxylated primary alcohols and mixtures of these surfactants with structurally more complex surfactants such as polyoxypropylene / polyoxyethylene / polyoxypropylene ((PO / EO / PO) surfactants).Such (PO / EO / PO) niotonic surfactants are also characterized by good foam control. Particularly preferred niotonic surfactants are those which have alternating ethylene oxide and alkylene oxide units. Among these, surfactants with EO-AO-EO-AO blocks are preferred, wherein one to ten EO or AO groups are bonded together before a block of the other groups follows. Here, nonionic surfactants of the general formula in which R. 1 for a straight-chain or branched, saturated or mono- or polyunsaturated C 6-24 -Alkyl or -alkenyl group is present; each group R 2 or R 3 The values ​​are selected independently from -CH3, -CH2CH3, -CH2CH2-CH3, -CH(CH3)2 and the indices w, x, y, z are independent of each other and represent integers from 1 to 6.

[0153] Therefore, non-ionic surfactants that contain a C are particularly preferred. 9-15-Alkyl group with 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.

[0154] Preferred nonionic surfactants are those of the general formula R 1 -CH(OH)CH2O-(AO) w -(A'O) x -(A''O) y -(A'''O) z -R 2 , in the R 1 for a straight-chain or branched, saturated or mono- or polyunsaturated C 6-24 -Alkyl or -alkenyl group is present, R 2 H or a linear or branched hydrocarbon residue with 2 to 26 C atoms stands for, A, A', A'' and A''' independently stand for a residue from the group -CH2CH2, -CH2CH2-CH2, -CH2-CH(CH3), -CH2-CH2-CH2-CH2, -CH2-CH(CH3)-CH2-, -CH2-CH(CH2-CH3), w, x, y and z stand for values ​​between 0.5 and 120, where x, y and / or z can also be 0.

[0155] Particularly preferred are end-capped, poly(oxyalkylated) niosurfactants which, according to formula R 1 O[CH2CH2O] x CH2CH(OH)R 2 , besides a remainder R 1 , which represents linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon residues with 2 to 30 C atoms, preferably with 4 to 22 C atoms, furthermore a linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon residue R 2 having 1 to 30 C atoms, where x represents values ​​between 1 and 90, preferably values ​​between 30 and 80 and particularly values ​​between 30 and 60.

[0156] Surfactants of formula R are particularly preferred. 1 O[CH2CH(CH3)O] x [CH2CH2O] y CH2CH(OH)R 2 , in the R 1R stands for a linear or branched aliphatic hydrocarbon residue with 4 to 18 carbon atoms or mixtures thereof. 2 A linear or branched hydrocarbon residue with 2 to 26 carbon atoms or mixtures thereof is designated, where x represents values ​​between 0.5 and 1.5 and y represents a value of at least 15. Examples of nonionic surfactants include the C 2-26 Fatty alcohol (PO)1-(EO) 15-40 -2-hydroxyalkyl ethers, especially the C 8-10 Fatty alcohol (PO)1-(EO) 22 -2-hydroxydecyl ether.

[0157] Particularly preferred are end-group-capped poly(oxyalkylated) niosurfactants of formula R 1 O[CH2CH2O] x [CH2CH(R 3 )O] y CH2CH(OH)R 2 , in the R 1 and R 2 independently of each other stands for a linear or branched, saturated or mono- or polyunsaturated hydrocarbon residue with 2 to 26 C atoms, R3 is independently selected from -CH3, -CH2CH3, -CH2CH2-CH3, -CH(CH3)2, but preferably for -CH3, and x and y independently represent values ​​between 1 and 32, where niotensides with R 3 = -CH3 and values ​​for x from 15 to 32 and y from 0.5 and 1.5 are particularly preferred.

[0158] Other preferred niotenes are the end-capped poly(oxyalkylated) niotenes of formula R 1 O[CH2CH(R 3 )O] x [CH2] k CH(OH)[CH2] j OR 2 , in the R 1 and R 2 R represents linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon residues with 1 to 30 carbon atoms. 3where H or a methyl, ethyl, n-propyl, isopropyl, n-butyl, 2-butyl, or 2-methyl-2-butyl residue stands, x represents values ​​between 1 and 30, k and j represent values ​​between 1 and 12, preferably between 1 and 5. If the value x ≥ 2, any R can be 3 in the formula R above 1 O[CH2CH(R 3 )O] x [CH2] k CH(OH)[CH2] j OR 2 be different. R 1 and R 2 The residues are preferably linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon residues with 6 to 22 carbon atoms, with residues containing 8 to 18 carbon atoms being particularly preferred. For the residue R 3 H, -CH3, or -CH2CH3 are particularly preferred. Particularly preferred values ​​for x are in the range of 1 to 20, especially from 6 to 15. As described above, any R 3The formula above will differ if x ≥ 2. This allows the alkylene oxide unit in the square brackets to be varied. For example, if x represents 3, the residue R can be 3 selected to produce ethylene oxide (R 3 = H) or propylene oxide (R 3 = CH3) units that can be joined together in any order, e.g., (EO)(PO)(EO), (EO)(EO)(PO), (EO)(EO)(EO), (PO)(EO)(PO), (PO)(PO)(EO), and (PO)(PO)(PO). The value 3 for x is chosen here as an example and can certainly be larger, with the range of variation increasing with increasing x-values ​​and including, for example, a large number of (EO) groups combined with a small number of (PO) groups, or vice versa. Particularly preferred end-capped poly(oxyalkylated) alcohols of the formula above have values ​​of k = 1 and j = 1, so that the above formula becomes R 1 O[CH2CH(R 3 )O] x CH2CH(OH)CH2OR 2simplified. In the latter formula, R 1 , R 2 and R 3 as defined above, where x represents numbers from 1 to 30, preferably from 1 to 20, and particularly from 6 to 18. Surfactants in which the residues R 1 and R 2 have 9 to 14 carbon atoms, R 3 H stands for and x takes values ​​from 6 to 15.

[0159] Finally, the non-ionic surfactants of the general formula R proved to be particularly effective. 1 -CH(OH)CH2O-(AO) w -R 2 proven, in the R 1 for a straight-chain or branched, saturated or mono- or polyunsaturated C 6-24 -Alkyl or -alkenyl group is present, R 2where represents a linear or branched hydrocarbon residue with 2 to 26 carbon atoms, A represents a residue from the group CH2CH2, CH2CH2CH2, CH2CH(CH3), preferably CH2CH2, and w represents values ​​between 1 and 120, preferably 10 to 80, particularly 20 to 40. Examples of these nonionic surfactants include the C 4-22 Fatty alcohol (EO) 10-80 -2-hydroxyalkyl ethers, especially the C 8-12 Fatty alcohol (EO) 22 -2-hydroxydecyl ether and the C 4-22 Fatty alcohol (EO) 40-80 -2-hydroxyalkyl ether.

[0160] In various embodiments of the invention, the corresponding non-end-group-capped hydroxyl mixed ethers can be used instead of the end-group-capped hydroxyl mixed ethers defined above. These can satisfy the above formulas, wherein R 2 but hydrogen is and R 1 , R 3, A, A', A'', A'''', w, x, y and z as defined above. In various embodiments, the agents, in particular the machine dishwashing detergents, contain at least one nonionic surfactant from the group of hydroxy mixed ethers.

[0161] The composition according to the invention further preferably comprises a builder, preferably at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The builders include, in particular, silicates, carbonates, and organic (co)builders.

[0162] Examples of organic (co)builders include polycarboxylates / polycarboxylic acids, polymeric polycarboxylates, aspartic acid, polyacetals, dextrins, other organic cobuilders, and phosphonates. These classes of substances are described below. Organic cobuilder substances can be present in compositions according to the invention in amounts up to 60% by weight, based on the total weight of the composition.

[0163] Useful organic framework substances include, for example, polycarboxylic acids, which can be used in the form of the free acid and / or its sodium salts. Polycarboxylic acids are defined as those carboxylic acids that carry more than one acid function. Examples include citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids and carboxymethylinulins, monomeric and polymeric aminopolycarboxylic acids, in particular glycine diacetic acid, methylglycine diacetic acid, glutamine diacetic acid, iminodisuccinates such as ethylenediamine-N,N'-disuccinic acid and hydroxyiminodisuccinates, ethylenediaminetetraacetic acid and polyaspartic acid, polymeric hydroxy compounds such as dextrin, and polymeric (poly)carboxylic acids, especially those produced by the oxidation of polysaccharides.Dextrin-accessible polycarboxylates, and / or polymeric acrylic acids, methacrylic acids, maleic acids, and copolymers thereof, which may also contain small amounts of polymerizable substances without carboxylic acid functionality. In textile detergents, the organic (co)builders are preferably present in amounts of up to 25 wt.% and more preferably 1 to 8 wt.%, based on the total weight of the product. Machine dishwashing detergents preferably contain the organic co-builders in an amount of 10 to 55 wt.%, particularly preferably 15 to 50 wt.%, based on the total weight of the product.

[0164] In addition to their builder properties, free acids typically also possess the properties of an acidifying component and thus serve to adjust the pH of preparations to a lower and milder value. Citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid, and any mixtures thereof are particularly noteworthy in this regard. Citric acid or its salts are especially preferred as the building block. Other particularly preferred building blocks include methylglycine diside acid (MGDA), glutamic acid diacetate (GLDA), aspartic acid diacetate (ASDA), hydroxyethyliminodiacetate (HEIDA), iminodisuccinate (IDS), ethylenediamine disuccinate (EDDS), carboxymethylinulin, and polyaspartate.

[0165] In preferred embodiments, citric acid and / or citrate are used as water-soluble, organic builders. Particularly preferred is the use, based on the total weight of the compound, of 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.% citric acid and / or 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.% citrate, preferably alkali citrate, and even more preferably sodium citrate. Citric acid / citrate can each be used in the form of their hydrates; for example, citric acid can be used in the form of the monohydrate, and citrate in the form of the trisodium citrate dihydrate.

[0166] Another preferred component of the composition according to the invention is a complexing agent. Phosphonates are particularly preferred complexing agents, provided their use is permitted under regulations. In addition to 1-hydroxyethane-1,1-diphosphonic acid, the complexing phosphonates include a number of different compounds, such as diethylenetriaminepenta(methylenephosphonic acid) (DTPMP). In this application, hydroxyalkane and aminoalkane phosphonates are particularly preferred. Among the hydroxyalkane phosphonates, 1-hydroxyethane-1,1-diphosphonate (HEDP) is of particular importance as a cobuilder. It is preferably used as a sodium salt, with the disodium salt being neutral and the tetrasodium salt reacting alkaline (pH 9). Ethylenediaminetetramethylenephosphonate (EDTMP), diethylenetriaminepentamethylenephosphonate (DTPMP), and their higher homologs are preferably suitable as aminoalkane phosphonates. They are preferably used in the form of the neutral-reacting sodium salts, e.g.,Aminoalkane phosphonates are used as the hexasodium salt of EDTMP or as the hepta- and octa-sodium salts of DTPMP. HEDP, from the phosphonate class, is preferred as a builder. Furthermore, aminoalkane phosphonates possess a pronounced heavy metal binding capacity. Accordingly, especially when the products also contain bleach, it may be preferable to use aminoalkane phosphonates, particularly DTPMP, or mixtures of the aforementioned phosphonates.A preferred agent within the scope of this application contains one or more phosphonates from the group consisting of 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; nitrilotri(methylenephosphonic acid) (NTMP) and / or its salts. Particularly preferred are compositions containing 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) as phosphonates. Naturally, compositions according to the invention can contain two or more different phosphonates.

[0167] Preferred compositions according to the invention are characterized in that the composition contains at least one complexing agent from the group of phosphonates, preferably 1-hydroxyethane-1,1-diphosphonate, wherein the weight fraction of the phosphonate in the total weight of the composition is preferably 0.1 to 10.0 wt.%, more preferably 0.2 to 8.0 wt.%. In textile detergents, phosphonates, preferably 1-hydroxyethane-1,1-diphosphonate, are preferably used in amounts of 0.25 to 5.0 wt.%, more preferably 0.3 to 3.0 wt.%, and particularly preferably 0.5 to 2.0 wt.%. In machine dishwashing detergents according to the invention, at least one complexing agent from the group of phosphonates, preferably 1-hydroxyethane-1,1-diphosphonate, is preferably used, wherein the weight fraction of the phosphonate to the total weight of the agent is preferably 0.5 to 8.0 wt.%, preferably 1.0 to 7.0 wt.%, and particularly preferably 1.5 to 6.5 wt.%.

[0168] In further preferred embodiments, the compositions according to the invention are essentially free of phosphonate-containing compounds. "Essentially free of phosphonate-containing compounds" in this context means that the corresponding compositions or compositions contain less than 2% by weight, preferably less than 1% by weight, more preferably less than 0.5% by weight, and particularly preferably less than 0.1% by weight, of phosphonate-containing compounds, based on the total weight of the composition. In particularly preferred embodiments, these compositions / compositions are free of phosphonate-containing compounds.

[0169] In more preferred embodiments, the complexing agents (builder substances) are selected from aminopolycarboxylic acids, in particular MGDA and GLDA. As used herein, the term "MGDA" includes, among others, methylglycine diacetic acid, α-alanine diacetic acid, N-(1-carboxyethyl)iminodiacetic acid, and N,N-bis(carboxymethyl)-DL-alanine, wherein the free acid forms and the corresponding salts, preferably alkali salts, in particular trisodium salts, are included. As used herein, the term "GLDA" includes, among others, glutamic acid diacetic acid, L-glutamic acid-N,N-diacetic acid, and N,N-bis(carboxylatomethyl)-L-glutamate, wherein the free acid forms and corresponding salts, preferably alkali salts, in particular tetrasodium salts, are included.

[0170] In textile detergents, although higher MGDA or GLDA concentrations are possible based on the total weight of the product, particularly up to 25 wt.%, 0.2 to 5 wt.%, preferably 0.25 to 3 wt.%, and even more preferably 0.5 to 2 wt.% MGDA, preferably MGDA trisodium salt (MGDA-Na3), is particularly preferred. Even more preferred is the use, based on the total weight of the product, of 0.2 to 5 wt.%, preferably 0.25 to 3 wt.%, and even more preferably 0.5 to 2 wt.% GLDA, preferably GLDA tetrasodium salt (GLDA-Na4).

[0171] In machine dishwashing detergents, the amount of MGDA or GLDA, based on the total weight of the product, is preferably 2.0 to 40 wt.%, particularly preferably 5.0 to 30 wt.%, especially 8.0 to 25 wt.%, and most preferably 10.0 to 20 wt.%. Preferably, MGDA trisodium salt is used in these amounts.

[0172] A solid composition according to the invention preferably contains at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The water-soluble organic builder substances include the organic scaffolding substances mentioned above.

[0173] In addition to the aforementioned water-soluble organic builders, the composition of the invention may also contain inorganic water-soluble builders. Suitable water-soluble inorganic builder materials include, in particular, alkali silicates, alkali carbonates, alkali hydrogen carbonates, alkali phosphates, and / or sesquicarbonates, which may be present in the form of their alkaline, neutral, or acidic sodium or potassium salts. Small amounts of calcium carbonate may also be present in solid textile detergents.

[0174] Suitable materials include, for example, water-soluble crystalline and / or amorphous alkali silicates. The alkali silicates usable as framework materials in the compositions according to the invention preferably have a molar ratio of alkali oxide to SiO₂ below 0.95, in particular from 1:1.1 to 1:12, and can be amorphous or crystalline. Preferred alkali silicates are sodium silicates, in particular amorphous sodium silicates, with a molar ratio Na₂O:SiO₂ of 1:2 to 1:2.8. Crystalline silicates, which can be present alone or in a mixture with amorphous silicates, are preferably crystalline layered silicates of the general formula Na₂Si₂. x O 2x+1The general formula β- and δ-sodium disilicates (Na₂Si₂O₅ Η y H₂O) are used, in which x, the so-called modulus, is a number from 1.9 to 22, in particular 1.9 to 4, and y is a number from 0 to 33, with preferred values ​​for x being 2, 3, or 4. Preferred crystalline layered silicates are those in which x in the aforementioned general formula takes the values ​​2 or 3. In particular, both β- and δ-sodium disilicates (Na₂Si₂O₅ Η y H₂O) are preferred. Practically anhydrous crystalline alkali silicates of the above-mentioned general formula, in which x is a number from 1.9 to 2.1, prepared from amorphous alkali silicates, can also be used in compositions according to the invention. In a further embodiment of compositions according to the invention, a crystalline sodium layered silicate with a modulus of 2 to 3, such as can be produced from sand and soda, is used. In a further embodiment of the invention, crystalline sodium silicates with a modulus in the range of 1.9 to 3.5 are used.In compositions containing both amorphous and crystalline alkali silicates, the weight ratio of amorphous alkali silicate to crystalline alkali silicate is preferably 1:2 to 2:1 and particularly 1:1 to 2:1. Crystalline layered silicates of the formula given above are marketed by Clariant GmbH under the trade name Na-SKS, e.g., 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, makatite). Of these, Na-SKS-5 (a-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) are particularly suitable, but especially Na-SKS-6 (δ-Na2Si2O5). In one embodiment of the composition according to the invention, a granular compound of crystalline layered silicate and citrate, of crystalline layered silicate and the aforementioned (co-)polymeric polycarboxylic acid, or of alkali silicate and alkali carbonate is used, such as that commercially available under the name Nabion® 15. Such water-soluble inorganic builder materials are preferably contained in the composition according to the invention in amounts of 1 to 20 wt.%, in particular 5 to 15 wt.%, based on the total weight of the composition.Furthermore, carbonates (and hydrocarbon carbonates), especially sodium carbonate, are also important as water-soluble inorganic building substances.

[0175] Alkali carbonate(s), particularly sodium carbonate (soda), is preferred as a building material in machine dishwashing detergents. Typical amounts range from 5 to 50 wt.%, preferably 10 to 40 wt.%, and particularly 15 to 30 wt.%, based on the total weight of the detergent.

[0176] The composition according to the invention is preferably free of phosphate builder, i.e., contains less than 1 wt% of the composition by weight, preferably no deliberately added phosphate builder.

[0177] The composition according to the invention may also contain water-insoluble builder substances. In particular, crystalline or amorphous water-dispersible alkali aluminosilicates are used as water-insoluble inorganic builder materials, in amounts of up to 50 wt.%, preferably not exceeding 40 wt.%, particularly 3 to 20 wt.%, and most preferably 1 to 15 wt.%, based on the total weight of the composition. Among these, crystalline sodium aluminosilicates of detergent quality, in particular zeolite A, zeolite P, zeolite MAP, and optionally zeolite X, alone or in mixtures, e.g., in the form of a co-crystallizate of zeolites A and X (Vegobond® AX, a commercial product of Condea Augusta SpA), are preferred. Amounts close to the aforementioned upper limit are preferably used in solid, particulate compositions. Suitable aluminosilicates, in particular, do not contain particles with a particle size greater than 30 µm and preferably consist of at least 80 wt.-% of particles with a size of less than 10 µm. Their calcium binding capacity, which can be determined according to DE 2412837 A1, is generally in the range of 100 to 200 mg CaO per gram.

[0178] In preferred embodiments, the means according to the invention comprise a builder system comprising at least one builder, preferably in an amount of 0.5 to 50 wt.%, preferably 0.5 to 20 wt.%, particularly preferably 0.5 to 10 wt.%.-%, based on the total weight of the product, wherein the builder consists of polycarboxylic acids such as citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids and carboxymethylinulins or their salts, monomeric and polymeric aminopolycarboxylic acids such as glycine diacetic acid, methylglycine diacetic acid (MGDA), glutamic diacetic acid (GLDA), nitrile diacetic acid, iminodisuccinates such as ethylenediamine-N,N'-disuccinic acid (EDDS) and hydroxyiminodisuccinates, ethylenediaminetetraacetic acid and polyaspartic acid or their salts, polyphosphonic acids such as aminotris(methylenephosphonic acid), ethylenediaminetetrakis(methylenephosphonic acid), lysinetetra(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 are selected as part of the group.

[0179] In preferred embodiments, the means according to the invention, preferably textile detergents, comprise, in each case based on the total weight of the means, (j) at least 0.0000001 wt% of at least one peptide according to the invention ii) 0 to 10 wt.%, preferably 1 to 4 wt.% citric acid and / or citrate, preferably alkali citrate, iii) 0 to 40 wt.%, preferably 0 to 15 wt.%, more preferably 1 to 3 wt.%, alkali carbonate, preferably sodium carbonate, iv) 0 to 20 wt.%, preferably 3 to 10 wt.% alkali silicate, v) 0 to 10 wt.%, preferably 0.5 to 2 wt.%, phosphonic acid and / or alkali phosphonate, particularly preferably HEDP and / or DTPMP, vi) 0 to 10 wt.%, preferably 0.5 to 3 wt.%, aminopolycarboxylic acids, preferably MGDA and / or GLDA, 0 to 10 wt.%, preferably 0.5 to 2 wt.%, phosphonic acid and / or alkali phosphonate, particularly preferably HEDP and / or DTPMP, (v) 0 to 10 wt.%, preferably 0.5 to 3 wt.%, aminopolycarboxylic acids, preferably MGDA and / or GLDA.

[0180] In other preferred embodiments, the means according to the invention, preferably machine dishwashing detergents, each based on the total weight of the means, (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.% citric acid and / or citrate, preferably alkali citrate, (iii) 0 to 40 wt.%, preferably 5 to 30 wt.%, more preferably 10 to 25 wt.%, alkali carbonate, preferably sodium carbonate, (iv) 0 to 20 wt.%, preferably 3 to 10 wt.% alkali silicate, (v) 0 to 10 wt.%, preferably 0.5 to 8 wt.%, phosphonic acid and / or alkali phosphonate, particularly preferably HEDP and / or DTPMP, (vi) 0 to 25 wt.%, preferably 5.0 to 20.0 wt.%, aminopolycarboxylic acids, preferably MGDA and / or GLDA.

[0181] Suitable peroxygen compounds for use in compositions according to the invention include, in particular, organic peracids or pericy salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid, or salts of diperdodecanedioic acid, hydrogen peroxide, and inorganic salts that release hydrogen peroxide under washing conditions, including perborate, percarbonate, persilicate, and / or persulfate such as caroate, as well as hydrogen peroxide inclusion compounds, such as H₂O₂ urea adducts. Hydrogen peroxide can also be generated using an enzymatic system, i.e., an oxidase and its substrate. If solid peroxygen compounds are to be used, these can be in the form of powders or granules, which can also be coated in a manner known in principle.The peroxygen compounds can be added to the washing liquor either as such or in the form of agents containing them, which in principle can contain all conventional washing, cleaning, or disinfecting agent components. Alkali percarbonate or alkali perborate monohydrate is particularly preferred. If an agent according to the invention contains peroxygen compounds, these are present in amounts of preferably up to 50 wt.%, in particular 5 to 30 wt.%, and more preferably 0.1 to 20 wt.%, in each case based on the total weight of the agent.

[0182] The bleaching activators used in these agents can be compounds that, under perhydrolysis conditions, yield aliphatic peroxocarboxylic acids with preferably 1 to 10 carbon atoms, particularly 2 to 4 carbon atoms, and / or optionally substituted perbenzoic acid. Suitable substances include those bearing O- and / or N-acyl groups of the specified number of carbon atoms and / or optionally substituted benzoyl groups. Preferred are multiply acylated alkylenediamines, in particular tetraacetylethylenediamine (TAED), acylated triazine derivatives, in particular 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, in particular tetraacetylglycoluril (TAGU), N-acylides, in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates or carboxylates or the sulfonic or carboxylic acids thereof, in particular nonanoyl- or isononanoyloxybenzenesulfonate or laroyloxybenzenesulfonate (NOBS or iso-NOBS or laroyloxybenzenesulfonate).LOBS), 4-(2-Decanoyloxyethoxycarbonyloxy)benzenesulfonate (DECOBS) or decanoyloxybenzoate (DOBA), carboxylic anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate, 2,5-diacetoxy-2,5-dihydrofuran and enol esters, as well as acetylated sorbitol and mannitol or their described mixtures (SORMAN), acylated sugar derivatives, in particular pentaacetylglucose (PAG), pentaacetylfructose, tetraacetylxylose and octaacetyllactose, acetylated, optionally N-alkylated glucamine and gluconolactone, N-acylated lactams, e.g. N-benzoylcaprolactam, nitriles from which perimidic acids are formed, in particular aminoacetonitrile derivatives with a quaternized nitrogen atom, and / or Oxygen-transferring sulfonimines and / or acylhydrazones. Hydrophilically substituted acylacetals and acyllactams are also preferred. Combinations of conventional bleaching activators can also be used.Such bleach activators may be present, particularly in the presence of the aforementioned hydrogen peroxide-supplying bleaching agents, in the usual quantity range, preferably in amounts of 0.5 to 10 wt.%, in particular 1 to 8 wt.%, based on the total weight of the agent, but are preferably completely absent when percarboxylic acid is used as the sole bleaching agent.

[0183] In addition to or instead of conventional bleach activators, solid products, especially textile detergents, may also contain sulfonimines and / or bleach-enhancing transition metal salts or transition metal complexes as so-called bleach catalysts.

[0184] Suitable anti-graying agents or soil-release agents (soil-release polymers) for textile detergents in particular include cellulose ethers such as carboxymethylcellulose, methylcellulose, hydroxyalkylcelluloses, and cellulose mixtures such as methylhydroxyethylcellulose, methylhydroxypropylcellulose, and methyl carboxymethylcellulose. Sodium carboxymethylcellulose, hydroxypropylmethylcellulose, and mixtures thereof, and optionally mixtures thereof with methylcellulose, are preferably used. Commonly used soil-release agents include copolyesters containing dicarboxylic acid units, alkylene glycol units, and polyalkylene glycol units. The proportion of anti-graying agents and / or soil-release agents in compositions according to the invention generally does not exceed 2% by weight and is preferably 0.5 to 1.5% by weight, particularly preferably 0.5 to 2% by weight, based on the total weight of the composition.

[0185] Optical brighteners in textile detergents, especially for textiles made of cellulose fibers (e.g., cotton), can include derivatives of diaminostilbene disulfonic acid or its alkali metal salts. Suitable examples include salts of 4,4'-bis(2-anilino-4-morpholino-1,3,5-triazin-6-yl-amino)stilbene-2,2'-disulfonic acid or similarly structured compounds that, instead of the morpholino group, have a diethanolamino group, a methylamino group, or a 2-methoxyethylamino group. Brighteners of the type of substituted 4,4'-distyryldiphenyl, such as 4,4'-bis-(4-chloro-3-sulfostyryl)diphenyl, may also be present. Mixtures of brighteners can also be used. Optical brighteners of the 1,3-diaryl-2-pyrazoline type, e.g., 1-(p-sulfoamoylphenyl)-3-(p-chlorophenyl)-2-pyrazolin, and similarly structured compounds, are particularly suitable for polyamide fibers. The concentration of optical brighteners or brightener mixtures in the agent generally does not exceed 1 wt.-%, preferably 0.05 to 0.5 wt.%, based on the total weight of the agent. In a preferred embodiment of the invention, the agent is free of such active ingredients.

[0186] Conventional defoamers that can be used in the compositions according to the invention include, for example, polysiloxane-silica mixtures, wherein the finely divided silica contained therein is preferably silanized or otherwise hydrophobized. The polysiloxanes can consist of linear compounds as well as cross-linked polysiloxane resins and mixtures thereof. Other defoamers are paraffin hydrocarbons, in particular microparaffins and paraffin waxes, whose melting point is above 40°C, saturated fatty acids or soaps with, in particular, 20 to 22 carbon atoms, e.g., sodium behenate, and alkali salts of phosphoric acid mono- and / or dialkyl esters in which the alkyl chains each have 12 to 22 carbon atoms. Among these, sodium monoalkyl phosphate and / or dialkyl phosphate with C is preferred. 16-18-Alkyl groups are used. The proportion of foam regulators can preferably be 0.2 to 2 wt.%, particularly preferably not more than 1 wt.%, based on the total weight of the agent.

[0187] To adjust the desired pH value, compositions according to the invention can contain system- and environmentally compatible acids, in particular citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid and / or adipic acid, but also mineral acids, in particular sulfuric acid or alkali hydrogen sulfates, or bases, in particular ammonium or alkali hydroxides, preferably sodium hydroxide. Such pH regulators are preferably present in the compositions according to the invention in a concentration of no more than 10% by weight, in particular from 0.5 to 6% by weight, and most preferably from 0.3 to 2% by weight, based on the total weight of the composition.

[0188] The inventive composition preferably has a pH value in the range of about 6 to about 11.5, more 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, when dissolved in a 1 wt% solution in deionized water at 20°C. The pH value is preferably measured using a standard hydrogen electrode.

[0189] As a further component, compositions according to the invention can contain an organic solvent. The addition of organic solvents has a beneficial effect on the enzyme stability and the cleaning performance of these compositions. Preferred organic solvents are from the group consisting of monohydric or polyhydric alcohols, alkanolamines, or glycol ethers.Preferably, the solvents are selected from ethanol, n- or i-propanol, butanol, glycol, propanediol, butanediol, glycerin, diglycylene glycol, propyldiglycylene glycol, butyldiglycylene glycol, hexylene glycol, 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, methoxytriglycol, ethoxytriglycol, butoxytriglycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether, and mixtures of these solvents. The weight fraction of these organic solvents in the total weight of the composition according to the invention is preferably 0.1 to 10 wt.%, preferably 0.2 to 8.0 wt.% and further preferably 0.5 to 5.0 wt.%.A particularly preferred organic solvent, especially effective for stabilizing the composition, is glycerin and 1,2-propylene glycol. Liquid compositions preferably comprise at least one polyol, preferably from the group consisting of glycerin and 1,2-propylene glycol, based on the total weight of the composition, preferably in amounts of 0.1 to 10 wt.%, more preferably 0.2 to 8.0 wt.%, and further preferably 0.5 to 5.0 wt.%. Other preferred organic solvents are the organic amines and alkanolamines. Compositions according to the invention preferably contain these amines in amounts of 0.1 to 10 wt.%, more preferably 0.2 to 8.0 wt.%, and further preferably 0.5 to 5.0 wt.%, based on the total weight of the composition. A particularly preferred alkanolamine is ethanolamine.

[0190] Furthermore, the compositions according to the invention (especially for machine dishwashing) can contain bleaching catalysts. The bleaching catalysts that can be used include, but are not limited to, the group of bleach-enhancing transition metal salts and transition metal complexes, preferably Mn, Fe, Co, Ru or Mo complexes, particularly preferably from the group of manganese and / or cobalt salts and / or complexes, in particular 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).

[0191] Machine dishwashing detergents are preferred which contain 0.001 to 1 wt.%, preferably 0.01 to 0.1 wt.% bleaching catalyst, preferably a Mn complex, in particular a complex 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).

[0192] The composition according to the invention may contain further hydrolytic enzymes or other enzymes in a concentration suitable for the efficacy of the composition. A further embodiment of the invention thus comprises compositions that additionally include one or more enzymes. Preferably used as enzymes are all enzymes that can exhibit catalytic activity in the composition according to the invention, in particular selected from proteases, amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, β-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases, and mixtures thereof. Advantageously, each enzyme is present in the composition in an amount of 1 x 10 -8 up to 5% by weight, based on active protein and total weight of the product. Each enzyme is increasingly preferred in an amount of 1 x 10 -7Up to 3 wt.%, from 0.00001 to 1 wt.%, from 0.00005 to 0.5 wt.%, from 0.0001 to 0.1 wt.% and particularly preferably from 0.0001 to 0.05 wt.% in the composition according to the invention, based on active protein and total weight of the composition. Enzymes particularly preferably exhibit synergistic cleaning performance against certain soils or stains, i.e., the enzymes contained in the composition mutually support each other in their cleaning performance.

[0193] In preferred embodiments, a composition according to the invention contains at least one enzyme and increasingly preferably at least two, three, four or five enzymes, which are preferably selected from proteases, amylases, cellulases, mannanases, pectate lyases and mixtures thereof, in a total amount of 0.01 to 10 wt.%, preferably 0.1 to 8 wt.%, particularly preferably 0.2 to 6 wt.%, based on active protein and the total weight of the composition.

[0194] Examples of proteases include subtilisins BPN' from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, protease PB92, subtilisins 147 and 309, the protease from Bacillus lentus, subtilisin DY, and the enzymes thermitase, proteinase K, and proteases TW3 and TW7, which are classified as subtilases but not as subtilisins in the strict sense. Subtilisin Carlsberg is available in an advanced form under the trade name Alcalase® from Novozymes. subtilisins 147 and 309 are marketed by Novozymes under the trade names Esperase® and Savinase®, respectively. Protease variants derived from the protease in Bacillus lentus DSM 5483 are described, for example, in WO 95 / 23221, WO 92 / 21760, WO 2013 / 060621, and EP 3660151. Other useful proteases include, for example...the enzymes available under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase®, Progress Uno 101L® and Ovozyme® from Novozymes, the enzymes available under the trade names Purafect®, Purafect® OxP, Purafect® Prime, Excellase®, Properase®, Preferenz P100® and Preferenz P300® from Danisco / DuPont, the enzyme available under the trade name Lavergy pro 104 LS® from BASF, the enzyme available under the trade name Protosol® from Advanced Biochemicals Ltd., the enzyme available under the trade name Wuxi® from Wuxi Snyder Bioproducts Ltd., the enzymes available under the trade names Proleather® and Protease P® from Amano Pharmaceuticals Ltd., and the enzyme available under the name Proteinase K-16 from Kao Corp. Proteases from Bacillus gibsonii and Bacillus pumilus, disclosed in WO 2008 / 086916, WO 2007 / 131656, WO 2017 / 215925, WO 2021 / 175696 and WO 2021 / 175697, are also particularly favored.

[0195] Examples of amylases include the α-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens, and Bacillus stearothermophilus, as well as their improved formulations for use in detergents and cleaning agents. The enzyme from Bacillus licheniformis is available from Novozymes under the name Termamyl® and from Danisco / DuPont under the name Purastar® ST. Further developments of this α-amylase are available under the trade names Duramyl® and Termamyl® ultra (both from Novozymes), Purastar® OxAm (Danisco / DuPont), and Keistase® (Daiwa Seiko Inc.). The α-amylase from Bacillus amyloliquefaciens is marketed by Novozymes under the name BAN®, and derivatives of the α-amylase from Bacillus stearothermophilus are marketed under the names BSG® and Novamyl®, also by Novozymes. Furthermore, α-amylase from Bacillus sp. is suitable for this purpose.A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) are particularly noteworthy. Fusion products of all the aforementioned molecules can also be used. Furthermore, the advanced versions of α-amylase from Aspergillus niger and A. oryzae, available under the trade names Fungamyl® from Novozymes, are suitable. Other commercially available products that can be used advantageously include Amylase-LT® and Stainzyme® or Stainzyme® ultra or Stainzyme® plus, as well as 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, PREFERENZ S100®, PREFERENZ S1000® or PREFERENZ S210®. Variants of these enzymes obtained through point mutations can also be used.

[0196] Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein-engineered mutants are included. Suitable cellulases are those from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, e.g., the fungal cellulases from Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum. Particularly suitable cellulases are alkaline or neutral cellulases with color-preserving properties. Examples of cellulases with endo-1,4-glucanase activity (EC 3.2.1.4) are described in WO 2002 / 099091, e.g., those with a sequence of at least 97% identity to the amino acid sequence of positions 1 to 773 of SEQ ID NO:2 of WO 2002 / 099091. Another example may include a GH44 xyloglucanase, e.g. a xyloglucanase enzyme with a sequence of at least 60% identity to positions 40 to 559 of SEQ ID NO:2 of WO 2001 / 062903.Other examples of cellulases include the GH45 cellulases described in WO 96 / 29397. Commercially available cellulases include Celluzyme™, Carezyme™, Carezyme Premium™, Celluclean™ (e.g., Celluclean™ 5000L and Celluclean™ 4000T), Celluclean Classic™, Cellusoft™, Endolase®, Renozyme®, and Whitezyme™ (Novozymes A / S), Clazinase™ and Puradax HA™ (Genencor International Inc.), KAC-500(B)™ (Kao Corporation), Revitalenz™ 1000, Revitalenz™ 2000, and Revitalenz™ 3000 (DuPont), as well as Ecostone® and Biotouch® (AB Enzymes).

[0197] Common mannanases are produced by Bacillus subtilis Endo-b-mannanase, Bacillus sp. I633 Endo-b-Mannanase, Bacillus sp. AAI12 Endo-b-Mannanase, Bacillus sp. AA349 Endo-b-Mannanase, Bacillus agaradhaerens NCIMB 40482 Endo-b-Mannanase, Bacillus halodurans Endo-b-Mannanase, Bacillus clausii Endo-b-Mannanase, Bacillus licheniformis Endo-b-Mannanase, Humicola insolens Endo-b-Mannanase und Caldocellulosiruptor sp. Endo-b-Mannanase (ZB US 6060299, WO 99 / 64573, US 6566114 and WO 99 / 64619).

[0198] Pectate lyases suitable for washing and cleaning agents are described, for example, in WO 2003 / 095638 or WO 2015 / 121133. Examples of suitable pectinolytic enzymes also include those available under the trade names Gamanase®, Pectinex AR®, X-Pect® or Pectaway® from Novozymes, under the trade names Rohapect UF®, Rohapect TPL®, Rohapect PTE100®, Rohapect MPE®, Rohapect MA plus HC, Rohapect DA12L®, Rohapect 10L®, Rohapect B1L® from AB Enzymes, and under the trade name Pyrolase® from Diversa Corp.

[0199] The peptides, proteins, and enzymes described herein are preferably mature peptides, proteins, or enzymes, i.e., the catalytically active molecule without signal and / or propeptide(s). Unless otherwise stated, the sequences given also refer to mature (processed) peptides, proteins, or enzymes.

[0200] In various embodiments of the invention, the respective peptide, protein, or enzyme is a free peptide, protein, or enzyme. This means that the peptide, protein, or enzyme can interact directly with all components of the composition and, if the composition is a liquid, that the peptide, protein, or enzyme is in direct contact with the solvent of the composition (e.g., water). In other embodiments, a composition may contain peptides, proteins, or enzymes that form an interaction complex with other molecules or that contain a "coating." In this case, a single or multiple peptide, protein, or enzyme molecule(s) may be separated from the other components of the composition by a surrounding structure. Such a separating structure can be formed by, but is not limited to, vesicles, such as a micelle or a liposome.The surrounding structure can also be a virus particle, a bacterial cell, or a eukaryotic cell. In various embodiments, a product may contain cells of Bacillus pumilus or Bacillus subtilis expressing peptides, proteins, or enzymes, or cell culture supernatants of such cells.

[0201] In the context of the present invention, the feature that a peptide, protein, or enzyme has the specified substitution(s) (or deletion or insertion) means that it contains one (of the specified) substitution(ies) (or deletion or insertion) at the respective position, i.e., at least the specified positions are not otherwise mutated or deleted, e.g., by fragmentation of the peptide, protein, or enzyme. In various embodiments, the peptides, proteins, and / or enzymes described herein, with the exception of the explicitly mentioned substitutions, have the sequence of the respective reference sequence, i.e., apart from the substituted positions, they are 100% identical to the respective reference sequence.

[0202] The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the established and commonly used BLAST algorithm (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 Acids Res., 1997, 25, 3389-3402) and is essentially performed by matching similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences. A tabular assignment of the relevant positions is called an alignment. Another algorithm available in the art is the FASTA algorithm. Sequence comparisons (alignments), especially multiple sequence comparisons, are performed using computer programs. The Clustal series (Chenna et al.) is frequently used, for example.Multiple sequence alignment with the Clustal series 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 programs or algorithms. Sequence comparisons (alignments) are also possible using the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the predefined standard parameters, whose AlignX module for sequence comparisons is based on ClustalW, or Clone Manager 10 (using the BLOSUM 62 scoring matrix for sequence alignment at the amino acid level). Unless otherwise specified, the sequence identity stated herein is determined using the BLAST algorithm.

[0203] Such a comparison also allows for a statement about the similarity of the compared sequences to one another. This is usually expressed as percent identity, meaning the proportion of identical nucleotides or amino acid residues at the same positions or positions corresponding to each other in an alignment. The broader concept of homology, in the case of amino acid sequences, includes conserved amino acid substitutions in the analysis, i.e., amino acids with similar chemical activity, since these usually exert similar chemical activities within the peptide, protein, or enzyme. Therefore, the similarity of the compared sequences can also be expressed as percent homology or percent similarity. Identity and / or homology statements can be made for entire polypeptides or genes, or only for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are thus defined by similarities in the sequences.Such regions often exhibit identical functions. They can be small, comprising only a few nucleotides or amino acids. Often, these small regions perform essential functions for the overall activity of the peptide, protein, or enzyme. It can therefore be advantageous to refer to sequence similarities only in individual, possibly small, regions. Unless otherwise stated, however, identity or homology claims in this application refer to the total length of the respective nucleic acid or amino acid sequence.

[0204] In the context of the present invention, the statement that an amino acid position corresponds to a numerically designated position in SEQ ID NO:1 therefore means that the corresponding position is assigned to the numerically designated position in SEQ ID NO:1 in an alignment as defined above.

[0205] For the description of substitutions affecting exactly one amino acid position (amino acid exchanges), the following convention is used: first, the naturally occurring amino acid is designated using the internationally accepted one-letter code, followed by the corresponding sequence position, and finally the inserted amino acid. Multiple or alternative exchanges within the same polypeptide chain are separated by slashes. Thus, "130D / V" means that position 130 has been mutated to D or V. In the case of insertions, additional amino acids are named after the sequence position. In the case of deletions, the missing amino acid is replaced by a symbol, e.g., an asterisk or a dash, or a Δ is indicated before the corresponding position.For example, P9T describes the substitution of proline at position 9 by threonine, P9TH the insertion of histidine after the amino acid threonine at position 9, and P9* or ΔP9 the deletion of proline at position 9. This nomenclature is familiar to those skilled in the art in enzyme technology.

[0206] Using well-known methods such as chemical synthesis or polymerase chain reaction (PCR) in conjunction with standard molecular biological and / or protein chemistry techniques, a specialist can synthesize the corresponding nucleic acids, even complete genes, from known DNA and / or amino acid sequences. Such methods are described, for example, in Sambrook, J., Fritsch, EF and Maniatis, T. 2001. Molecular cloning: a laboratory manual, 3rd Edition Cold Spring Laboratory Press.

[0207] Furthermore, the peptides, proteins, enzymes, and / or other ingredients contained in the composition can be encapsulated with a substance that is impermeable to the peptide, protein, or enzyme at room temperature or in the absence of water, but which becomes permeable to the peptide, protein, or enzyme under the conditions of use. Such an embodiment of the invention is thus characterized in that the peptide, protein, or enzyme is encapsulated with a substance that is impermeable to the peptide, protein, or enzyme at room temperature or in the absence of water. Furthermore, the washing or cleaning agent itself can also be packaged in a container, preferably an air-permeable container, from which it is released shortly before use or during the washing process.

[0208] In the agents described herein, the peptides, proteins, or enzymes to be used may also be formulated together with accompanying substances, for example, from fermentation. In liquid formulations, the peptides, proteins, or enzymes are preferably used as peptide, protein, or enzyme liquid formulation(s).

[0209] The peptides, proteins, or enzymes are generally not provided in the form of pure protein, but rather in the form of stabilized preparations that are suitable for storage and transport. These pre-prepared formulations include, for example, solid preparations obtained by granulation, extrusion, or lyophilization, or, particularly in the case of liquid or gel-like products, solutions of the peptides, proteins, or enzymes, advantageously as concentrated as possible, with a low water content, and / or containing stabilizers or other additives.

[0210] Alternatively, the peptides, proteins, or enzymes can be encapsulated for both solid and liquid dosage forms, e.g., by spray drying or extrusion of the peptide, protein, or enzyme solution together with a preferably natural polymer, or in the form of capsules, e.g., capsules in which the peptides, proteins, or enzymes are enclosed as if in a solidified gel, or in core-shell type capsules in which an enzyme-containing core is coated with a protective layer impermeable to water, air, and / or chemicals. Additional active ingredients, e.g., stabilizers, emulsifiers, pigments, bleaching agents, or dyes, can be applied in superimposed layers. Such capsules are produced using methods known per se, e.g., by shake or roll granulation or in fluid-bed processes. Advantageously, such granules are low-dust and, due to the coating, have a long shelf life, e.g., through the application of polymeric film formers.

[0211] Furthermore, it is possible to combine two or more peptides, proteins or enzymes so that a single granule has multiple enzyme activities.

[0212] The peptides, proteins, or enzymes can also be incorporated into water-soluble films, such as those used in the formulation of unit-dose detergents and cleaning agents. Such a film enables the release of the peptides, proteins, or enzymes upon contact with water. As used herein, "water-soluble" refers to a film structure that is preferably completely water-soluble. Preferably, such a film consists of (fully or partially hydrolyzed) polyvinyl alcohol (PVA).

[0213] The composition according to the invention may comprise one or more reversible enzyme inhibitor(s) / stabilizer(s). The composition according to the invention may contain the reversible enzyme inhibitor(s) / stabilizer(s) in a concentration of 0.1 to 2% by weight, preferably 0.3 to 1.5% by weight, based on the total weight of the composition. If several inhibitors / stabilizers are included, these values ​​refer to the total concentration. These may be selected, in particular, from the group consisting of polyols, such as glycerol or 1,2-ethylene glycol, benzamidine hydrochloride, borax, boric acids, boronic acids or their salts or esters or derivatives, in particular phenylboronic acid derivatives or 4-formylphenylboronic acid (4-FPBA), antioxidants, specific peptide compounds, and combinations thereof.

[0214] In preferred embodiments, the composition according to the invention is a washing and / or cleaning agent comprising at least one of the fat-binding peptides described herein and at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, and especially preferably lipase.

[0215] In preferred embodiments, the composition according to the invention is a washing and / or cleaning agent comprising at least one of the fat-binding peptides described herein, at least one lipase and optionally at least one salt, where the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical; and where, if available, the salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0216] In preferred embodiments, the composition according to the invention is a washing and / or cleaning agent consisting of at least two phases, wherein the at least one fat-binding peptide described herein and the optionally at least one salt are contained in a first phase, and the at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, is contained in a second phase.

[0217] In preferred embodiments, the composition according to the invention is a washing and / or cleaning agent consisting of at least two phases, wherein the at least one fat-binding peptide described herein and the optionally at least one salt are contained in a first phase and the at least one lipase are contained in a second phase. where the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256 has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical.

[0218] In preferred embodiments, the composition according to the invention is a washing and / or cleaning agent consisting of at least two phases, wherein the at least one fat-binding peptide described herein and the optionally at least one salt are contained in a first phase and the at least one lipase are contained in a second phase. where the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256 has at least one amino acid substitution selected from the group consisting of 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 that is identical to the amino acid sequence specified 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 over its total length to at least 70% and increasingly preferably 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%, 99% or 100%; and where, if available, the salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0219] In preferred embodiments, the composition according to the invention is a textile detergent, preferably a multiphase textile detergent. The textile detergent according to the invention is particularly suitable for use on textiles made of plastic and / or containing a plastic component (blended fabrics) and / or made of a natural fiber such as cotton.Preferably, the textile comprises or consists 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), polyhydroxyalkanoate (PHA), polyhydroxybutyrate (PHB), polyimide (PI), polylactide (PLA), polyvinylidene fluoride (PVDF), polyetherketone (PEK), and / or copolymers or a mixture thereof, more preferably polyester (PES), polyethylene (PE), polypropylene (PP), polystyrene (PS), copolymers or mixtures thereof, preferably a cotton / polyester blend with a polyester content of at least 10%, preferably at least 20%, further preferably at least 30%, particularly preferably at least 40%, most especially preferably at least 50%, in particular at least 60%, e.g.65% or 70%, or pure polyester or copolymers thereof. The term "mixture" or "blended fabric" refers to textiles with a plastic component, preferably textiles made of at least one natural fiber and at least one plastic fiber (plastic component). In particular, the mixture or blended fabric consists of cotton and at least one plastic, especially polyester. In preferred embodiments, a textile with a plastic component or a plastic mixture or blended fabric has a plastic component of at least 10%, preferably at least 20%, more preferably at least 30%, particularly preferably at least 40%, most preferably at least 50%, and in particular at least 60%, e.g., 65% or 70%.

[0220] In preferred embodiments, the agent is a cleaning agent for hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0221] It is preferred that the peptide according to the invention, particularly when used in washing and / or cleaning agents according to the invention, achieves a dirt-removing, and in particular a grease- and / or oil-containing, preferably fatty, soiling on textiles, especially those containing or consisting of cotton, polyester, and mixtures thereof, and / or hard surfaces, especially dishes (preferably made of ceramic such as porcelain or stoneware, as well as plastic), metal (e.g., cutlery or pots), or glass, effect. Thus, the washing and / or cleaning agent is preferably used as a detergent in a washing process, especially in machine washing or hand washing.The peptides described herein, when used in detergents and / or cleaning agents, not only improve the cleaning performance of greasy and / or oily soils, but also exhibit a dirt-removing effect, particularly effective at dissolving grease and / or oil. They thus represent a biodegradable alternative to soil-release polymers. Therefore, these peptides are especially suitable for use in detergents and cleaning agents and can contribute to improved cleaning performance. Furthermore, they can help reduce or completely eliminate the use of synthetic and chemical substances, e.g., in detergents and / or cleaning agents, by providing a biodegradable alternative. They could also contribute to the stabilization of other ingredients.

[0222] In particularly preferred embodiments, the peptides described herein, in washing and / or cleaning agents according to the invention, achieve improved cleaning performance on at least one type of greasy and / or oily soiling on textiles, in particular those containing or consisting of cotton, polyester, and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware, as well as plastic), metal (e.g., cutlery or pots), or glass. Preferably, the improved cleaning performance is based on a synergistic interaction of the peptide according to the invention and esterase. Particularly preferably, the improved cleaning performance is based on a synergistic interaction of the peptide according to the invention and lipase.

[0223] It is preferred that the improved cleaning performance of the washing and / or cleaning agent according to the invention is based on the interaction of the enzyme, which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase, and the peptide according to the invention, which binds to at least one fatty and / or oily, preferably fatty, soiling on a textile, in particular containing or consisting of cotton, polyester and mixtures thereof. It is particularly preferred that the improved cleaning performance of the washing and / or cleaning agent according to the invention is based on the interaction of the lipase and the peptide according to the invention, which binds to at least one fatty and / or oily, preferably fatty, soiling on a textile, in particular containing or consisting of cotton, polyester and mixtures thereof.

[0224] It is preferred that the improved cleaning performance of the washing and / or cleaning agent according to the invention is based on the interaction of the enzyme, which has hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase, and the peptide according to the invention, which binds to at least one fatty and / or oily, preferably fatty, soiling on a hard surface, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass.It is particularly preferred that the improved cleaning performance of the washing and / or cleaning agent according to the invention is based on the interaction of the lipase and the peptide according to the invention, which binds to at least one fatty and / or oily, preferably greasy, soiling on a hard surface, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0225] It is preferred that the peptide according to the invention has a dirt-removing, in particular grease- and / or oil-removing, effect, especially with regard to at least one grease- and / or oil-containing soiling on a textile surface, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or a hard surface, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass. In particular, the surfaces are freed from this soiling by the presence of the peptide, which binds to at least one grease-containing soiling on the textile and / or the hard surface.

[0226] One possible mechanism for the grease-dissolving effect could be that the peptides described herein are able to adsorb onto solid fats and thereby soften the grease film. This surfactant-like behavior makes it easier to remove the grease film during the cleaning process. The softened grease can be detached (roll-up mechanism) and / or rinsed away. Another possible mechanism is that the peptides described herein form a stable monolayer on the grease layer. This functionalization of the grease-containing surface, or the binding to the grease-containing soiling on a surface, allows other grease-removing and / or grease-dissolving substances or molecules, in particular lipases, easier access to the grease layer. Peptides according to the invention therefore also allow the removal of grease-containing soiling at lower temperatures, e.g., approximately 15°C, approximately 20°C, or approximately 30°C.This enables the formulation of high-performance washing and / or cleaning agents that exhibit good cleaning performance on at least one type of greasy soiling even at low temperatures, e.g., around 15°C, 20°C, or 30°C. In preferred embodiments, this effect is also due to the interaction with lipase. The improved grease removal, in addition to the hydrolysis of grease molecules by lipase, also results in better removal of the breakdown products, thus preventing their accumulation or retention on the surface. This reduces the risk of unpleasant odors caused by lipase breakdown products.

[0227] All the facts, objects, and embodiments described above are also applicable to this invention. Therefore, explicit reference is made here to the disclosure at the relevant point, with the note that this disclosure also applies to the aforementioned means according to the invention.

[0228] Another object of the invention is a method for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, characterized in that an agent according to the invention is used in at least one process step.

[0229] In preferred embodiments, in a first step the at least one peptide according to the invention is brought into contact with the item to be washed or rinsed, and in a second step the at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, and most preferably lipase, is brought into contact with the item to be washed or rinsed. In preferred embodiments, in a first step the at least one peptide according to the invention is brought into contact with the item to be washed or rinsed in the presence of at least one salt, and in a second step the at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, and most preferably lipase, is brought into contact with the item to be washed or rinsed.

[0230] In preferred embodiments, in a first step the at least one peptide is brought into contact with the material to be washed or rinsed, and in a second step the at least one lipase is brought into contact with the material to be washed or rinsed. where 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 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0, and / or; b) 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 peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence that has at least 80% and increasingly 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; and wherein the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical.

[0231] In preferred embodiments, in a first step the at least one peptide is brought into contact with the material to be washed or rinsed in the presence of at least one salt, and in a second step the at least one lipase is brought into contact with the material to be washed or rinsed, 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 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0, and / or; b) 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 peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence that has at least 80% and increasingly 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; where the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical; and the salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures, in particular

[0232] In various embodiments, the above-described method is characterized by the fact that it is 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 40°C, particularly preferably at about 20°C to about 30°C, and most preferably at about 20°C.

[0233] In various embodiments, the method described above is characterized in that the at least one salt is present in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, and particularly preferably about 1 to about 2 wt.%, wherein the salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0234] This includes both manual and machine-based methods, with machine-based methods being preferred due to their more precise controllability, for example, regarding the quantities used and contact times. Methods for cleaning textiles are generally characterized by the fact that, in several process steps, various cleaning agents are applied to the item to be cleaned and rinsed off after the contact time, or that the item to be cleaned is otherwise treated with a detergent or a solution or dilution thereof. Preferably, the method relates to a machine washing process, in particular in a washing machine, or a hand washing process. The peptide described herein preferably acts as a dirt-repellent and / or dirt-removing agent.

[0235] This invention also encompasses a machine dishwashing method. The dosage of the agent according to the invention into the cleaning solution can be achieved, for example, by means of the dosing chamber in the door or by means of an additional dosing container inside the dishwasher. Alternatively, the agent can also be applied directly to the soiled dishes or to one of the interior walls of the dishwasher, e.g., the inside of the door. The method according to the invention is carried out inside a standard dishwasher. The cleaning program of a dishwasher can generally be selected and set by the user before the dishwashing process begins. The dishwasher cleaning program used in the method according to the invention comprises at least one cleaning cycle.According to the invention, cleaning programs that include further cleaning or rinsing cycles, e.g., a pre-rinse and / or a final rinse cycle, are preferred. The method according to the invention is particularly advantageously integrated into a cleaning program comprising an optional pre-rinse cycle, a cleaning cycle, and a final rinse cycle. The method according to the invention is preferably used in conjunction with cleaning programs in which the cleaning solution is heated during the cleaning cycle.

[0236] Alternative embodiments of this invention also include methods for treating textile raw materials or for textile care, in which an agent or peptide according to the invention is activated in at least one process step. Methods for textile raw materials, fibers, or textiles with natural components are preferred, and especially for those containing wool or silk.

[0237] Another object of the invention is the use of an agent according to the invention for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, preferably in a temperature range of about 10°C to about 60°C, more preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0238] A further aspect of the invention is the use of a peptide described herein in a washing and / or cleaning agent according to the invention, preferably a lipase-containing washing and / or cleaning agent, to improve the cleaning performance of the agent on at least one greasy and / or oily soiling, where 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 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0, and / or; b) 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 peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence that has at least 80% and increasingly 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; and where the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical, preferably in a temperature range of about 10°C to about 60°C, more preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0239] Another aspect of the invention is the use of a peptide according to the invention as a dirt-removing, in particular grease- and / or oil-removing, active ingredient in a washing and / or cleaning agent, preferably in a lipase-containing washing and / or cleaning agent. where 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 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0, and / or; b) 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 peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence that has at least 80% and increasingly 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; and where the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical, preferably in a temperature range of about 10°C to about 60°C, more preferably about 15°C to about 40°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0240] The uses described above are characterized in various embodiments. characterized in that the composition contains at least one salt in an amount of about 0.001 to about 10 wt.%, preferably about 0.01 to about 5 wt.%, more preferably about 0.1 to about 3 wt.%, and particularly preferably about 1 to about 2 wt.%, wherein the salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride.

[0241] All facts, objects, and embodiments described for peptides and agents according to the invention are also applicable to these inventions. Therefore, explicit reference is made here to the disclosure at the relevant point, with the note that this disclosure also applies to the foregoing methods and uses according to the invention. PREFERRED EXECUTION FORMS 1. Washing and / or cleaning agents, including (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 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or b) 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 peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence that has at least 80% and increasingly 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; (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 2. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 3. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from 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 peptide has an amino acid sequence having the following sequence in N- to C-terminal orientation (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 4. Washing and / or cleaning agents, including (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 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or b) 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 peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence that has at least 80% and increasingly 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; (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 5. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 6. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from 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 peptide has an amino acid sequence having the following sequence in N- to C-terminal orientation (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 7. Agents according to point 1, 3, 4 or 6, wherein the peptide is according to point 1b, 3, 4b or 6 (i) has a total charge of 0 to +4, or (ii) if r ≥ 4 has a total charge of 0 to +4, or (iii) if r < 4 has a total charge of +1 to +4, preferably +2 or +3. 8. Means according to point 1, 3, 4, 6 or 7, wherein in the peptide according to point 1b, 3, 4b or 6, if o = 1, p = 0, 1 or 2, q = 2 and r = 4, the sequence (X 2 ) o[ (X 3 ) p (X 4 ) q ] r (X 5 ) s equal Z 1 Z 2 Z 3 [(Z 4 ) u Z 5 Z 6 ]3(Z 7 )v is, whereby Z 1 like X 2 defined and selected in point 1, 3, 4 or 6 is from R, H and K, preferably R, Z 2 , Z 3 , Z 5 and Z 6 like X 4 defined and selected in points 1, 3, 4 or 6 are from A, L and V, preferably A and L, Z 4 like X 3 defined in point 1, 3, 4 or 6 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 F, R, E, A, Q and W, u 1 or 2 is, Z 7 like X 5 defined in point 1, 3, 4 or 6 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 like s in point 1, 3, 4 or 6 and is an integer from 0 to 4. 9. Means according to point 8, 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. 10. Means according to point 8 or 9, wherein (i) the peptide comprises at least one motif selected from RAL and RLA, preferably RAL, wherein this sequence is preferably located in the N-terminal amino acids at positions 1-3; and / or (ii) the peptide comprises at least one motif selected from EAL and ELA, preferably EAL, wherein this motif is preferably not located in the N-terminal amino acids at positions 1-4; and / or (iii) the peptide comprises at least one motif selected from QAL and QLA, preferably QAL; and / or (iv) the peptide comprises the motif RAL and at least one of QAL or EAL, preferably both; and / or (v) the peptide comprises at least one, preferably two or three, motif(s) RAL; and / or (vi) the peptide comprises the motif RAL at least twice and at least one of QAL or EAL, preferably both. 11. Means according to point 1, 3, 4, 6 or 7, wherein in the peptide according to point 1b, 3, 4b or 6, if o = 1, p = 3-6, q = 1 or 2 and r = 2, the sequence (X 2 ) o[ (X 3 ) p (X 4 ) q ] r equal Z 11 (Z 12 )6Z 13 Z 14 (Z 15 ) w Z 16 is, where Z 11 like X 2 defined and selected in point 1, 3, 4 or 6 is from R, H and K, Z 12 like X 3 defined in point 1, 3, 4 or 6 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 like X 4defined and selected in points 1, 3, 4 or 6 are from A, L and V, preferably A and L, Z 15 like X 3 defined in point 1, 3, 4 or 6 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 R, K, E, S, Q and N, w is an integer from 3 to 6. 12. Means according to point 11, wherein, (i) Z 13 Z 14 selected from AL and LA, preferably AL; and / or (ii) (Z 15 ) w with w = 3-6, comprising a sequence that includes at least one positively charged amino acid (R, H, or K); and / or (iii) (Z 15 ) w with w = 3-6 comprising a motif selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, more preferably RQN; and / or (iv) Z 16 The selection is made from A and L, preferably A. 13. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably 6.0 to 13.0, and particularly preferably 6.5 to 12.0; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 14. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, and particularly preferably of -0.75 to +1.5; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 15. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 16. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 17. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably 6.0 to 13.0, and particularly preferably 6.5 to 12.0; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 18. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, and particularly preferably of -0.75 to +1.5; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 19. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 20. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or (B) at least one enzyme exhibiting hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and / or (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 21. Means according to any of points 1 to 20, wherein the peptide has an amino acid sequence that is 80% and increasingly preferentially 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: 1-31; and / or wherein the peptide has an amino acid sequence according to one of the amino acid sequences listed in SEQ ID NOs: 1-31, 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, further preferably SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29. 22. Means according to one of points 1 to 21, where the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and optionally (ii) at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256 has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical. 23. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256 (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 24. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T at at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256 (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 25. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 26. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 27. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 28. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 29. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 30. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 31. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 32. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; (B) at least one lipase, wherein the lipase is a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T; and (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 33. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0; (B) at least one lipase exhibiting lipolytic activity and comprising an amino acid sequence that is 100% identical over its entire length to the amino acid sequence specified in SEQ ID NO:33; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 34. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; (B) at least one lipase exhibiting lipolytic activity and comprising an amino acid sequence that is 100% identical over its entire length to the amino acid sequence specified in SEQ ID NO:33; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 35. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; (B) at least one lipase exhibiting lipolytic activity and comprising an amino acid sequence that is 100% identical over its entire length to the amino acid sequence specified in SEQ ID NO:33; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 36. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; (B) at least one lipase exhibiting lipolytic activity and comprising an amino acid sequence that is 100% identical over its entire length to the amino acid sequence specified in SEQ ID NO:33; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 37. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0; (B) at least one lipase exhibiting lipolytic activity and comprising an amino acid sequence that is 100% identical over its entire length to the amino acid sequence specified in SEQ ID NO:33; and (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 38. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; (B) at least one lipase exhibiting lipolytic activity and comprising an amino acid sequence that is 100% identical over its entire length to the amino acid sequence specified in SEQ ID NO:33; and (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 39. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; (B) at least one lipase exhibiting lipolytic activity and comprising an amino acid sequence that is 100% identical over its entire length to the amino acid sequence specified in SEQ ID NO:33; and (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 40. Washing and / or cleaning agents, including (A) at least one peptide, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; (B) at least one lipase exhibiting lipolytic activity and comprising an amino acid sequence that is 100% identical over its entire length to the amino acid sequence specified in SEQ ID NO:33; and (C) at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, further preferably 7.5 to 10.5, particularly preferably 8.0 to 10.0. 41. A composition according to any one of points 1 to 40, wherein the peptide binds to a greasy surface or a surface coated with grease or to a surface contaminated with at least one greasy and / or oily substance, wherein the surface is preferably selected from hard surfaces, more preferably containing or consisting of ceramic (e.g. porcelain, earthenware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the adhesion is determined as described in Example 2. 42. Means according to one of points 1 to 41, wherein the salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride 43. A means according to any one of points 1 to 42, wherein the means is preferably selected from textile detergent, machine dishwashing detergent, hand dishwashing detergent and hard surface cleaner. 44. A composition according to any of points 1 to 43, wherein the composition has at least two spatially separated compartments, wherein the peptide and optionally the salt are contained in a first compartment and the at least one lipase are contained in a second compartment. 45. Method for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, characterized in that in at least one process step a washing or cleaning agent according to one of points 1 to 44 is used. 46. ​​Method according to point 45, wherein in a first step the at least one peptide and optionally the salt is brought into contact with the item to be washed or rinsed and in a second step the at least one lipase is brought into contact with the item to be washed or rinsed. 47. Method according to point 45 or 46, wherein it is carried out in a temperature range of 10°C to 60°C, preferably 15°C to 40°C, particularly preferably 20°C to 30°C, most preferably 20°C. 48. Use of a product according to any of points 1 to 44 for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass. 49. Use of a peptide in a lipase-containing washing and / or cleaning agent according to any one of points 1 to 44 to improve the cleaning performance of the agent on at least one greasy and / or oily soiling, preferably greasy soiling, 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 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or b) 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 peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence (C) m (X 1 ) n (X 2 ) o [(X 3 ) p (X 4 ) q ] r (X 5 )s(C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence that has at least 80% and increasingly 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. 50. Use of a peptide in a lipase-containing washing and / or cleaning agent according to any of points 1 to 44 to improve the cleaning performance of the agent on at least one greasy and / or oily soiling, preferably greasy soiling, wherein the peptide is selected from a peptide having an amino acid sequence identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31. 51. Use of a peptide in a washing and / or cleaning agent, preferably a lipase-containing washing and / or cleaning agent, according to one of points 1 to 44 as a dirt-removing, in particular grease- and / or oil-removing, active ingredient in the agent, 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 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15.0, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1; and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and / or b) 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 peptide has an amino acid sequence which, in N- to C-terminal orientation, has the following sequence (C) m (X 1 ) n (X 2 )o [(X 3 ) p (X 4 ) q ] r (X 5 ) s (C) t where X 1 selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, further preferably G and I, X 2 selected from R, H and K, preferably R and K, 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, preferably A and L, X 5 selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, E and L. 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 from 0 to 2, r is an integer from 1 to 4, s is an integer from 0 to 4; and / or c) a peptide having an amino acid sequence that has at least 80% and increasingly 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. 52. Use of a peptide in a washing and / or cleaning agent, preferably a lipase-containing washing and / or cleaning agent, according to any one of points 1 to 44 as a dirt-removing, in particular grease- and / or oil-removing, active ingredient in the agent, wherein the peptide is selected from a peptide having an amino acid sequence identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31. 53. Use according to one of points 48 to 53, wherein the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical. 54. Use according to any one of points 48 to 54, wherein the lipase is selected from a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with respect to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) has at least one amino acid substitution at at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, selected from the group consisting of D27R, N33Q, G38A, G91Q, G91T, D96E, D111A, D254S, G163K, P208N, E210Q, F211N, T231R, N233R, P253N, I255A and P256T. 55. Use according to any of points 48 to 54 in a temperature range of 10°C to 60°C, preferably 15°C to 40°C, particularly preferably 20°C to 30°C, most particularly preferably 20°C. EXAMPLES Example 1: Peptide sequences

[0242] The peptides listed in Table 2 were produced by chemical synthesis. Table 2: Peptide names and associated amino acid sequences Peptide No . Amino acid sequence SEQIDNO Isoelectric point (calculated) Charge value at pH 8.0 (calculated) Charge value at pH 9.0 (calculated) Charge value at pH 10.0 (calculated) P1 HFVKTPARWAWG 1 11,40 +1,37 +1,02 +0,76 P2 IYASNHSHPASY 2 7,34 -0,60 -1,04 -1,66 P3 GHQGHWYGMFRA 3 9,03 +0,41 +0,01 -0,33 P4 SLAFMPAWHASR 4 10,02 +0,37 +0,05 +0,00 P5 HNHHQLALVESY 5 6,83 -1,56 -1,99 -2,33 P6 SQLFNSQRLAYS 6 9,00 +0,33 +0,00 -0,33 P7 WRHPRLRCGNLL 7 12,00 +1,43 +1,06 +0,99 P8 SRARLFVVTYHKC 8 10,38 +1,42 +0,98 +0,42 P9 HMISTMNAASRRC 9 9,89 +0,43 +0,06 +0,00 P10 RSIVTFSLRQNRC 10 12,00 +1,39 +1,05 +0,99 P11 RSIVTFSLRQNSEQAC 11 7,25 -0,61 -0,95 -1,00 P12 KSIVTFSLRQNRC 12 11,23 +1,39 +1,02 +0,76 P13 KSIVTFSLKQNRC 13 10,49 +1,39 +0,99 +0,52 P14 RALFRALFEALEALRC 14 7,25 -0,61 -0,95 -1,01 P15 RALFEALQALFRALEALC 15 5,65 -1,61 -1,95 -2,00 P16 RALRALFEALEALC 16 5,65 -1,61 -1,95 -2,00 P17 RALFEALFRALEALRC 17 7,25 -0,61 -0,95 -1,01 P18 RALEALFRALEALC 18 5,65 -1,61 -1,95 -2,00 P19 RALFRALWEALFEALC 19 5,65 -1,61 -1,95 -2,00 P20 RALFEALWRALFEALC 20 5,65 -1,61 -1,95 -2,00 P21 RALFEALFRALEALC 21 5,65 -1,61 -1,95 -2,00 P22 SHTWGSQATSSS 22 7,15 -0,63 -0,95 -0,99 P23 RALEALWRALEALC 23 5,65 -1,61 -1,95 -2,00 P24 RALRALQALEALEALC 24 5,65 -1,61 -1,95 -2,00 P25 RALRALQALQALEALC 25 7,25 -0,61 -0,95 -1,00 P26 RALRALQALQALEAELC 26 5,65 -1,61 -1,95 -2,00 P27 RALARALARALAQALAC 27 12,00 +1,39 +1,05 +0,99 P28 RALARALARALARALAC 28 12,30 +2,39 +2,05 +1,99 P29 RALRALRALEALEALC 29 7,25 -0,61 -0,95 -1,01 P30 RALQALRALQALEALC 30 7,25 -0,61 -0,95 -1,00 P31 RALRALEALQALEALC 31 5,65 -1,61 -1,95 -2,00 P32 INQDARTMVMVP 32 5,71 -0,67 -0,95 -1,00

[0243] The isoelectric point and charge values ​​were calculated using the Henderson-Hasselbalch equation, as described in Kozlowski, LP, “IPC - Isoelectric Point Calculator”. Biol Direct 11, 55 (2016), https: / / doi.org / 10.1186 / s13062-016-0159-9. The pKa values ​​used in the calculation were disclosed in Grimsley GR, Scholtz JM, Pace CN. “A summary of the measured pK values ​​of the ionizable groups in folded proteins”. Protein Sci. 2009 Jan;18(1):247-51. doi: 10.1002 / pro.19. PMID: 19177368; PMCID: PMC2708032. Example 2: Verification of peptide adhesion with respect to their substrate specificity on fats

[0244] In an initial experiment, the adhesion of various peptides to grease stains on textiles was measured using the fluorescamine method. The protein dye fluorescamine is a fluorescent dye used to quantify minute quantities of proteins and peptides in solution. The fluorescamine reagent reacts rapidly with primary amines.

[0245] The following pre-soiled textile swatches were used (e.g., CFT, Center For Testmaterial): C-FF CS46, Frying Fat, used, Cotton (Frying fat on cotton) P-FF PS46, Frying Fat, used, Polyester (Frying fat on polyester) CO2, Olive Oil with carbon black with thickening agent, Cotton (Olive oil on cotton) PO P02, Olive Oil with carbon black with thickening agent, Polyester (olive oil on polyester) CS CS32, Sebum Bey with Carbon black, Cotton (Sebum on cotton) PS PS32, Sebum Bey with Carbon black, Polyester (Sebum on Polyester)

[0246] For the investigation, three textile patches (each approximately 10 mm in diameter) were placed into the wells of a 48-well microtiter plate twice. 0.2 ml of peptide solution (0.02 mg / ml 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 patches served as controls. The microtiter plates were incubated for 1 h at 20°C with gentle shaking (750 rpm, Titramax). After incubation, 50 µl of supernatant from each well was transferred to wells of a black 96-well microtiter plate. 17 µl of fluorescamine solution (3 mg / ml in DMSO; Fluorescamine, ex. AcrosOrganics) was added and mixed for 15 min at 20°C. The fluorescence of the samples in the 96-well plate was measured in a biophotometer (Ex 260 nm, Em 465 nm).Since the fluorescence response is linearly dependent on the peptide concentration, the percentage adhesion of the peptide to the test material can be determined from the final and initial values ​​of the fluorescence.

[0247] The results are shown in Table 3. The higher the value, the better the adhesion of the peptide to the corresponding surface. Values ​​from 40% to 59% indicate moderate adhesion, values ​​from 60% to 79% indicate good adhesion, and values ​​above 79% indicate very good adhesion. Differences of 5% or more are considered significant. Table 3: Results of the adhesion peptide C-FF CO CS P-FF PO PS P1 97,3% 98,5% 98,3% 14,6% 89,0% 70,6% P2 80,6% 0,0% 60,3% 3,4% 0,0% 48,6% P3 97,3% 96,3% 98,4% 23,5% 79,7% 75,7% P4 89,0% 78,1% 93,9% 17,3% 44,7% 54,4% P5 77,3% 42,1% 74,9% 8,5% 26,4% 91,2% P6 67,5% 19,3% 84,6% 21,7% 42,6% 86,9% P7 98,0% 81,3% 69,7% 63,6% 92,5% 26,4% P8 100% 61,6% 64,4% 83,3% 71,5% 68,8% P9 93,8% 79,2% 90,9% 39,2% 78,5% 62,0% P10 99,2% 83,5% 85,5% 65,4% 78,5% 81,7% P11 76,4% 19,5% 57,3% 60,9% 35,8% 63,3% P12 88,9% 79,5% 81,6% 29,4% 75,9% 72,4% P13 91,6% 75,5% 77,1% 17,4% 70,4% 67,4% P14 100,0% 50,5% 1,6% 14,6% 100,0% 0,0% P15 67,4% 47,5% 38,2% 58,5% 47,4% 14,4% P16 46,2% 53,4% 39,4% 64,7% 49,7% 2,8% P17 94,5% 75,3% 57,7% 66,4% 63,6% 38,2% P18 54,2% 70,8% 61,0% 35,8% 62,4% 31,5% P19 95,6% 84,9% 7,6% 81,2% 58,0% 80,5% P20 91,3% 69,2% 33,5% 98,3% 53,5% 71,8% P21 81,2% 67,5% 52,1% 93,6% 71,4% 76,9% P22 77,6% 12,5% 0,0% 86,9% 18,9% 0,0% P23 72,2% 84,8% 79,0% 56,8% 39,5% 21,4% P24 72,0% 46,7% 66,7% 46,4% 31,4% 54,7% P25 90,9% 63,6% 57,5% 66,7% 97,6% 73,6% P26 87,7% 92,0% 83,0% 97,5% 90,6% 82,2% P27 92,1% 85,6% 83,0% 58,6% 100,0% 90,8% P28 100,0% 28,1% 14,7% 41,1% 52,5% 22,8% P29 80,7% 76,2% 56,5% 62,3% 78,9% 38,1% P30 71,7% 47,3% 47,5% 70,1% 45,1% 55,3% P31 33,6% 24,9% 26,8% 68,2% 69,6% 58,6% P32 0% 0% 0% 0% 0% 12,1%

[0248] All peptides P1 to P31 show good to very good adhesion to at least one greasy and / or oily soil on polyester and / or cotton textiles. The non-inventive peptide P32 shows no adhesion to greasy and / or oily soils. Examples 3 and 5: QCM-D measurement

[0249] The grease-dissolving effect was investigated using a quartz crystal microbalance with dissipation monitoring (QCM-D). This surface-sensitive method allows for the in-situ monitoring of adsorption and desorption processes of materials or substances (as well as associated processes, e.g., swelling) on ​​a sensor surface with ng resolution. The sensors used for this purpose consist of a thin quartz crystal disc surrounded by two metal electrodes. Due to the piezoelectric properties of quartz, it can be mechanically deformed when an external electrical 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, the resonance frequency f, the quartz sensor oscillates in resonance.Since the resonance frequency depends on the thickness of the disk, measuring temporal changes in the resonance frequency allows conclusions to be drawn about mass or layer thickness changes for the processes mentioned above. In addition to the change in the resonance 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. Viscoelastic models can be created by simultaneously measuring Δf and ΔD. In simple cases, i.e., for rigid, thin, and homogeneously distributed films firmly bonded to the quartz crystal surface, mass changes Δm due to adsorption and desorption processes can be calculated solely from the frequency change Δf (Sauerbrey equation; see, e.g., Snabe et al.).(2003), Lag phase and hydrolysis mechanisms of triacylglycerol film lipolysis, Chemistry and Physics of Lipids, 125: 69-82; QSense analysis documentation & manufacturer's instructions, available at: https: / / www.biolinscientific.com / qsense / instruments / qsense-pro#knowledge). Performing the QCM-D measurement:

[0250] The quartz sensors of the quartz crystal microbalance (QSense Analyzer, QSense Flow module QFM 401, ex. QSense®) were prepared for the investigation by cleaning the quartz sensors with a hydrogen peroxide-ammonia-millipore water solution (ratio 1:1:5) at 75°C,

[0251] After cleaning, the quartz sensors were coated with a model grease solution (1% Tricaprin in toluene, 50 µl at 75 rps) using spin coating. Spin-coating is a method known to those skilled in the art and allows the application of very thin substrate layers with a thickness of a few nm or mm (see, e.g., 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). This is carried out for all examples 3 to 5. Subsequently, the measuring cell was first filled, depending on the test series, with millipore water or with a buffered Tris / HCl solution (flow rate 50 µL / min), which additionally contained no or 5, 50, or 500 mmol / L potassium chloride, and the frequencies or dissipations of the fundamental tone or overtones of the grease-coated quartz sensor were measured in millipore water or the respective buffer at 20°C (baseline).(Termination criterion: time-constant values ​​for frequency or dissipation, i.e., the frequency or dissipation was determined over a time course at which the system has settled to a stable frequency or dissipation).

[0252] The peptide solution (peptide P2 or peptide P4) was then passed through at a flow rate of 50 µl / min, and the frequencies and dissipations of the fundamental tone and overtones of the grease-coated quartz sensors in the peptide solution were measured over time (termination criterion: constant values ​​for frequency and dissipation over time), see Example 3. The system was then rinsed again with the corresponding buffer system at the respective salt concentration.

[0253] To measure the fat-dissolving effect of peptide and lipase (Example 5), following the steps for peptide binding already described in the Procedure section, the measuring cell was briefly rinsed with the buffered Tris / HCl solution (pH 8.0 at 20 °C) (flow rate 50 µl / min). Subsequently, the lipase solution (lipase according to SEQ ID NO:33) was passed through at a flow rate of 50 µl / min, and the frequencies and dissipations of the fundamental and overtones of the grease-coated quartz sensors in the lipase solution were measured over time (termination criterion: constant values ​​for frequency and dissipation). Afterward, the cell was rinsed again with the corresponding buffer system at the respective salt concentration.

[0254] To restore the measuring cell, after each measurement is completely finished, it is rinsed with a 2% aqueous surfactant solution and then with millipore water. Evaluation principle of the QCM-D measurement:

[0255] The changes in the measured frequency values ​​(Δf) are to be interpreted as follows: Values ​​Δf < 0 mean that the sensor becomes heavier, i.e., material is adsorbed onto it, in this case the peptide on the fat layer. The larger the value, the more peptide mass binds to the fat on the sensor. Values ​​Δf > 0 mean that the sensor is becoming lighter, i.e., material is detaching from it, in this case the layer of grease. The larger the value, the more grease mass is detaching from the sensor. A value of 0 means that the mass of the sensor does not change (in this case, this is the mass of the grease-coated sensor).

[0256] Initially, the frequency (Δf) is lowered below the baseline (Δf = 0) by the added mass of the adhering peptide; that is, the peptide adheres or adsorbs to the fat applied to the sensor. Subsequently, the frequency (Δf) remains stable for several hours.

[0257] The adsorption rate of the peptide to the lipid layer can be determined from the temporal profile of the measured frequency values ​​(adsorption rate; Example 3). This is calculated from the abrupt change in frequency after peptide addition and the time required for this change (v). ads ,s). A continuous, but slower-acting peptide adsorption can be observed via further frequency changes and also related to the time required for it (v ads,l). If the frequencies and dissipations are constant over time, the experiment can be switched to the corresponding measuring solution (without peptide). If frequencies and dissipations are constant again, the experiment can be ended or started with lipase. In the latter case, the reaction times for the removal of the grease contamination / coating on the sensor can also be determined after the addition of lipase. The reaction time for grease removal is calculated from the difference between the time at which the frequency change begins after lipase addition (i.e., when lipase dissolves the grease layer from the sensor) and the time at which frequencies and dissipations are constant after lipase addition. Example 3: Adhesion of peptides to fat on hard surfaces:

[0258] Peptides P2 and P4 were tested as exemplary peptides. The adsorption rate of each peptide (P2 or P4) on the lipid surface was determined for 0 mM, 5 mM, 50 mM, and 500 mM KCl in 10 mM TRIS / HCl buffer at pH 8 by measuring the slope of the frequency jump after peptide addition (Hz / min).

[0259] In Fig. Figure 3 shows a QCM-D measurement with the addition of a peptide (as an example). As described above, a sudden frequency change can be observed after peptide addition as a function of time (v). ads ,s). Furthermore, slower peptide adsorption ((v ads ,l) observed. Table 4: QCM-D measurements with 10 µM peptide P2 or P4 in 10 mM TRIS / HCI buffer at pH 8.0 (mean values ​​from 3 measurements, harmonics 5, 7 and 9 were used) KCl[mmol / l] Adsorption velocity vads,s [Hz / min] P2 Adsorption rate vads,l[10 2 Hz / min] for P2 ratioΔD 1h / Δf 1h [10 -8 / H z ]for P2 Adsorption velocity vads,s [Hz / min] P4 Adsorption rate vads,l [10 -2 Hz / min] for P4 ratioΔD 1h / Δf 1h [10 -8 / Hz] for P4 0 0,1 3,2 4,6 0,9 4,0 3,4 5 0,3 5,3 5,8 1,0 5,2 4,4 50 0,5 5,1 5,6 0,8 5,6 5,9 500 0,5 5,9 6,4 0,8 5,5 7,1

[0260] It has been shown that adding a salt solution, such as a potassium chloride solution, improves the adhesion of peptides to the grease layer. The greater the adsorption rate, the faster the peptide binds to the grease surface. This is particularly important for technical applications in washing machines or dishwashers, ensuring that the peptide adheres to the grease surface as early and completely as possible. The subsequent interaction between lipase / peptide and the grease layer can then occur very quickly, while other interactions between the enzyme or peptide components and active substances can be avoided. Example 4: Measurement of the flow potential:

[0261] The sensors were spin-coated using the method described above and inserted into the gap measuring cell. The flow potential measurement was performed with 10 µM of peptide P2 or peptide P4 in 10 mM TRIS / HCl at pH 8.0 in the presence of 5 mM potassium chloride at 20 °C.

[0262] First, the zeta potential in mV is determined in the equilibrated state with buffer and saline solution (zeta potential without peptide). In the next step, the respective peptide is added. The zeta potential then shows a significant increase. For evaluation, the maximum value of the zeta potential after peptide addition is determined. However, up to this maximum value, the negative charges of the peptide also accumulate, which decrease the zeta potential again with ongoing peptide adsorption.

[0263] When the zeta potential no longer changes significantly or reaches a baseline (here approximately 50 minutes after peptide addition), the peptide end value of the flow potential is determined.

[0264] Fig. Figure 2 shows the flow potential measurement for an uncoated and coated gold sensor as a function of pH. The in Fig. The 1 graphically shown measured values ​​of the flow potential measurement (for peptide P2) were presented numerically in Table 5: Table 5: Flow potential measurement of peptide P2 or P4 in mV Zeta potential (mV) With 10 µM P2 at 5 mM KCl in TRIS / HCl pH 8 Zeta potential (mV) with 10 µM P4 at 5 mM KCl in TRIS / HCI pH 8 Zeta potential without peptide -56,7 -59,3 Zeta potential with peptide - maximum value -17,5 -16,5 Jump 1 -39,2 -42,8 Zeta potential with peptide - final value -47,4 -35,7 Jump 2 -29,9 -15,2

[0265] The difference between the maximum zeta potential value with peptide and the final value of the zeta potential (step 2) is considered. It is observed that different difference values ​​result depending on the charge value of the respective peptide at pH 8 (P2 (-0.6) or P4 (+0.37)). Example 5: Determining the fat-dissolving effect by combining peptide and lipase

[0266] Table 4 shows the reaction times in the QCM-D measurement with 10 µM peptide (P2 or P4) and without peptide and 20 µl lipase in 50 ml buffer solution (TRIS, pH 8.0) (lipase according to SEQ ID NO:33; concentration: 5.8 mg / ml total protein content, determined by BCA assay, pl=4.7). The mean values ​​from three measurements each are shown (harmonic tones 5, 7, and 9 were used to evaluate the reaction times). Table 6: Reaction time of fat removal peptide KCl [mmol / l] Response time [min] 0 5 81 Peptide P2 (10 µM) 5 75 Peptide P4 (10 µM) 5 71 0 50 34 Peptide P2 (10 µM) 50 21 Peptide P4 (10 µM) 50 22

[0267] As can be seen from the data, the fat dissolves more quickly when using the combination of peptide and lipase according to the invention. Surprisingly, the effect can be further improved by adding salt, in particular KCl.

[0268] The QCM-D measurements described above also correspond to observations that can be made with the naked eye. Before the coated quartz sensor is brought into contact with the peptide and lipase, or with the lipase alone, the presence of the grease layer is visible. After the measurement is complete, 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 invention can remove greasy and / or oily contaminants adhering to a surface. Example 6: Exemplary washing and cleaning agent formulations

[0269] The at least one peptide according to the invention can be used in various washing and cleaning agent compositions and achieve its effect. Table 7: Liquid detergents ingredient wt% active substance in the formulation A B C D E Demineralized water. rest rest rest rest rest LAS 5,5 20 5,5 21,7 23,5 FAEOS 7,0 - - - - Palm kernel oleic acid 3,0 8,0 - 7,0 7,4 FAEO 5,5 - - - - C 13 / 15 Oxoalcohol, 8 EO - 25 - - - C 12-18 Fettalkoholethoxylat, 7 EO - - - 22,4 23,4 Non-ionic surfactants - - 3,1 - - Soap - - 0,5 - - HEDP 0,5 - - - - DTPMP 7Na - 1,0 0,2 0,5 1,7 citric acid 2,5 - 0,23 - - NaOH 3,0 - 0,7 - - Glycerin 3,0 5,0 0,5 9,4 10,2 Ethanol 1,5 3,0 - - 3,2 1,2-Propanediol - 10,0 - 5,0 5,6 Monoethanolamine - 6,0 - 6,0 6,1 boric acid 1,0 - 0,5 - - Polyalkoxylated alkanolamine - - - 4,5 - Ethoxylated polyethyleneimine - - - 4,5 3,0 Peptides according to the invention 2,0 1,5 2,5 1,0 2,0 Lipase (active enzyme) 0,3 0,3 0,3 0,3 0,3 DTI, SRP, other enzymes, defoamers, etc. minors minors minors minors minors Table 8: Solid detergents ingredient wt% active substance in the formulation A B C LAS 12,2 12,0 10,1 Sodium fatty alcohol sulfate, C 12-18 4,2 - - Fatty alcohol, C 12-18 , 7 EO 4,1 2,3 1,5 Soap 0,4 - - Citrate 2,0 - - Sodium carbonate 2,4 17,9 25,1 Builder 23,0 7,0 7,6 Phosphonate 1,2 1,1 1,2 Carboxymethylcellulose 2,3 2,0 1,1 2 Na2 Carbonate 3 H2O2 18,5 15,8 - TAED 10,9 3,5 - Peptides according to the invention 2,0 1,0 0,5 Lipase (active enzyme) 0,3 0,3 0,3 Sodium sulfate, foam inhibitor, optical brightener, fragrances, other enzymes rest rest rest Table 9: Two-phase solid machine dishwashing detergents Powder phase (Phase A) Active ingredient content in wt.% (unless otherwise stated), based on the total weight of the powder phase A1 A2 Sodium percarbonate 13,0 15,0 Non-ionic surfactants 4,0 4,0 sulfonic acid group-containing polymer 4,0 4,0 HEDP (sodium salt) 6,0 6,0 Sodium carbonate (including sodium hydrogen carbonate) 24,0 28,0 Layered silicate 4,0 4,0 Sodium citrate (calculated as anhydrous sodium citrate) 21,0 21,0 Amylase (Stainzyme® Plus 24 Evity T; percentage by weight based on the amount of preparation used, tq) 1,5 1,5 Lipase (total active protein) 40 mg / job 40 mg / job Protease (total active protein) 40 mg / job 40 mg / job Misc (including perfume, dyes, preservatives, fillers e.g. sodium sulfate, bleach catalyst (MnTACN), bleach activator (TAED), zinc acetate, silver protectant, other enzymes) Add 100 Add 100 Peptides according to the invention 0,75 0,75 Gel phase (Phase B) Active ingredient content in wt.% (unless otherwise stated), based on the total weight of the gel phase B1 B2 Polymer comprising monomers containing acrylic acid and amidopropylsulfonic acid 10,0 11,0 Glycerin 27,0 25,0 1,3-Propanediol 30,0 30,0 PEG 400 15,0 17,0 PVOH 15,0 14,0 Misc (including process aids, pH adjusters, perfume, dye) Ad 100 Ad 100 Phases A1 and A2, and phases B1 and B2, can be combined in any way. Total weight of both phases in a single serving is 18.5 g. Table 10: Solid machine dishwashing detergents ingredient (Active substance content in wt.%, based on total weight) framework recipe Example recipe 1 Example recipe 2 Sodium citrate 0,0-30,0 22,0 0,0 Sodium percarbonate 10,0-15,0 15,0 15,0 Aminopolycarboxylate, preferably MGDA, trisodium salt 0,0-25,0 0,0 12,0 Non-ionic surfactants 2,0-10,0 4,0 4,0 sulfonic acid group-containing polymer 5,0-10 2,5 3,0 HEDP (sodium salt) 2,5-7,5 4,5 4,8 Sodium carbonate (including sodium hydrogen carbonate) 12,5-25,0 20,0 20,0 Sodium disilicate 5,0-15,0 5,0 5,0 TAED 2,0-3,0 2,5 2,5 Peptides according to the invention 0,0001-5,0 2,5 2,5 Protease (total active protein) 0,0001-3,0 0,5 0,5 Amylase (total active protein) 0,0001-3,0 0,1 0,1 Lipase (total active protein) 0,0001-3,0 0,1 0,1 Misc (including perfume, dyes, preservatives, processing aids, pH adjusters, fillers e.g. sodium sulfate, bleach catalyst (MnTACN), bleach activator (TAED), zinc acetate, silver protectant, other enzymes) Ad 100 Ad 100 Ad 100 Table 11: Single-phase liquid machine dishwashing detergents ingredient wt% active substance i...

Claims

[1] Washing and / or cleaning agents, including (A) at least one peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5, and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1, and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.0; and (B) at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, especially preferably lipase; and (C) optionally at least one salt, preferably in an amount of 0.001 to 10 wt.%, more preferably 0.01 to 5 wt.%, further preferably 0.1 to 3 wt.%, particularly preferably 1 to 2 wt.%, wherein the agent in a 1 wt.% solution in deionized water at 20°C preferably has a pH value in the range of 6.0 to 11.5, more preferably 7.0 to 11.0, more preferably 7.5 to 10.5, particularly preferably 8.0 to 10.

0. [2] Composition according to claim 1, wherein the peptide has an amino acid sequence which is 80% and increasingly 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% identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31; and / or wherein the peptide has an amino acid sequence according to one of the amino acid sequences listed in SEQ ID NOs: 1-31, 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, further preferably SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29. [3] Composition according to any one of claims 1 to 2, wherein the lipase is selected from (a) a lipase having lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical. [4] Composition according to any one of claims 1 to 3, wherein the salt is selected from (a) Alkali and / or alkaline earth metal salts, in particular alkali metal salts; and / or (b) Lithium chloride, lithium sulfate, lithium nitrate, lithium formate, lithium acetate, lithium propionate, lithium lactate, sodium chloride, sodium sulfate, sodium nitrate, sodium formate, sodium acetate, sodium propionate, sodium lactate, potassium chloride, potassium sulfate, potassium nitrate, potassium formate, potassium acetate, potassium propionate, potassium lactate, magnesium chloride, magnesium sulfate, magnesium nitrate, magnesium formate, magnesium acetate, magnesium propionate, magnesium lactate, calcium chloride, calcium sulfate, calcium nitrate, calcium formate, calcium acetate, calcium propionate, calcium lactate and mixtures thereof, in particular lithium chloride, sodium chloride, potassium chloride and mixtures thereof, preferably sodium chloride and / or potassium chloride. [5] A composition according to any one of claims 1 to 4, wherein the peptide binds to a fatty surface or to a surface coated with grease or to a surface provided with at least one fatty and / or oily soiling, wherein the surface is preferably made of hard surfaces, more preferably containing or consisting of ceramic (e.g. porcelain, stoneware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surfaces, wood, laminate, linoleum and mixtures thereof, particularly preferably tableware (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the adhesion is determined as described in Example 2. [6] Composition according to any one of claims 1 to 5, wherein the composition is preferably selected from textile detergent, machine dishwashing detergent, hand dishwashing detergent and hard surface cleaner. [7] Composition according to any one of claims 1 to 6, wherein the composition has at least two spatially separated compartments, wherein the peptide, and optionally at least one salt, is contained in a first compartment and the at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, is contained in a second compartment. [8] Methods for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass, characterized by, that in at least one process step a washing or cleaning agent according to one of claims 1 to 7 is used. [9] Method according to claim 8, wherein in a first step the at least one peptide and optionally at least one salt is brought into contact with the item to be washed or rinsed and in a second step the at least one enzyme having hydrolytic activity on an ester bond, preferably selected from lipase and esterase, in particular esterase with lipolytic activity, particularly preferably lipase, is brought into contact with the item to be washed or rinsed. [10] Method according to claim 8 or 9, wherein it is carried out in a temperature range of 10°C to 60°C, preferably 15°C to 40°C, particularly preferably 20°C to 30°C, most preferably 20°C. [11] Use of an agent according to any one of claims 1 to 7 for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or stoneware as well as plastic), metal (e.g. cutlery or pots) or glass. [12] Use of a peptide in a lipase-containing washing and / or cleaning agent according to any one of claims 1 to 7 to improve the cleaning performance of the agent on at least one greasy and / or oily soiling, preferably greasy soiling, wherein the at least one peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.

0. [13] Use of a peptide in a washing and / or cleaning agent, preferably a lipase-containing washing and / or cleaning agent, according to any one of claims 1 to 7 as a dirt-removing, in particular grease- and / or oil-removing, active ingredient in the agent, wherein the peptide is selected from a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 10 to 18 amino acids, wherein i) the peptide has an isoelectric point of 5.0 to 15, preferably of 6.0 to 13.0, particularly preferably of 6.5 to 12.0, and / or ii) the peptide has a charge value at pH 8 of -3.0 to +3.0, preferably of -1.0 to +2.0, particularly preferably of -0.75 to +1.5; and / or iii) the peptide has a charge value at pH 9 of -3.0 to +3.0, preferably of -1.5 to +1.5, particularly preferably of -1.1 to +1.1 and / or iv) the peptide has a charge value at pH 10 of -3.0 to +3.0, preferably of -2.0 to +2.0, particularly preferably of -1.8 to +1.

0. [14] Use according to one of claims 12 or 13, wherein the lipase is selected from a) a lipase exhibiting lipolytic activity and comprising an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:33 over its entire length to at least 70% and increasingly preferably 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%, in each case with reference to the numbering according to SEQ ID NO:33, (i) at positions corresponding to positions 231 and 233, the amino acid substitutions T231R and N233R and (ii) optionally, at least one of the positions corresponding to positions 27, 33, 38, 91, 96, 111, 163, 208, 210, 211, 231, 233, 253, 254, 255 and 256, has at least one amino acid substitution selected from the group consisting of 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 that corresponds to the amino acid sequence specified 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 over its total length by at least 70% and increasingly preferably by 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% identical. [15] Use according to any one of claims 11 to 14 in a temperature range of 10°C to 60°C, preferably 15°C to 40°C, particularly preferably 20°C to 30°C, most particularly preferably 20°C.

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