Peptides for adhesion to grease and use thereof for removing grease-containing stains from surfaces

Abstract

The invention relates to the use of substrate-specific peptides for adhesion to a grease- and / or oil-containing surface, in particular to grease- and / or oil-containing stains on a surface, wherein the surface is selected from hard surfaces and / or textiles. The invention further relates to agents, preferably detergents and / or cleaning agents, comprising at least one peptide described herein, to methods for cleaning hard surfaces and / or textiles, and to the use of peptides described herein as dirt-removing active ingredients, in particular grease- and / or oil-removing active ingredients, for cleaning textiles and / or hard surfaces.

Description

[0001] PEPTIDES FOR ADHESION TO FAT AND THEIR USE FOR THE REMOVING GREASY SOILS FROM SURFACES

[0002] DESCRIPTION

[0003] The invention relates to the use of substrate-specific peptides for adhesion to a fat- and / or oil-containing surface or to a surface coated with fat and / or oil or to a surface provided with at least one fat- and / or oil-containing soil, wherein the surface is selected from hard surfaces, more preferably surfaces 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 textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof.Furthermore, the invention relates to agents, preferably washing and / or cleaning agents, comprising at least one peptide described herein, to methods for cleaning hard surfaces and / or textiles, and to the use of peptides described herein as dirt-removing, in particular fat- and / or oil-removing, active ingredients in cleaning textiles and / or hard surfaces.

[0004] Intensive research is being conducted into the development of adhesive peptides. In particular, peptides that specifically bind to or interact with oxidic surfaces such as metal surfaces, as well as peptides that specifically bind to plastic surfaces, have already been described (WO 2014 / 072313 A1, WO 2023 / 110572 A1). Adhesive peptides are also of interest for many other surfaces, particularly for functionalizing such surfaces or imparting other desired properties.

[0005] It is known to use so-called "functional polymers" in detergents and cleaning agents, such as "soil release polymers" in detergents to improve soil removal from textiles or "soil repellent polymers" in detergents to prevent / reduce dirt build-up on textiles. Such 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 ability of oil and grease to be washed out of textiles. Typical SRPs are based, for example, on copolymers of polyester and polyether, also terephthalate, e.g., polypropylene terephthalate. However, these polymers are not biodegradable. Therefore, there is a need for alternative or improved, particularly biodegradable SRPs for use in detergents and cleaning agents, and / or alternatives thereto.The dispersant polymers used in automatic dishwashing detergents fulfill similar functions to prevent or reduce soil buildup. These are typically (co)polymeric polycarboxylates, such as poly(meth)acrylates or sulfonic acid-containing polymers based on (meth)acrylic acid. However, the biodegradability of such polymers has so far been limited, so readily biodegradable alternatives are being sought for dishwashing detergents.

[0006] Grease and / or oily soils on hard surfaces and / or textiles are among the more stubborn types of soiling that are not easy to remove. In conventional washing and / or cleaning processes, such soils are removed by first liquefying the fats due to the washing and / or cleaning temperature, usually between approximately 40°C and approximately 60°C, and then detaching them from the surface by surfactants contained in the washing and / or cleaning agents ("roll-up mechanism"). The detached, liquefied fat molecules are then carried away, i.e., rinsed away, by mechanical forces during the washing and / or rinsing process. Additionally or alternatively, grease and / or oily soils can be removed by esterases, lipolytic enzymes, or lipases, in which the enzyme breaks down the fats and / or oils, and the degradation products are then in turn washed away or rinsed away.However, there is currently no satisfactory alternative for removing grease and / or oily soiling at low temperatures, ie at temperatures below 40°C, particularly at, for example, about 20°C or about 30°C, since the greases do not liquefy or only insufficiently liquefy at temperatures below about 30°C or about 40°C.

[0007] The inventors have discovered and developed special peptides which are surprisingly suitable for adhesion to fatty and / or oil-containing surfaces as described herein and which also enable the removal of at least one fatty and / or oil-containing soil from surfaces.

[0008] In the context of the present invention, a "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 soiled with at least one fatty and / or oily soil. In the context 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. Furthermore, according to the invention, all known fatty acids having 8 to 36, preferably 10 to 24, carbon atoms, both mono- and polyunsaturated and saturated fatty acids, are encompassed. In the context of the present invention, "oil" or "oils" are understood to mean fatty acids that are liquid or soluble at room temperature.Flowable, fatty substances that do not mix with water are understood. Both synthetic and bio-based fats and / or oils are encompassed within the scope of the invention. Within the scope of the present invention, "fatty and / or oily soiling" is understood to mean soiling on a surface, in particular a hard surface and / or textile surface, that contains or consists of a fat and / or oil. Examples of typical fat and / or oily soiling include fat and / or oily food and food residue soiling, such as vegetable fats (e.g., coconut fat), 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), even burnt-in food residues, and / or synthetic fats and / or oils, such as, for example,Mineral oil(s) and / or greases, engine oil, bicycle chain oil, pigment greases, pigment oils, and / or fats and / or oils from personal care products, such as lipstick, make-up, lotion, cream, and / or body fat deposits, such as sebum, tallow. In preferred embodiments, the fatty surface contains or consists of a fat that is solid at room temperature. In preferred embodiments, the surface coated with fat is coated with a fat that is solid at room temperature. In preferred embodiments, the surface provided with at least one fatty soil is provided or soiled with at least one solid fat, ie the at least one fatty soil preferably contains or consists of a fat that is solid at room temperature.

[0009] In the context of the present invention, the fat- and / or oil-containing surface and / or the surface coated with fat and / or oil and / or the surface provided with at least one fat- and / or oil-containing soil is preferably selected from hard surfaces and / or textiles.

[0010] Preferably, the greasy and / or oil-containing surface and / or the surface coated with greasy and / or oil and / or the surface provided with at least one greasy and / or oil-containing soiling is a hard surface containing or consisting of ceramic (e.g. porcelain, earthenware), metal, steel, stainless steel, plastic, glass, natural and artificial stone, painted and enamelled surface, wood, laminate, linoleum and mixtures thereof, particularly preferably crockery (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass.

[0011] Preferably, the fat- and / or oil-containing surface and / or the surface coated with fat and / or oil and / or the surface provided with at least one fat- and / or oil-containing soil 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 can be in the form of knits, wovens, denims, nonwovens, felts, yarns, and terry cloth. The textile can be cellulose-based, such asNatural cellulose fibers such as cotton, flax / linen, jute, ramie, sisal, or coconut fibers, or man-made cellulose fibers (e.g., from wood pulp) such as viscose / rayon, cellulose acetate fibers (Tricell), lyocell, or blends thereof. The textile or fabric can also be made 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 blends thereof, as well as blends of cellulose fibers and non-cellulose fibers. Examples of blends are 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 cellulosic 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 term "fabric" or "garment" is used, it is intended to include the broader term "textiles." Textiles containing or consisting of cotton, polyester, polyamide, polypropylene, and mixtures thereof are preferred, with cotton, polyester, and mixtures thereof being particularly preferred.

[0012] By the adhesion of substrate-specific peptides to fat- and / or oil-containing surfaces, in particular fat-containing surfaces as defined herein, ieFunctional groups can be selectively bound to the fat and / or oil molecules on a surface containing fat and / or oil, in particular a surface containing fat and / or oil, and / or to a surface coated with fat and / or oil, in particular to a surface coated with fat, and / or to a surface provided with at least one fat and / or oil-containing soiling, in particular to a surface provided with at least one fat-containing soiling, preferably to a hard surface and / or textile containing fat and / or oil, in particular a surface and / or textile containing fat and / or oil, and / or to a hard surface and / or textile coated with fat and / or oil, in particular a surface and / or textile coated with fat and / or oil, and / or to a hard surface and / or textile provided with at least one fat and / or oil-containing soiling, in particular to a hard surface and / or textile provided with at least one fat-containing soiling.Furthermore, surfaces described herein can be coated using the substrate-specific peptides, so that the surface can be given new, desired properties. A further advantage of the functionalization of surfaces described herein can also bring about a substrate-specific removal of soiling. Thus, peptides that specifically bind to fats and / or oils, preferably solid fats, or fat- and / or oil-containing soils, preferably fat-containing soils, on surfaces can be used to specifically remove these fats and / or oils, in particular solid fats, from the surface. Possible application examples include, for example, the use in washing and / or cleaning agents for cleaning hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or earthenware, as well as plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, preferably containing or consisting of cotton, polyester, and mixtures thereof. Adhesion-promoting peptides can also be used as anchors for other peptides, polypeptides, or enzymes, whereby these other peptides, polypeptides, or enzymes may have a different function.

[0013] The invention therefore relates in a first aspect to the use of a peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.Cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence.

[0014] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0015] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0016] X 2 is selected from R, H and K, preferably R and K,

[0017] X 3is 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,

[0018] X 4 is selected from AL and V, preferably A and L,

[0019] X 5 is 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; or b) a peptide having an amino acid sequence which 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 any of the amino acid sequences set out in SEQ ID NOs: 1-31.

[0020] In a further aspect, the invention relates to the use of an agent, preferably a washing and / or cleaning agent, comprising at least one peptide, for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soiling and / or for removing at least one, preferably two or more, greasy and / or oily soiling(s) from a surface and / or for improving the cleaning performance of the agent on at least one, preferably two or more, greasy and / or oily soiling(s) on a surface, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, more preferably cotton, polyester and mixtures thereof, wherein the at least one peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which has the following sequence in N- to C-terminal orientation.

[0021] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5)s(C)t where

[0022] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0023] X 2 is selected from R, H and K, preferably R and K,

[0024] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0025] X 4 is selected from AL and V, preferably A and L,

[0026] X 5is 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; or b) a peptide having an amino acid sequence which 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 any of the amino acid sequences set out in SEQ ID NOs: 1-31.

[0027] In still further aspects, the invention relates to preferred embodiments of the aforementioned uses as described herein. In preferred embodiments, the peptide used according to the invention 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, preferably the peptide has an amino acid sequence according to one of the amino acid sequences mentioned 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, particularly preferred SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0028] In a further aspect, the invention also relates to a peptide used according to the invention for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the peptide is as defined in any one of the preceding claims, and wherein the adhesion is determined as described in Example 2.

[0029] Furthermore, the invention relates to an agent, in particular a washing and / or cleaning agent, which comprises one or more of the peptides according to the invention.

[0030] Further objects of the invention relate to the

[0031] • Use of an 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 earthenware and plastic), metal (e.g. cutlery or pots) or glass, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C; and / or

[0032] • Use of a peptide described herein as a soil-removing, in particular grease- and / or oil-removing, active ingredient in a washing or cleaning agent, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C; and / or

[0033] • Use of a peptide described herein for improving the cleaning performance of a washing or cleaning agent on at least one fatty and / or oil-containing soil, preferably fatty soil, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0034] These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art from a study of the following detailed description and claims. Any feature of one aspect of the invention may be employed in any other aspect of the invention. Furthermore, it is to be understood that the examples contained herein are intended to describe and illustrate the invention, but not to limit it, and in particular, the invention is not limited to these examples.

[0035] Unless otherwise stated, all percentages are by weight (wt%), based on the total weight of the corresponding composition or agent.

[0036] Numerical ranges specified in the format "from x to y" include the specified values. If multiple preferred numerical ranges are specified in this format, it goes without saying that all ranges resulting from the combination of the different endpoints will also be included.

[0037] "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. With reference to an ingredient, the statement refers to the type of ingredient and not to the absolute number of molecules. "At least one peptide" thus means, for example, at least one type of peptide, i.e., one type of peptide or a mixture of several different peptides can be meant. Together 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 this type beyond the stated amount of the corresponding compounds.

[0038] "Approximately" or "approximately" as used herein with reference to numerical values ​​means the corresponding value ±10%, preferably ±5%.

[0039] The term "washing and cleaning agent" or "washing or cleaning agent" as used herein refers to a composition for cleaning textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, as explained in the description.

[0040] "Liquid," as used herein, includes liquids and gels, as well as pasty compositions. It is preferred that the liquid compositions be flowable and pourable at room temperature, but it is also possible that they have a yield point.

[0041] For the purposes of the invention, the term "room temperature" refers, unless explicitly stated otherwise, to 20°C at 1,013 mbar. A substance, e.g., a composition or agent, is solid according to the definition of the invention if it exists in the solid state at 20°C and 1,013 mbar.

[0042] A substance, e.g., a composition or agent, is liquid according to the invention's definition if it exists in the liquid state at 20°C and 1,013 mbar. Liquid also includes gel.

[0043] The term "N-terminus" or "N-terminal" in the context of the present invention typically describes the end of the amino acid chain of a peptide which has a free amino group.

[0044] The term "C-terminus" or "C-terminal" in the context of the present invention typically describes the end of the amino acid chain of a peptide which has a free carboxyl group.

[0045] The term "in N- to C-terminal orientation" in the context of this invention refers to an amino acid sequence in which the order of the amino acids is described starting from the N-terminus to the C-terminus.

[0046] When reference is made herein to various linked or individual amino acid sequences, these are always shown in 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.

[0047] 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-promoting" refers to the ability, under suitable conditions, i.e., usually non-denaturing conditions, to interact with and / or adhere to various surfaces, e.g., textile surfaces, in particular those containing or consisting of cotton, polyester, and mixtures thereof, or hard surfaces, such as, in particular, tableware (preferably made of ceramic such as porcelain or earthenware, as well as plastic), metal (e.g., cutlery or pots), or glass. "Fat-binding peptides," as used herein, mean that the peptide binds to fat, e.g., to at least one fatty and / or oily soil on a surface.In preferred embodiments, the binding affinity is greater than that of a reference sequence or a reference molecule that does not exhibit adhesion-promoting properties. The lipid-binding peptides described herein preferably exhibit 10-fold, 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). The term "binding" in the context of this invention preferably refers to "covalent bonds" between the peptide and a surface.A peptide is, in the sense of the invention, a fat-binding peptide in particular 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 soiling on a surface is demonstrated, wherein the binding affinity is greater than that of a reference molecule (peptide according to SEQ ID NO: 32). The invention relates to the use of a peptide for adhesion to a fat-containing surface or to a surface coated with fat or to a surface provided with at least one fat- and / or oil-containing soiling, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, more preferably cotton, polyester and mixtures thereof, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence.

[0048] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0049] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0050] X 2 is selected from R, H and K, preferably R and K,

[0051] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0052] X 4 is selected from A, L and V, preferably A and L,

[0053] X 5is 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; or b) a peptide having an amino acid sequence which 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 any of the amino acid sequences set out in SEQ ID NOs: 1-31.

[0054] A "peptide" in the context of the present invention is understood to mean a polymer composed of amino acids, preferably the 20 proteinogenic L-amino acids, preferably of a linear structure, which has up to 100 amino acids linked to one another via peptide bonds. According to the invention, the peptides of the invention have an amino acid sequence of 4 to 50 amino acids. The amino acids are specified in the context of this invention in a one-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 represents a cysteine ​​residue. It is further understood that, unless otherwise stated, the amino acids in an amino acid sequence disclosed herein are linked via peptide bonds and, unless otherwise stated, the sequence is listed in N- to C-terminal orientation.

[0055] Table 1: Proteinogenic amino acids

[0056] 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. References herein to "any" amino acids typically refer to one of the 20 naturally occurring proteinogenic amino acids (Table 1).

[0057] Unless otherwise stated, 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.

[0058] In various embodiments, the peptide used according to the invention has a total charge of 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 positively and negatively charged amino acids in the peptide, in particular R, K, H, D and E, and results from the sum of the negative and positive charges, with one positive and one negative charge canceling each other out. A peptide with 2 R residues and 1 E residue would therefore have a total charge of +1. In preferred embodiments, the total charge of the peptide is 0 to +4.

[0059] In various embodiments, the peptide used according to the invention

[0060] (a1) has a total charge of 0 to +4, or

[0061] (a2) if r > 4, has a total charge of 0 to +4, or

[0062] (a3) if r < 4, has a total charge of +1 to +4, preferably +2 or +3.

[0063] In various embodiments,

[0064] (b) the N-terminus comprising the first 1-5 amino acids has a positive net charge; and / or (c1) the C-terminus comprising the last 1-5 amino acids has a negative net charge, so 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

[0065] (c2) the C-terminus comprising the last 1-5 amino acids has a neutral net charge, so 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

[0066] (c3) the C-terminus comprising the last 1-5 amino acids has a positive net charge, so 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.

[0067] All of the above features can be implemented individually or in any combination.

[0068] The feature that the peptide has a positive net charge at the N-terminus comprising the first 1-5 amino acids means that the N-terminal 1-5 amino acids comprise more positively charged than negatively charged amino acids. In various embodiments, this feature is met, for example, when the N-terminal 1-5 amino acids comprise 1 or 2 positively charged amino acids, i.e., H, K, or R, preferably K or R, 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 2 for the net charge to remain positive.

[0069] The feature that the peptide has a negative 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 charged amino acids, i.e., D and E, must be greater than the number of positively charged amino acids. In various embodiments, this feature is met, for example, if the C-terminal 1-5 amino acids, i.e., within the last 5 amino acids at the C-terminus, have 1 or 2 negatively charged amino acids, i.e., D or E, and no positively charged amino acids, i.e., H, K, or R. An example of such a C-terminal sequence would be, for example, EAL or the double sequence of this motif.

[0070] For the feature that the peptide has a neutral net charge at the C-terminus comprising the last 1-5 amino acids, this means that the number of charged amino acids must be 0 or the number of negatively and positively charged amino acids must be equal.

[0071] In various embodiments, the peptide used according to the invention 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

[0072] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0073] X 2 is selected from R, H and K, preferably R and K,

[0074] X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V,

[0075] X 4 is selected from A, L and V, preferably A and L,

[0076] X 5is 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.

[0077] In various embodiments, in a peptide used according to the invention, 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 equals Z 1 Z 2 Z 3 [(Z 4 )uZ 5 Z 6 ]3(Z 7 ) v , where

[0078] Z 1 like X 2 defined above and selected from R, H and K, preferably R,

[0079] Z 2 , Z 3 , Z 5 and Z 6 like X 4defined above and selected from A, L and V, preferably A and L, Z 4 like X 3 defined above 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 is 1 or 2,

[0080] Z 7 like X 5 defined above and selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and v as s is defined above and is an integer from 0 to 4.

[0081] In various embodiments

[0082] (i) if u = 1 , Z 4 selected from R, E and Q, or

[0083] (ii) if u = 2, (Z 4 )2 selected from FR, FE, AR, WE, WR and AQ.

[0084] In various embodiments, the peptide used according to the invention comprises

[0085] (i) at least one motif selected from RAL and RI_A, preferably RAL, and wherein this sequence is preferably located in the N-terminal amino acids of positions 1-3; and / or

[0086] (ii) at least one motif selected from EAL and ELA, preferably EAL, and wherein this motif is preferably not located in the N-terminal amino acids of positions 1-4; and / or

[0087] (iii) at least one motif selected from QAL and QI_A, preferably QAL; and / or

[0088] (iv) the motif RAL and at least one of QAL or EAL, preferably both; and / or

[0089] (v) at least one, preferably two or three, RAL motif(s); and / or

[0090] (vi) the motif RAL at least twice and at least one of QAL or EAL, preferably both.

[0091] In various embodiments, the peptide used according to the invention comprises a motif selected from RAL, RSI, and RLA, preferably RAL and RLA, more preferably RAL. The N-terminal sequence RAL or RLA not only advantageously has a positive net charge, it also comprises amino acids with a particularly high α-helix-forming potential. In various embodiments, the R residue can also be replaced by K, but the N-terminal R residue is particularly preferred.

[0092] In various embodiments, the peptide used according to the invention 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, W and 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.

[0093] In various embodiments, the peptide used according to the invention 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, more preferably E, A, L, M, Q, K, R, F, I and H, particularly preferably E, A, L, M, Q, K, R and H.

[0094] In various embodiments, the peptide used according to the invention 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 used according to the invention can contribute to the stability of the helical structure because these amino acids have a high α-helix potential.

[0095] In various embodiments, in a peptide used according to the invention, when o = 1, p = 3-6, q = 1 or 2 and r = 2, the sequence (X 2 )0[(X 3 ) P (X 4 ) q ]r equals Z 11 (Z 12 )6Z 13 Z 14 (Z 15 ) W Z 16 , where

[0096] Z11 like X 2 defined above and selected from R, H and K,

[0097] Z 12 like X 3 defined above 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 defined above and selected from A, L and V, preferably A and L, Z 15 like X 3 defined above 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.

[0098] In various embodiments, a peptide used according to the invention

[0099] (i) Z is 13 Z 14 selected from AL and LA, preferably AL; and / or

[0100] (ii) includes (Z 15 ) wwith w = 3-6 a sequence comprising at least one positively charged amino acid (R, H or K); and / or

[0101] (iii) includes (Z 15 ) w with w = 3-6 a motif selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, more preferably RQN; and / or

[0102] (iv) Z is 16 selected from A and L, preferably A.

[0103] In various embodiments, the peptide used according to the invention 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. In various embodiments, the proportion of hydrophobic amino acids, ie the number of hydrophobic amino acids, based on the number of all amino acids of the peptide, is at least 30%, preferably at least 40%, more preferably at least 50% and particularly preferably at least 60%. In various embodiments, the proportion of hydrophobic amino acids in the peptide is at least 30% and increasingly preferably at least 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69% or 70%.In various embodiments, at least three, preferably at least four hydrophobic amino acids, in particular those selected from A, L, F, W, V, M and I, are located next to one another in the peptide sequence. In various embodiments, the proportion of hydrophobic amino acids, i.e. the number of hydrophobic amino acids, based on the number of all amino acids of the peptide, is at least 30%, preferably at least 40%, more preferably at least 50%, particularly preferably at least 60%, and at least three, preferably four hydrophobic amino acids, in particular those selected from A, L, F, W, V, M and I, are located next to one another in the peptide sequence. In various embodiments, the peptide used according to the invention has an amino acid sequence which has a length 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 12 to 18 amino acids.

[0104] In various embodiments, the peptide used according to the invention has an amino acid sequence which 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, and the proportion of hydrophobic amino acids, ie the number of hydrophobic amino acids, based on the number of all amino acids of the peptide, is at least 30%, preferably at least 40%, more preferably at least 50%, particularly preferably at least 60%, and there are at least three, preferably four hydrophobic amino acids, in particular those selected from A, L, F, W, V, M and I, next to one another in the peptide sequence.

[0105] In various embodiments, the peptide used according to the invention has the amino acid cysteine ​​(C) at the C-terminus. In various embodiments, the peptide used according to the invention has the amino acid cysteine ​​at the N-terminus. This amino acid can enable coupling to other molecules, structures, or substrates via the free sulfhydryl group. This amino acid therefore serves as a linkage site but is typically not involved in the desired adhesive effect.

[0106] In preferred embodiments, the peptide used according to the invention has an amino acid sequence which 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.

[0107] In preferred embodiments, the peptide used according to the invention 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), SRARLFWTYHKC (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), RALF RAL WE ALF EALC (SEQ ID NO:19), RALFEALWRALFEALC (SEQ ID NQ: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). In preferred embodiments, the peptide used according to the invention has a sequence shown 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.

[0108] In various embodiments, peptides according to the invention may be surface-active or non-surface-active.

[0109] In preferred embodiments, peptides according to the invention are not surface-active.

[0110] In preferred embodiments, peptides according to the invention are surface-active.

[0111] Various methods for determining interfacial activity are known to those skilled in the art. Within the scope of the invention, the dynamic surface tension is determined as a measure of interfacial activity, based on the bubble pressure method (also called bubble differential pressure method). Using the SITA science line t100 laboratory tensiometer (formerly SITA Messtechnik GmbH, Dresden), the dynamic surface tension of surfactants or molecules with surfactant-like properties is measured in liquids, in particular aqueous liquids, at pH 8.0 and 20°C. The dynamic surface tension provides, among other things, information on the kinetics of surfactants and is thus a measure of the interfacial activity of, for example, surfactants, but also other molecules (cf. If the dynamic surface tension remains constant throughout the bubble lifetime, the corresponding test substance is not surface-active. Even a deviation of a few mN / m from the ideal surface tension of 72 mN / m for pure water indicates a surfactant effect and would be an indication of surface-active behavior. In the context of the invention, "non-surface-active" is understood to mean a substance in which the dynamic surface tension remains constant throughout the bubble lifetime, i.e., the deviation is less than 10 mN / m, preferably less than 8 mN / m, more preferably less than 6 mN / m, particularly preferably less than 5 mN / m, and most preferably less than 2 mN / m. In the context of the invention, "surface-active" is understood to mean a substance in which the dynamic surface tension does not remain constant throughout the bubble lifetime, i.e.that the deviation is at least 2 mN / m, preferably at least 5 mN / m, more preferably at least 6 mN / m, particularly preferably at least 8 mN / m, most preferably at least 10 mN / m.

[0112] In various embodiments, peptides of the invention may be surface-active or non-surface-active, with the surface activity being determined by the bubble pressure method as described herein.

[0113] In preferred embodiments, peptides according to the invention are not surface-active, wherein the surface activity is determined by the bubble pressure method as described herein.

[0114] In preferred embodiments, peptides according to the invention are surface-active, wherein the surface activity is determined by the bubble pressure method as described herein. Peptides used according to the invention bind to a fat- and / or oil-containing surface and / or to a surface coated with fat and / or oil and / or to a surface provided with at least one fat- and / or oil-containing soil, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, ie the peptides have the ability to adhere to corresponding surfaces under suitable conditions, ie usually non-denaturing conditions, and thus have 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 N- and / or C-terminally bound further functional groups.Furthermore, a peptide used according to the invention can be N- and / or C-terminally and / or via suitable side chains covalently and / or similar suitable binding mechanisms under the desired application conditions stably associated with a carrier substance, in particular to a fat- and / or oil-containing surface and / or to a surface coated with fat and / or oil and / or to a surface provided with at least one fat- and / or oil-containing soil, as described herein.

[0115] In preferred embodiments, peptides used according to the invention bind to fatty and / or oil-containing 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 earthenware as well as plastic), metal (e.g. cutlery or pots) or glass. In preferred embodiments, peptides used 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 earthenware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0116] In preferred embodiments, peptides used 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 dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots), metal (e.g. cutlery) or glass. In preferred embodiments, peptides used 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 dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots).In preferred embodiments, peptides used according to the invention bind to at least one fatty and / or oily soil 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 earthenware as well as plastic), metal (e.g. cutlery or pots). In preferred embodiments, peptides used according to the invention bind to at least one fatty soil 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 earthenware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0117] In particularly preferred embodiments, peptides used according to the invention bind to at least one fatty and / or oil-containing, preferably fatty, soil on textiles. In particularly preferred embodiments, peptides used according to the invention bind to at least one fatty and / or oil-containing, preferably fatty, soil on textiles, wherein the textile contains or consists of cotton, polyester, or mixtures thereof.

[0118] Good adhesion to textile surfaces, in particular textile surfaces made of synthetic fibers, such as polyester-containing textiles, can be achieved, for example, by a peptide with a pronounced helix structure (in particular a-helix structure) and / or a high arginine content, in particular at one of the termini.

[0119] Preferably used peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on polyester textiles have an amino acid sequence which 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 to one of the amino acids shown 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. Peptides which are further preferably used and which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soil on polyester textiles have an amino acid sequence which is identical to one of the amino acid sequences given 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 preferably used peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soil on polyester textiles have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 3, 7, 8, 9, 10, 11, 12, 13, 17, 19, 20, 21, 25, 26, 27, 29, 31. Very particularly preferably used peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soil on polyester textiles have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 8, 10, 21, 25, 26.

[0120] Preferably used peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on cotton textiles have an amino acid sequence which 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 to one of the amino acids shown 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. Peptides which are further preferably used and which have good to very good adhesion to at least one fat- and / or oil-containing, preferably fat-containing, soil on cotton textiles have an amino acid sequence which is identical to one of the amino acid sequences given 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 preferably used peptides which have good to very good adhesion to at least one fat- and / or oil-containing, preferably fat-containing, soil on cotton textiles have an amino acid sequence which is identical to one of the amino acid sequences given 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. Peptides which are particularly preferably used and which have good to very good adhesion to at least one fat- and / or oil-containing, preferably fat-containing, soil on cotton textiles have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 3, 4, 6, 7, 8, 9, 10, 12, 13, 23, 26, 27.

[0121] In particularly preferred embodiments, peptides used according to the invention bind to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, e.g. fatty and / or oil-containing soiling on dishes, pots, cutlery (metal) or glass.

[0122] Preferably used peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, have an amino acid sequence which 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 to one of the amino acid sequences given in SEQ ID NO:1-31. Further preferred peptides are those which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g.cutlery or pots) or glass, have an amino acid sequence which is identical to one of the amino acid sequences given 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 preferably used peptides which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, have an amino acid sequence which is identical to one of the amino acid sequences given 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.Peptides which are particularly preferably used and which have good to very good adhesion to at least one fatty and / or oil-containing, preferably fatty, soiling on hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1, 2, 3, 4, 5, 9, 10, 12, 29.

[0123] Methods for determining adhesion are known to those skilled in the art, and any suitable methods can be used. Further methods are described in the examples.

[0124] The term "variant," as used herein, refers to variants of the peptides and enzymes described herein that retain the functionality of the parent peptide and / or enzyme, but differ from the parent sequence by one or more sequence variations, e.g., 1, 2, or 3 sequence variations, e.g., a substitution, deletion, or insertion. The sequence identity of such variants may range from 80% to 86% of the total length of the parent peptide and / or enzyme, and may be at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5%.

[0125] The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the BLAST algorithm, which is established and commonly used in the state of the art (see, for example, Altschul et al. (1990) Basic local alignment search tool, J. Mol. Biol., 215:403-410, and Altschul et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res., 25:3389-3402) and is essentially achieved by matching similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences to one another. A tabular assignment of the relevant positions is referred to as an alignment. Another algorithm available in the state of the art is the FASTA algorithm. Sequence comparisons (alignments), especially multiple sequence comparisons, are created using computer programs. Frequently used are, for example, the Clustal series (see e.g. Chenna et al.(2003) Multiple sequence alignment with the Clustal series of programs, Nucleic Acid Res., 31:3497-3500), T-Coffee (cf. e.g. Notredame et al. (2000) T-Coffee: A novel method for multiple sequence alignments, J. Mol. Biol., 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 (use of the BLOSUM 62 scoring matrix for sequence alignment at the amino acid level). Unless otherwise stated, sequence identity reported herein is determined using the BLAST algorithm.

[0126] Such a comparison also allows a statement to be made about the similarity of the compared sequences. This is usually expressed as percent identity, i.e. the proportion of identical nucleotides or amino acid residues at the same positions or corresponding positions in an alignment. The broader term homology in amino acid sequences includes conserved amino acid substitutions, i.e. amino acids with similar chemical activity, since these usually exert similar chemical activities within the protein. 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 just for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by similarities in the sequences.Such regions often exhibit identical functions. They can be small and comprise only a few nucleotides or amino acids. Such small regions often perform essential functions for the overall activity of the protein. It may therefore be useful to refer sequence matches only to individual, possibly small regions. Unless otherwise stated, however, statements of identity or homology in this application refer to the entire length of the respective nucleic acid or amino acid sequence.

[0127] The peptide or protein concentration can be determined using known methods, e.g., the BCA method (bicinchoninic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method (Gornall et al., J. Biol. Chem., 1948, 177:751-766). Those skilled in the art of peptide and protein technology are familiar with a variety of suitable methods for determining peptide or protein concentration that can be applied within the scope of this invention.

[0128] In preferred embodiments, peptides, proteins, and enzymes used according to the invention can also be modified. Preferred modifications can include, for example, coupling the peptide or enzyme with certain other molecules or chemical groups, e.g., organic (macro)molecules, e.g., via a covalent bond or a linker / spacer via a suitable amino acid of the chain and / or N- and / or C-terminal.

[0129] 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.

[0130] In some embodiments, the peptides used according to the invention, which may, for example, have the amino acid cysteine ​​N- or C-terminally for coupling purposes, are coupled with biotin (functionally modified), preferably at a suitable amino acid of the chain and / or N- and / or C-terminally.

[0131] It is also possible for the peptide used according to the invention to be part of a protein or polypeptide. Such proteins and polypeptides can be produced recombinantly, for example, as fusion proteins. In such embodiments, the peptide according to the invention is located either N- or C-terminally to mediate the adhesion of the entire molecule to a surface. In such embodiments, the peptide also acts as an adhesion tag. All of the aforementioned features and embodiments can be implemented individually or in any desired combination.

[0132] 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, 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. The term "polypeptide" in this context refers in particular to peptides that comprise 100 or more amino acids. The term "larger peptides" preferably refers to peptides with at least 40 amino acids, unless otherwise described.

[0133] 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 to one another by at least one spacer; preferably, the at least one spacer comprises or consists 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 to one another linearly via peptide bonds, optionally also via a spacer.

[0134] Peptides and / or enzymes used according to the invention can, in various embodiments, be chemically synthesized and / or produced recombinantly by protein design. Short peptides are now easily synthesized, e.g., by solid-phase synthesis. Longer peptides and polypeptides, such as enzymes, are often also produced recombinantly in host organisms, e.g., in bacteria or yeast.

[0135] It is preferable to produce peptides and enzymes using recombinant methods. This refers to all genetic engineering or microbiological methods based on introducing the genes for the peptides or enzymes of interest into a host organism suitable for production and transcribing and translating them by this host organism (collectively referred to as biotechnological methods within the scope of this invention). For example, the genes in question are introduced via vectors, in particular expression vectors; but also via those that allow the gene of interest to be inserted into a pre-existing genetic element in the host organism, such as the chromosome or other vectors. The functional unit consisting of gene and promoter, and possibly other genetic elements, is typically referred to as an expression cassette. However, it does not necessarily have to be present as a physical unit.

[0136] The invention further relates to a nucleic acid which encodes a peptide or enzyme used according to the invention, as well as to a vector containing such a nucleic acid, in particular a cloning vector or an expression vector. These can be DNA or RNA molecules. They can be present as a single strand, as a single strand complementary to this single strand, or as a double strand. In particular in the case of DNA molecules, the sequences of both complementary strands must be taken into account in all three possible reading frames. Furthermore, it must be taken into account that different codons, i.e. base triplets, can code for the same amino acids, so that a specific amino acid sequence can be encoded by several different nucleic acids. Due to this degeneracy of the genetic code, all nucleic acid sequences which encode one of the peptides or enzymes described above are included in this subject matter of the invention.Can encode enzymes. The skilled person is able to determine these nucleic acid sequences without doubt because, despite the degeneracy of the genetic code, defined amino acids can be assigned to individual codons. Therefore, starting from an amino acid sequence, the skilled person can easily determine nucleic acids encoding this amino acid sequence. Furthermore, in nucleic acids according to the invention, one or more codons can be replaced by synonymous codons. This aspect relates in particular to the heterologous expression of the enzymes according to the invention. Thus, every organism, e.g. a host cell of a production strain, has a specific codon usage. Codon usage is understood to mean the translation of the genetic code into amino acids by the respective organism.Bottlenecks in protein biosynthesis can occur when the codons located on the nucleic acid in the organism are faced with a comparatively small number of loaded tRNA molecules. Although they code for the same amino acid, this results in a codon being translated less efficiently in the organism than a synonymous codon encoding the same amino acid. Due to the presence of a higher number of tRNA molecules for the synonymous codon, it can be translated more efficiently in the organism.

[0137] Using methods commonly known today, such as chemical synthesis or the polymerase chain reaction (PCR) in conjunction with standard molecular biological and / or protein chemical methods, a person skilled in the art can produce the corresponding nucleic acids, including complete genes, based on known DNA and / or amino acid sequences. Such methods are known, for example, from Sambrook, J., Fritsch, EF and Maniatis, T. 2001. Molecular cloning: a laboratory manual, 3rd Edition, Cold Spring Laboratory Press.

[0138] For the purposes of the present invention, vectors are understood to be elements consisting of nucleic acids which contain a nucleic acid according to the invention as a characteristic nucleic acid region. They are capable of establishing this nucleic acid as a stable genetic element in a species or cell line over several generations or cell divisions. Vectors are, particularly when used in bacteria, special plasmids, i.e. circular genetic elements. Within the scope of the present invention, a nucleic acid according to the invention is cloned into a vector. Vectors include, for example, those whose origin is bacterial plasmids, viruses or bacteriophages, or predominantly synthetic vectors or plasmids with elements of various origins. With the additional genetic elements present in each case, vectors are capable of establishing themselves as stable units in the respective host cells over several generations.They can be present extrachromosomally as separate units or integrated into a chromosome or chromosomal DNA. Expression vectors comprise nucleic acid sequences that enable them to replicate in the host cells containing them, preferably microorganisms, particularly preferably bacteria, and to express a contained nucleic acid there. Expression is influenced in particular by the promoter(s) that regulate transcription. In principle, expression can occur through the natural promoter originally located upstream of the nucleic acid to be expressed, but also through a promoter of the host cell provided on the expression vector or through a modified or completely different promoter of another organism or another host cell. In the present case, at least one promoter for the expression of a nucleic acid according to the invention is provided and used for its expression.Expression vectors can also be regulated, e.g., by changing the cultivation conditions or upon reaching a certain cell density of the host cells they contain, or by adding certain substances, particularly activators of gene expression. An example of such a substance is the galactose derivative isopropyl-ß-D-thiogalactopyranoside (IPTG), which is used as an activator of the bacterial lactose operon (lac operon). In contrast to expression vectors, the nucleic acid contained in cloning vectors is not expressed.

[0139] The invention further relates to a non-human host cell which comprises a nucleic acid according to the invention or a vector according to the invention, or which comprises a peptide or enzyme used according to the invention, in particular one which secretes the peptide or enzyme into the medium surrounding the host cell. Preferably, a nucleic acid according to the invention or a vector according to the invention is transformed into a microorganism, which then represents a host cell according to the invention. Alternatively, individual components, ie nucleic acid parts or fragments of a nucleic acid according to the invention, can be introduced into a host cell in such a way that the resulting host cell contains a nucleic acid according to the invention or a vector according to the invention.This procedure is particularly suitable when the host cell already contains one or more components of a nucleic acid according to the invention or of a vector according to the invention and the further components are then supplemented accordingly. Methods for transforming cells are established in the prior art and sufficiently known to the person skilled in the art. In principle, all cells are suitable as host cells, i.e. prokaryotic or eukaryotic cells. Preference is given to host cells that can be handled genetically in a favorable manner, for example with regard to transformation with the nucleic acid or the vector and its stable establishment, e.g. unicellular fungi or bacteria. Furthermore, preferred host cells are characterized by good microbiological and biotechnological handling. This applies, for example, to easy culturability, high growth rates, low requirements for fermentation media and good production and secretion rates for foreign proteins.Preferred host cells according to the invention secrete the (transgenically) expressed peptide or enzyme into the medium surrounding the host cells. Furthermore, the peptides or enzymes can be modified by the cells producing them after their production, e.g., by attaching sugar molecules, formylations, aminations, etc. Such post-translational modifications can functionally influence the peptide or enzyme. Further preferred embodiments are host cells whose activity can be regulated due to genetic regulatory elements, which are provided, for example, on the vector, but can also be present in these cells from the outset. These can be stimulated to express these peptides, for example, by the controlled addition of chemical compounds that serve as activators, by changing the cultivation conditions, or when a certain cell density is reached.This enables economical production of the peptides or enzymes according to the invention. An example of such a compound is IPTG, as described above.

[0140] Preferred host cells are prokaryotic or bacterial cells. Bacteria are characterized by short generation times and low demands on cultivation conditions. This allows for the establishment of cost-effective cultivation or production processes. Furthermore, experts in bacterial fermentation technology have extensive experience. For a specific production process, gram-negative or gram-positive bacteria may be suitable for a variety of reasons, which can be determined experimentally in each individual case, such as nutrient sources, product formation rate, time requirements, etc. In gram-negative bacteria, such as Escherichia coli, a multitude of proteins are secreted into the periplasmic space, the compartment between the two membranes surrounding the cells. This can be advantageous for specific applications.Furthermore, Gram-negative bacteria can also be engineered to secrete expressed proteins not only into the periplasmic space, but also into the medium surrounding the bacteria. Gram-positive bacteria, such as Bacilli or Actinomycetes or other members of the Actinomycetales, in contrast, lack an outer membrane, so secreted proteins are immediately released into the medium surrounding the bacteria, usually the nutrient medium, from which the expressed proteins can be purified. They can be directly isolated from the medium or further processed. Furthermore, Gram-positive bacteria are related to or identical to most of the source organisms for technically important enzymes and usually produce comparable enzymes themselves, so they have a similar codon usage and their protein synthesis apparatus is naturally oriented accordingly.Host cells according to the invention can be modified with regard to their culture requirements, have different or additional selection markers, or express different or additional proteins. In particular, they can also be host cells that transgenically express multiple peptides, proteins, or enzymes. The present invention is applicable in principle to all microorganisms, in particular to all fermentable microorganisms, particularly preferably to those of the genus Bacillus, and results in the production of peptides or enzymes used according to the invention through the use of such microorganisms. Such microorganisms then represent host cells within the meaning of the invention.In a further embodiment of the invention, the host cell is characterized in that it is a bacterium, preferably one selected from the group of the genera Escherichia, Klebsiella, Bacillus, Staphylococcus, Corynebacterium, Arthrobacter, Streptomyces, Stenotrophomonas and Pseudomonas, more preferably one selected from the group of Escherichia coli, Klebsiella planticola, Bacillus licheniformis, Bacillus lentus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus alcalophilus, Bacillus globigii, Bacillus gibsonii, Bacillus clausii, Bacillus halodurans, Bacillus pumilus, Staphylococcus carnosus, Corynebacterium glutamicum, Arthrobacter oxidans, Streptomyces lividans, Streptomyces coelicolor and Stenotrophomonas maltophilia.

[0141] The host cell can also be a eukaryotic cell, which is characterized by having a cell nucleus. A further subject of the invention is therefore a host cell which is characterized by having a cell nucleus. In contrast to prokaryotic cells, eukaryotic cells are capable of post-translationally modifying the protein they produce. Examples of this are fungi such as Actinomycetes or yeasts such as Saccharomyces or Kluyveromyces. This can be particularly advantageous, for example, if the proteins are to undergo specific modifications in connection with their synthesis, which enable such systems. The modifications that eukaryotic systems carry out, particularly in connection with protein synthesis, include the binding of low-molecular-weight compounds such as membrane anchors or oligosaccharides. Such oligosaccharide modifications can, for example,to reduce the allergenicity of an expressed protein may be desirable. Co-expression with enzymes naturally produced by such cells may also be advantageous. Furthermore, thermophilic fungal expression systems, for example, may be particularly suitable for the expression of temperature-stable proteins or variants.

[0142] The host cells according to the invention are cultivated and fermented in a conventional manner, e.g., in discontinuous or continuous systems. In the former case, a suitable nutrient medium is inoculated with the host cells, and the product is harvested from the medium after a period of time to be determined experimentally. Continuous fermentations are characterized by the achievement of a steady state in which cells partially die but also regrow over a comparatively long period of time, and at the same time, the formed peptide or enzyme can be removed from the medium.

[0143] Host cells according to the invention are preferably used to produce peptides used according to the invention. The invention therefore further provides a process for producing a peptide comprising a) culturing a host cell according to the invention, and b) isolating the peptide from the culture medium or from the host cell.

[0144] This subject matter of the invention preferably comprises fermentation processes. Fermentation processes are known per se from the prior art and represent the actual large-scale production step, usually followed by a suitable purification method of the product produced, e.g. the peptides used according to the invention. All fermentation processes based on a corresponding process for producing a peptide or enzyme used according to the invention represent embodiments of this subject matter of the invention. Fermentation processes which are characterized in that the fermentation is carried out via a feed strategy are particularly suitable. In this case, the media components which are consumed by the ongoing cultivation are fed in. This can result in considerable increases in both cell density and cell mass orDry mass and / or in particular in the activity of the peptides or enzymes of interest. Furthermore, the fermentation can also be designed in such a way that undesired metabolic products are filtered out or neutralized by adding buffer or appropriate counterions. The produced peptide or enzyme can be harvested from the fermentation medium. Such a fermentation process is preferred over isolation of the peptide or enzyme from the host cell, i.e., product preparation from the cell mass (dry mass), but requires the provision of suitable host cells or one or more suitable secretion markers or mechanisms and / or transport systems so that the host cells secrete the peptide or enzyme into the fermentation medium. Without secretion, the peptide or enzyme can alternatively be isolated from the host cell, i.e., purified from the cell mass, e.g.by precipitation with ammonium sulfate or ethanol, or by chromatographic purification.

[0145] All of the above-mentioned facts can be combined into processes to produce peptides or enzymes used according to the invention.

[0146] A further subject of the invention are peptides for adhesion to a fat- and / or oil-containing, preferably fatty, surface and / or to a surface coated with fat and / or oil, preferably fat, and / or to a surface provided with at least one fat- and / or oil-containing, preferably fatty, soiling, wherein the surface is preferably made of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.Cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which in N- to C-terminal orientation has the following sequence.

[0147] (C)m(X 1 )n(X 2 )o[(X 3 )p(X 4 )q]r(X 5 )s(C)t where

[0148] X 1 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I,

[0149] X 2 is selected from R, H and K, preferably R and K,

[0150] X 3is 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,

[0151] X 4 is selected from A, L and V, preferably A and L, X 5 is 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; or b) a peptide having an amino acid sequence which 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 any of the amino acid sequences set out in SEQ ID NOs: 1-31.

[0152] In preferred embodiments, the invention relates to peptides for adhesion to a fat- and / or oil-containing, preferably fatty, surface and / or to a surface coated with fat and / or oil, preferably fat, and / or to a surface provided with at least one fat- and / or oil-containing, preferably fatty, soiling, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton,Polyesters and mixtures thereof, wherein the peptide has an amino acid sequence 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), SRARLFWTYHKC (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 NQ: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). All facts, objects, and embodiments described above are also applicable to this subject matter of the invention. Therefore, express reference is made here to the disclosure at the appropriate point, with the note that this disclosure also applies to the above peptides according to the invention.

[0153] In a further aspect, the invention further relates to agents, preferably washing and / or cleaning agents, which comprise or consist of at least one peptide according to the invention.

[0154] The at least one peptide according to the invention can be present as an 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.

[0155] In various embodiments, the peptide described herein is used in washing or cleaning agents according to the invention in a concentration of 1 x 10 -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 agent.

[0156] In various embodiments, agents according to the invention contain an amount of the peptide according to the invention sufficient for one wash or rinse cycle. The peptide according to the invention is preferably contained in agents according to the invention in an amount, based on active protein, of 0.5 to 1,500 mg / job, 5 to 500 mg / job, and in particular 10 to 200 mg / job. Unless the agents according to the invention are single-dose units, the usual dosage amount of the agent per wash / rinse cycle is to be used for the calculation.

[0157] The compositions of the washing or cleaning agents according to the invention, as well as the amounts of the ingredients, depend on the respective intended use and the trained specialist is generally familiar with suitable dosages of these components and can obtain these from the relevant specialist literature.

[0158] The washing and cleaning agents according to the invention include all conceivable types of washing or cleaning agents, both concentrated and undiluted, for use on a commercial scale, in washing machines or for hand washing or cleaning. These include, for example, washing agents for textiles, carpets, or natural fibers, for which the term "washing agent" is used. These 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. Thus, in addition to manual and machine dishwashing detergents, scouring agents, glass cleaners, toilet air fresheners, etc.The washing and cleaning agents within the scope of the invention also include washing aids which are added to the actual washing agent during manual or machine washing of textiles in order 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 item of laundry is brought into contact before the actual washing, e.g. to dissolve stubborn soiling, and also agents which, in a step following the actual textile washing, impart further desirable properties to the laundry such as a pleasant feel, freedom from creasing or low static charge. The latter agents include, among others, fabric softeners. This also includes agents for use in (semi-)automated washing or cleaning systems such as robot mops or wet vacuum cleaners.

[0159] The detergents or cleaning agents according to the invention, which may be in powdered or granular solid form, in compacted or recompacted particle form, as homogeneous solutions or suspensions, can contain all known ingredients commonly used in such agents. The agents according to the invention can contain, in particular, 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, sequestering agents, electrolytes, pH regulators, and / or other auxiliaries such as optical brighteners, graying inhibitors, dye transfer inhibitors, foam regulators, as well as dyes and fragrances.Advantageous ingredients of the compositions 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 the disclosure content therein is incorporated into the present patent application.

[0160] Further embodiments of the invention include all solid, powdered, liquid, gel-like, or pasty dosage forms of agents according to the invention, which may optionally also consist of multiple phases and may be in compressed or uncompressed form. The agent may be in the form of a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l. Solid dosage forms of the agent also include extrudates, granules, tablets, or pouches. Alternatively, the agent 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 agents are generally preferred. Furthermore, the agent may be in the form of a one-component system. Such agents consist of one phase. Alternatively, an agent may also consist of multiple phases.Such a remedy is therefore divided into several components.

[0161] In preferred embodiments, the agent according to the invention is a washing and / or cleaning agent comprising at least one of the fat-binding peptides described herein.

[0162] In preferred embodiments, the agent according to the invention is a washing and / or cleaning agent which consists of at least two phases, wherein the at least one fat-binding peptide is contained in one of the phases.

[0163] In preferred embodiments, the agent 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 with a plastic content (mixed fabric) and / or made of a natural fiber such as cotton.The textile preferably 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 (PI_A), polyvinylidene fluoride (PVDF), polyether ketone (PEK), and / or copolymers or a blended fabric thereof, even more preferably polyester (PES), polyethylene (PE), polypropylene (PP), polystyrene (PS), copolymers or blended fabrics thereof, preferably a cotton / polyester blend with a polyester content of at least 10%, preferably at least 20%, more preferably at least 30%, particularly preferably at least 40%, most preferably at least 50%, especially 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 content, preferably to textiles made of at least one natural fiber and at least one plastic fiber (plastic content). In particular, the mixture or blended fabric consists of cotton and at least one plastic, in particular polyester. In preferred embodiments, a textile with a plastic content or a plastic mixture or blended fabric has a plastic content of at least 10%, preferably at least 20%, more preferably at least 30%, particularly preferably at least 40%, very particularly preferably at least 50%, in particular at least 60%, e.g. 65% or 70%.

[0164] In preferred embodiments, the agent is a cleaning agent for hard surfaces, in particular metal, pots, dishes, ceramics, in particular porcelain, or glass.

[0165] 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-repellent, in particular grease- and / or oil-removing, effect, in particular by binding / adhering to at least one grease- and / or oil-containing, preferably fatty, soil on textiles, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass. Thus, the washing and / or cleaning agent is preferably used as a detergent in a washing process, in particular in machine washing or hand washing.When used in detergents and / or cleaning agents, the peptides described herein not only improve the cleaning performance of greasy and / or oily soils, but also exhibit a dirt-removing, particularly grease- and / or oil-removing, effect. They thus represent a biodegradable alternative to soil release polymers. These peptides are therefore particularly suitable for use in detergents and cleaning agents and can contribute to improved cleaning performance. Furthermore, they can help reduce or completely eliminate 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.

[0166] It is preferred that the peptide according to the invention is suitable for adhesion to at least one fat- and / or oil-containing, preferably fat-containing, soil on textiles, in particular containing or consisting of cotton, polyester and mixtures thereof.

[0167] It is preferred that the peptide according to the invention is suitable for adhesion to at least one fat- and / or oil-containing, preferably fatty, soil on hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass.

[0168] It is preferred that the peptide according to the invention has a soil-removing, in particular grease and / or oil-removing, effect, in particular with regard to at least one grease- and / or oil-containing soil on a textile surface, in particular containing or consisting of cotton, polyester and mixtures thereof, and / or hard surface, in particular tableware (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass.

[0169] One possible mechanism for the fat-removing effect could be that the peptides described here are able to adsorb onto solid fats and thereby soften the fatty film. This surfactant-like behavior makes it easier to remove the fatty film during the cleaning process. The softened fat can be detached (roll-up mechanism) and / or rinsed off. This mechanism could be explained by the surface-active behavior of peptides according to the invention. An example of such a peptide is a peptide with SEQ ID NO: 29. Another possible mechanism is that the peptides described here, in particular the non-surface-active peptides according to the invention, form a stable layer on the fatty layer. This functionalization of the fatty surface orBy binding to the greasy soil on a surface, other grease-removing and / or dissolving substances or molecules gain easier access to the fatty layer. Peptides according to the invention therefore also allow the removal of greasy soils at lower temperatures, e.g., approximately 15°C, approximately 20°C, or approximately 30°C. They thus enable the formulation of high-performance washing and / or cleaning agents that exhibit good cleaning performance on at least one greasy soil even at low temperatures, e.g., approximately 15°C, approximately 20°C, or approximately 30°C.

[0170] All facts, objects, and embodiments described above are also applicable to this subject matter of the invention. Therefore, explicit reference is made here to the disclosure at the corresponding point, with the note that this disclosure also applies to the above-mentioned inventive means.

[0171] A further subject matter 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 tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, which is characterized in that an agent according to the invention or a peptide according to the invention is used in at least one method step.

[0172] In various embodiments, the process described above is characterized in 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 45°C, particularly preferably at about 20°C to about 30°C, most preferably about 20°C.

[0173] This includes both manual and mechanical processes, with mechanical processes being preferred due to their more precise controllability, e.g., with regard to the quantities used and contact times. Processes for cleaning textiles are generally characterized by the fact that various cleaning-active substances are applied to the items to be cleaned in several process steps and are washed off after the contact time, or by the items to be cleaned being treated in some other way with a detergent or a solution or dilution of this detergent. The process preferably relates to a mechanical washing process, in particular in a washing machine, or a hand-washing process. The peptide described herein preferably acts as a soil-repellent and / or soil-removing agent.

[0174] This subject matter of the invention also encompasses a machine dishwashing process. In such a process, the agent according to the invention can be dosed into the cleaning solution, for example, by means of the dosing chamber in the door or by means of an additional dosing container in the interior of the dishwasher. Alternatively, the agent can also be applied directly to the soiled dishes or to one of the interior walls of the dishwasher, for example the inside of the door. The process according to the invention is carried out in the interior of a commercially available dishwasher. In a dishwasher, the cleaning program can generally be selected and set by the consumer before the dishwashing process is carried out. The cleaning program of the dishwasher used in the process according to the invention comprises at least one cleaning cycle.According to the invention, cleaning programs that include additional 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 preferably a component of 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 liquor is heated during the cleaning cycle.

[0175] Alternative embodiments of this subject matter of the invention also represent processes for the treatment of textile raw materials or for textile care, in which an agent according to the invention or a peptide according to the invention becomes active in at least one process step. Among these, processes for textile raw materials, fibers or textiles with natural components are preferred, and very particularly for those with wool or silk. A further subject matter 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 tableware (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g.cutlery or pots) or glass, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0176] A further subject matter of the invention is the use of a peptide described herein in a washing and / or cleaning agent according to the invention for improving the cleaning performance of the washing and / or cleaning agent on at least one fatty and / or oily soil, preferably in a temperature range from about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0177] A further subject 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.

[0178] In preferred embodiments, the use of the peptide according to the invention leads to a dirt-removing, in particular grease- and / or oil-removing, effect, i.e. the peptide brings about a dirt-removing, in particular grease- and / or oil-removing, effect on 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 earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, preferably in the washing and / or cleaning process, more preferably as a component of a washing and / or cleaning agent. In particular, the surfaces are freed of this soiling by the presence of the peptide, which binds to at least one greasy soil on the textile and / or the hard surface.

[0179] All facts, subject matters, and embodiments described for peptides and agents according to the invention are also applicable to these subject matters of the invention. Therefore, express reference is made here to the disclosure at the appropriate point, with the note that this disclosure also applies to the above-mentioned methods and uses according to the invention. PREFERRED EMBODIMENTS

[0180] 1 . Use of a peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide having an amino acid sequence which 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.

[0181] 2. Use of a peptide for adhesion to a fatty surface, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide having an amino acid sequence which 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.

[0182] 3. Use of a peptide for adhesion to a surface coated with fat, wherein the surface preferably consists of hard surfaces, more preferably surfaces containing or consisting of ceramics (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 ceramics such as porcelain or earthenware and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide having an amino acid sequence which 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.

[0183] 4. Use of a peptide for adhesion to a surface provided with at least one greasy and / or oily soil, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide having an amino acid sequence which 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.

[0184] 5. Use of a peptide for adhesion to at least one greasy and / or oily soiling on a surface, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide having an amino acid sequence which 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.

[0185] 6. Use of a peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.Cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide having an amino acid sequence that is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31. 7. Use of a peptide for adhesion to a fatty surface, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide having an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0186] 8. Use of a peptide for adhesion to a surface coated with fat, wherein the surface is preferably selected from hard surfaces, more preferably surfaces 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 dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide which has an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0187] 9. Use of a peptide for adhesion to a surface provided with at least one greasy and / or oily soil, wherein the surface is preferably selected from hard surfaces, more preferably surfaces 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 dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide which has an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0188] 10. Use of a peptide for adhesion to at least one greasy and / or oily soil on a surface, wherein the surface is preferably selected from hard surfaces, more preferably surfaces 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 dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide which has an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0189] 11 . Use of a peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface is selected from hard surfaces, in particular dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and 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.

[0190] 12. Use of a peptide for adhesion to a fatty surface, wherein the surface is selected from hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, and 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.

[0191] 13. Use of a peptide for adhesion to a surface coated with fat, wherein the surface is selected from hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, and 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.

[0192] 14. Use of a peptide for adhesion to a surface provided with at least one greasy and / or oily soil, wherein the surface is selected from hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware as well as plastic), metal (e.g. cutlery or pots) or glass, and wherein the peptide is selected from a peptide having an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0193] 15. Use of a peptide for adhesion to at least one fatty and / or oily soil on a surface, wherein the surface is selected from hard surfaces, in particular tableware (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and 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.

[0194] 16. Use of a peptide for adhesion to a fatty surface or to a surface coated with fat or to a surface provided with at least one fatty and / or oily soil, wherein the surface is a textile surface containing or consisting of cotton, polyester and mixtures thereof, and 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.

[0195] 17. Use of a peptide for adhesion to a fatty surface, wherein the surface is a textile surface containing or consisting of cotton, polyester and mixtures thereof, and 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.

[0196] 18. Use of a peptide for adhesion to a grease-coated surface, wherein the surface is a textile surface containing or consisting of cotton, polyester and mixtures thereof, and wherein the peptide is selected from a peptide having an amino acid sequence identical to one of the amino acid sequences listed in SEQ ID NOs: 1-31.

[0197] 19. Use of a peptide for adhesion to a surface provided with at least one greasy and / or oily soil, wherein the surface is a textile surface containing or consisting of cotton, polyester and mixtures thereof, and 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.

[0198] 20. Use of a peptide for adhesion to at least one fatty and / or oily soil on a surface, wherein the surface is a textile surface containing or consisting of cotton, polyester and mixtures thereof, and 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.

[0199] 21. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide, for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soiling and / or for removing at least one, preferably two or more, greasy and / or oily soiling(s) from a surface and / or for improving the cleaning performance of the agent on at least one, preferably two or more, greasy and / or oily soiling(s) on a surface, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the at least one peptide is selected from a peptide having an amino acid sequence which is 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 any of the amino acid sequences listed in SEQ ID NOs: 1-31. 22.Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide, for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soiling and / or for removing at least one, preferably two or more, greasy and / or oily soiling(s) from a surface and / or for improving the cleaning performance of the agent on at least one, preferably two or more, greasy and / or oily soiling(s) on a surface, wherein the surface consists of hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g.cutlery or pots) or glass, and wherein the at least one peptide is selected from a peptide having an amino acid sequence which 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.

[0200] 23. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for adhering to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil and / or for removing at least one, preferably two or more, greasy and / or oily soil(s) from a surface and / or for improving the cleaning performance of the agent on at least one, preferably two or more, greasy and / or oily soil(s) on a surface, wherein the surface is selected from textile surfaces containing or consisting of cotton, polyester and mixtures thereof, and wherein the at least one peptide is selected from a peptide having an amino acid sequence which is 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%,has 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1-31.

[0201] 24. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soiling and / or for removing at least one, preferably two or more, greasy and / or oily soiling(s) from a surface and / or for improving the cleaning performance of the agent on at least one, preferably two or more, greasy and / or oily soiling(s) on a surface, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the at least one peptide is selected from a peptide which has an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0202] 25. at least one peptide for adhering to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil and / or for removing at least one, preferably two or more, greasy and / or oily soil(s) from a surface and / or for improving the cleaning performance of the agent on at least one, preferably two or more, greasy and / or oily soil(s) on a surface, wherein the surface is selected from hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and wherein the at least one 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.

[0203] 26. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for adhering to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil and / or for removing at least one, preferably two or more, greasy and / or oily soil(s) from a surface and / or for improving the cleaning performance of the agent on at least one, preferably two or more, greasy and / or oily soil(s) on a surface, wherein the surface is selected from textile surfaces containing or consisting of cotton, polyester and mixtures thereof, and wherein the at least one 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.

[0204] 27. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the at least one peptide is selected from a peptide having an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0205] 28. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface is selected from hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and wherein the at least one peptide is selected from a peptide having an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0206] 29. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface is selected from textile surfaces containing or consisting of cotton, polyester and mixtures thereof, and wherein the at least one 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.

[0207] 30. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide, for removing at least one, preferably two or more, greasy and / or oily soiling(s) from a surface, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the at least one peptide is selected from a peptide having an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0208] 31 . Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for removing at least one, preferably two or more, fatty and / or oily soiling(s) from a surface, wherein the surface is selected from hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and wherein the at least one peptide is selected from a peptide having an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0209] 32. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for removing at least one, preferably two or more, greasy and / or oily soil(s) from a surface, wherein the surface is selected from textile surfaces containing or consisting of cotton, polyester and mixtures thereof, and wherein the at least one 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. 33. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for improving the cleaning performance of the agent on at least one, preferably two or more, greasy and / or oily soil(s) on a surface, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, and wherein the at least one peptide is selected from a peptide which has an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0210] 34. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for improving the cleaning performance of the agent on at least one, preferably two or more, fatty and / or oily soil(s) on a surface, wherein the surface is selected from hard surfaces, preferably dishes (preferably made of ceramic such as porcelain or earthenware and plastic), metal (e.g. cutlery or pots) or glass, and wherein the at least one peptide is selected from a peptide having an amino acid sequence which is identical to one of the amino acid sequences mentioned in SEQ ID NOs: 1-31.

[0211] 35. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide for improving the cleaning performance of the agent on at least one, preferably two or more, fatty and / or oily soil(s) on a surface, wherein the surface is selected from textile surfaces containing or consisting of cotton, polyester and mixtures thereof, and wherein the at least one 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.

[0212] 36. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence mentioned in SEQ ID NO:1.

[0213] 37. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence mentioned in SEQ ID NO:2.

[0214] 38. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence specified in SEQ ID NO:3. 39. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence specified in SEQ ID NO:4.

[0215] 40. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence mentioned in SEQ ID NO:5.

[0216] 41. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence mentioned in SEQ ID NO:6.

[0217] 42. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:7.

[0218] 43. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence mentioned in SEQ ID NO:8.

[0219] 44. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:9.

[0220] 45. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NQ:10.

[0221] 46. ​​Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:11.

[0222] 47. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:12.

[0223] 48. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:13.

[0224] 49. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence specified in SEQ ID NO:14. 50. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence specified in SEQ ID NO:15.

[0225] 51. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence mentioned in SEQ ID NO:16.

[0226] 52. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:17.

[0227] 53. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:18.

[0228] 54. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:19.

[0229] 55. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NQ:20.

[0230] 56. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:21.

[0231] 57. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:22.

[0232] 58. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:23.

[0233] 59. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:24.

[0234] 60. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence specified in SEQ ID NO:25. 61. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence specified in SEQ ID NO:26.

[0235] 62. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:27.

[0236] 63. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:28.

[0237] 64. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:29.

[0238] 65. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence mentioned in SEQ ID NO:30.

[0239] 66. Use according to any one of items 1 to 35, wherein the at least one peptide is selected from a peptide having an amino acid sequence identical to the amino acid sequence set out in SEQ ID NO:31.

[0240] 67. Use according to any one of items 1 to 66, wherein the at least one peptide is surface-active.

[0241] 68. Use according to any one of items 1 to 66, wherein the at least one peptide is not surface-active.

[0242] 69. Use according to any one of items 1 to 66, wherein the at least one peptide is surface-active, wherein the surface activity is determined by the bubble pressure method as described herein.

[0243] 70. Use according to any one of items 1 to 66, wherein the at least one peptide is not surface-active, wherein the surface activity is determined by the bubble pressure method as described herein.

[0244] 71. Use according to any one of items 1 to 67 or 69, wherein the at least one peptide is surface-active, wherein the surface activity is determined by the bubble pressure method as described herein, and wherein the dynamic surface tension over the entire bubble lifetime has a deviation of at least 2 mN / m, preferably at least 5 mN / m, more preferably at least 6 mN / m, particularly preferably at least 8 mN / m, most preferably at least 10 mN / m. 72. Use according to any one of items 1 to 66, 68 or 70, wherein the at least one peptide is not surface-active, wherein the surface activity is determined according to the bubble pressure method as described herein, and wherein the dynamic surface tension over the entire bubble lifetime has a deviation of less than 10 mN / m, preferably less than 8 mN / m, more preferably less than 6 mN / m, particularly preferably less than 5 mN / m and most preferably less than 2 mN / m.

[0245] 73. Use according to any one of items 1 to 72, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

[0246] 74. Agents, preferably washing or cleaning agents, comprising at least one peptide as defined in any one of items 1 to 72.

[0247] 75. Use of an agent according to item 74 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 earthenware and plastic), metal (e.g. cutlery or pots) or glass, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C.

[0248] 76. Use of a peptide as defined in any one of items 1 to 72 as a soil-removing, in particular grease- and / or oil-removing, active ingredient in a washing or cleaning agent, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, further preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C.

[0249] 77. Use of a peptide as defined in any one of items 1 to 72 for improving the cleaning performance of a washing or cleaning agent on at least one greasy and / or oily soil, preferably greasy soil, preferably in a temperature range from about 10°C to about 80°C, preferably about 15°C to about 60°C, further preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C.

[0250] EXAMPLES

[0251] Example 1 : Peptide sequences

[0252] The peptides shown in Table 2 were prepared by chemical synthesis.

[0253] Table 2: Peptide names and corresponding amino acid sequences

[0254] Example 2: Testing the adhesion of peptides with regard to their substrate specificity to fats

[0255] 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 amounts of proteins and peptides in solution. The fluorescamine reagent reacts rapidly with primary amines.

[0256] The following pre-soiled textile rags were used (ex. CFT, Center For Test Material): C-FF CS46, Frying Fat, used, Cotton (frying fat on cotton)

[0257] P-FF PS46, Frying Fat, used, Polyester (frying fat on polyester)

[0258] C-0 C02, Olive Oil with carbon black with thickening agent, Cotton (olive oil on cotton)

[0259] P-0 P02, Olive Oil with carbon black with thickening agent, Polyester (olive oil on polyester)

[0260] CS CS32, Sebum Bey with Carbon black, Cotton (Sebum on cotton)

[0261] P-S PS32, Sebum Bey with Carbon black, Polyester (Sebum auf Polyester)

[0262] For the study, three textile patches (each approximately 10 mm in diameter) were placed twice in the wells of a 48-well microtiter plate. 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 with gentle shaking (750 rpm, Titramax) for 1 h at 20°C. 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 fluorescence values.

[0263] The results are shown in Table 3. The larger 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.

[0264] Table 3: Adhesion results

[0265] All peptides P1 to P31 exhibit 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 exhibits no adhesion to greasy and / or oily soils.

[0266] Example 3: Exemplary detergent and cleaning agent formulations

[0267] The at least one peptide according to the invention can be used in various detergent and cleaning compositions and realize its effect. Table 4: Liquid detergents

[0268] Table 5: Solid detergents

[0269]

[0270] Table 6: Two-phase solid dishwasher detergents

[0271] Table 7: Solid dishwasher detergents

[0272] Table 8: Single-phase liquid dishwasher detergents

[0273] Table 9: Two-phase liquid automatic dishwashing detergents in separate compartments

[0274] The respective enzyme phase is added to the respective alkaline phase in a ratio of 1:1, total weight 30 g, from a two-chamber bottle directly into the dosing chamber of an automatic dishwasher. Table 10: Multi-phase, liquid detergent combination. Suitable for automatic

[0275] Dosing, preferably in dishwashers in separate compartments Table 11 : Cleaning agents for hard surfaces

[0276] * pH = 10 was achieved by adding NaOH

[0277] Table 12: Hand dishwashing detergents

[0278] Table 13: Cleaning agents for hard surfaces, preferred for glass cleaning

[0279] In addition, the above-mentioned compositions were provided with amine oxide and a fatty alcohol ethoxylate with 7 EO units as additional surfactants in an amount of 0.2 wt.% each.

Claims

PATENT CLAIMS 1 . Use of a peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.Cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the 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 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I, X 2 is selected from R, H and K, preferably R and K, X 3is 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 is selected from A, L and V, preferably A and L, X 5 is 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; or b) a peptide having an amino acid sequence which 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 any of the amino acid sequences set out in SEQ ID NOs: 1-31.

2. Use of an agent, preferably a washing or cleaning agent, comprising at least one peptide, for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soiling and / or for removing at least one, preferably two or more, greasy and / or oily soiling(s) from a surface and / or for improving the cleaning performance of the agent on at least one, preferably two or more, greasy and / or oily soiling(s) on a surface, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g. cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, more preferably cotton, polyester and mixtures thereof, wherein the at least one peptide is selected from a) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 8 to 25 amino acids, more preferably 12 to 18 amino acids, wherein the peptide has an amino acid sequence which has 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 is selected from A, N, D, Q, E, G, I, L, M, F, S, T, W, Y and V, preferably G, I, S and W, more preferably G and I, X 2 is selected from R, H and K, preferably R and K, X 3 is selected from A, R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, preferably A, R, N, Q, G, H, I, L, K, M, F, P, S, T, W, Y and V, X 4 is selected from A, L and V, preferably A and L, X 5 is 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; or b) a peptide having an amino acid sequence which 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.

3. Use according to claim 1 or 2, wherein the peptide according to claim 1a) or 2a) (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.

4. Use according to one of claims 1 to 3, wherein in the peptide according to claim 1 a) or 2a), when o = 1, p = 0, 1 or 2, q = 2 and r = 4, the sequence (X 2 )0[(X 3 )p(X 4 )q] r (X 5 )s equals Z 1 Z 2 Z 3 [(Z 4 ) U Z 5 Z6 ]3(Z 7 )V, where Z 1 like X 2 defined in claim 1 or 2 and is selected from R, H and K, preferably R, Z 2 , Z 3 , Z 5 and Z 6 like X 4 defined in claim 1 or 2 and selected from A, L and V, preferably A and L, Z 4 like X 3 defined in claim 1 or 2 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 is 1 or 2, Z 7 like X 5 defined in claim 1 or 2 and is selected from A, R, N, D, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y and V, v is as defined in claim 1 or 2 and is an integer from 0 to 4.

5. Use according to claim 4, wherein, (i) if u = 1 , Z 4 is selected from R, E and Q, or (ii) if u = 2, (Z 4)2 is selected from FR, FE, AR, WE, WR and AQ.

6. Use according to claim 4 or 5, wherein (i) the peptide comprises at least one motif selected from RAL and RI_A, preferably RAL, and wherein this sequence is preferably located in the N-terminal amino acids of positions 1-3; and / or (ii) the peptide comprises at least one motif selected from EAL and EI_A, preferably EAL, and wherein this motif is preferably not located in the N-terminal amino acids of positions 1-4; and / or (iii) the peptide comprises at least one motif selected from QAL and QI_A, 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.

7. Use according to any one of claims 1 to 3, wherein in the peptide according to claim 1 a) or 2a), when o = 1, p = 3-6, q = 1 or 2 and r = 2, the sequence (X 2 )0[(X 3 )p(X 4 )q] r equal to Z 11 (Z 12 )6Z 13 Z 14 (Z 15 )wZ 16 is, where Z 11 like X 2 defined in claim 1 or 2 and selected from R, H and K, Z 12 like X 3 defined in claim 1 or 2 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 in claim 1 or 2 and selected from A, L and V, preferably A and L, Z 15 like X 3 defined in claim 1 or 2 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.

8. Use according to claim 7, wherein, (i) z 13 Z 14 is selected from AL and LA, preferably AL; and / or (ii) (Z 15 ) w with w = 3-6 comprises a sequence comprising at least one positively charged amino acid (R, H or K); and / or (iii) (Z 15 ) w with w = 3-6 comprises a motif selected from RQN, KQN, QNR and QNK, preferably RQN and KQN, more preferably RQN; and / or (iv) Z 16 is selected from A and L, preferably A.

9. Use according to any one of claims 1 to 8, 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 listed in SEQ ID NOs: 1-31.

10. Use according to one of claims 1 to 9, wherein the peptide has an amino acid sequence according to one of the amino acid sequences mentioned 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, more preferably SEQ ID NOs: 1, 2, 3, 4, 5, 9, 10, 12, 29.

11. Use according to any one of claims 1 to 10, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most preferably about 20°C.

12. Peptide for adhesion to a greasy surface or to a surface coated with grease or to a surface provided with at least one greasy and / or oily soil, wherein the surface preferably consists of hard surfaces, more preferably surfaces 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 and plastic), metal (e.g.cutlery or pots) or glass, and / or textiles, more preferably textiles containing or consisting of cotton, polyester, polyamide, polypropylene and mixtures thereof, particularly preferably cotton, polyester and mixtures thereof, wherein the peptide is as defined in any one of the preceding claims, and wherein the adhesion is determined as described in Example 2.

13. Agents, preferably washing or cleaning agents, comprising at least one peptide as defined in one of the preceding claims.

14. Use of an agent according to claim 13 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 earthenware and plastic), metal (e.g. cutlery or pots) or glass, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C.

15. Use of a peptide as defined in any one of claims 1 to 11 as a dirt-removing, in particular grease- and / or oil-removing, active ingredient in a washing or cleaning agent, preferably in a temperature range of about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C.

16. Use of a peptide as defined in any one of claims 1 to 11 for improving the cleaning performance of a washing or cleaning agent on at least one fatty and / or oily soil, preferably fatty soil, preferably in a temperature range from about 10°C to about 80°C, preferably about 15°C to about 60°C, more preferably about 15°C to about 45°C, particularly preferably about 20°C to about 30°C, most particularly preferably about 20°C.

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