Peptides as dye transfer inhibitors for washing or cleaning agent

Abstract

The invention relates to washing or cleaning agents, comprising at least one peptide comprising or consisting of an amino acid sequence with 5 to 50 amino acids, wherein (a) the amino acid sequence comprises at least 5 histidine groups (H) and at least five further amino acid groups, which are uncharged amino acid groups, and has net charge at a neutral pH of -2 to +6; and / or (b) the amino acid sequence has at least 80 % sequence identity with one of the amino acid sequences named in SEQ ID NOs: 1-5. The invention also relates to a method for cleaning textiles using said washing or cleaning agent and to the use of a peptide, as described within the washing or cleaning agent, as a dye transfer inhibitor.

Description

[0001] PEPTIDES AS DYE TRANSFER INHIBITORS FOR DETERGENT OR CLEANING AGENTS

[0002] The invention relates to washing or cleaning agents comprising at least one peptide as defined herein. Furthermore, the invention relates to a method for cleaning textiles using said washing or cleaning agent and to the use of a peptide as described in the context of the washing or cleaning agent as a dye transfer inhibitor.

[0003] DTI (dye transfer inhibitor) polymers have long been an important component of modern textile detergents and cleaning agents. Their purpose is to bind dyes that bleed during the washing of colored textiles, preventing them from redepositing on white or other colored textiles washed with the fabric, thus protecting them from discoloration. The problem of textile dye bleeding occurs particularly in intensively colored textiles.

[0004] Commercially used DTI polymers include homo- or copolymers based on vinylic, nitrogen-containing, preferably heterocyclic monomers, such as vinylpyrrolidone-vinylimidazole copolymers. However, these polymers are typically not biodegradable.

[0005] Therefore, there is a need for alternative or improved, particularly biodegradable, dye transfer inhibitors for use in detergents and cleaning agents.

[0006] It has now been surprisingly discovered that certain peptides can represent a biodegradable alternative to DTI polymers. Histidine-rich peptides are particularly noteworthy in this regard. For example, due to the imidazole ring of the histidine, the peptide can exhibit similar chemical properties to a DTI polymer, particularly a vinylpyrrolidone-vinylimidazole copolymer.

[0007] The invention therefore relates in a first aspect to a washing or cleaning agent comprising at least one peptide comprising or consisting of an amino acid sequence with 5 to 50 amino acids, preferably 10 to 30 amino acids, in particular 18 to 25 amino acids, wherein

[0008] (a) the amino acid sequence comprises at least 5 histidine residues (H), preferably at least 6 H, more preferably at least 10 H, in particular at least 12 H, at least five further amino acid residues, preferably at least 8 further amino acid residues, which are uncharged amino acid residues, preferably selected from A, G, P, F, I, W, S, V, L, Y and Q, in particular selected from A, G and P, and has a net charge at neutral pH of -2 to +6, preferably from 0 to +4, more preferably from 0 to +2, in particular from 0; and / or

[0009] (b) the amino acid sequence has at least 80%, preferably at least 81%, more preferably at least 82%, even more preferably at least 83%, even more preferably at least 84%, even more preferably at least 85%, even more preferably at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-5, preferably with one of the amino acid sequences mentioned in SEQ ID NO: 1 or SEQ ID NO: 4.

[0010] In various embodiments, the amino acid sequence of the at least one peptide comprises at least one arginine residue (R), preferably within the 8 C-terminal amino acids, more preferably within the 4 C-terminal amino acids; and / or the amino acid sequence of the at least one peptide comprises at least one lysine residue (K), preferably within the 8 C-terminal amino acids, more preferably within the 4 C-terminal amino acids, in particular within the 2 C-terminal amino acids; and / or the amino acid sequence of the at least one peptide does not comprise any negatively charged amino acid residues, preferably no E or D, within the 8 N-terminal amino acid residues and / or the 8 C-terminal amino acid residues, preferably within the 4 N-terminal amino acid residues and / or the 4 C-terminal amino acid residues; and / or the amino acid sequence of the at least one peptide has a neutral net charge at the N-terminus, comprising the first 3-5 amino acid residues;and / or the amino acid sequence of the at least one peptide at the C-terminus, comprising the last 3-5 amino acid residues, has a neutral or positive net charge;

[0011] In particular, it is preferred that the amino acid sequence of the at least one peptide does not comprise any charged amino acid residues within the first 8 N-terminal amino acid residues; and / or comprises at least one of the sequence motifs AHHH, AAHA or AHHHAAHA, optionally multiple times, such as two, three or four times, preferably the sequence motif (AHHHAAHA)3; and / or comprises the sequence motif GHHPH, preferably (GHHPH)2, (GHHPH)3, or (GHHPH)4.

[0012] In various embodiments, the amino acid sequence of the at least one peptide may contain at least one aromatic amino acid, preferably selected from W, Y or F.

[0013] It is preferred that the at least one peptide consists of at least 60% of amino acid residues with a high alpha-helix-forming potential, wherein these amino acid residues are preferably selected from E, A, L, M, Q, K, R, F, I, H and W, more preferably from E, A, L, Q, K, R, F, I, H and W, in particular from A, F, I, and H.

[0014] In preferred embodiments, the at least one peptide comprises or consists of an amino acid sequence of one of the amino acid sequences mentioned in SEQ ID NOs: 1-5, preferably an amino acid sequence of one of the amino acid sequences mentioned in SEQ ID NO: 1 or SEQ ID NO: 4.

[0015] In various embodiments, the at least one peptide is a peptide or polypeptide (multimer) comprising two or more of the peptides as described herein. Optionally, the two or more peptides can be linked together by at least one spacer; preferably, the at least one spacer comprises or consists of 1 to 10 amino acid residues, preferably selected from the group consisting of G, P, I, A, and S or combinations thereof, in particular GPI or GAS. The peptides described herein are typically linked to each other and / or to the spacer via a peptide bond.

[0016] It is particularly preferred that the at least one peptide is suitable for adhesion and / or binding to dyes, preferably it is a dye transfer inhibitor.

[0017] In preferred embodiments, the washing or cleaning agent according to the invention is a detergent.

[0018] The washing or cleaning agent is preferably used at a pH value of 2-12, more preferably 6 to 10, in particular 7 to 9.

[0019] In a further aspect, the invention relates to a method for cleaning textiles comprising at least one step in which a washing or cleaning agent according to the invention is used.

[0020] Finally, in a third aspect, the invention relates to the use of a peptide as a dye transfer inhibitor, wherein the peptide comprises or consists of an amino acid sequence having 5 to 50 amino acid residues, preferably 10 to 30 amino acid residues, in particular 18 to 25 amino acid residues, wherein

[0021] (a) the amino acid sequence comprises at least 5 histidine residues (H), preferably at least 6 H, more preferably at least 10 H, in particular at least 12 H, at least five further amino acid residues, preferably at least 8 further amino acid residues, which are uncharged amino acid residues, preferably selected from A, G, P, F, I, W, S, V, L, Y and Q, in particular selected from A, G and P, and has a net charge at neutral pH of -2 to +6, preferably from 0 to +4, more preferably from 0 to +2, in particular from 0; and / or

[0022] (b) the amino acid sequence has at least 80%, preferably at least 85%, more preferably at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-5, preferably with one of the amino acid sequences mentioned in SEQ ID NO: 1 or SEQ ID NO: 4.

[0023] Preferably, the peptide of use is at least one peptide as described herein, in particular according to the at least one peptide comprised in the washing or cleaning agent according to the invention.

[0024] In particularly preferred embodiments, the use of the peptide reduces or prevents color transfer to textiles, preferably during the washing process, and in particular the textiles are protected from discoloration. These and other embodiments, features, and advantages of the invention will become apparent to those skilled in the art from studying the following detailed description and claims. Individual described features or embodiments of the invention can be combined with other features or embodiments of the invention without these being described in combination within the scope of the invention. It is to be understood that the examples contained herein are intended to describe and illustrate the invention, but not to restrict it, and in particular the invention is not limited to the examples.

[0025] “At least one”, as used herein, refers to 1 or more, e.g. 1, 2, 3, 4, 5, 6, 7, 8, 9 or more. In relation to an ingredient, the information refers to the type of ingredient and not to the absolute number of molecules. “At least one peptide” therefore 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 information, the information refers to all compounds of the specified type contained in, for example, a product, i.e., the product typically does not contain any further compounds of this type beyond the stated amount of the corresponding compounds.

[0026] Unless otherwise stated, all quantities stated in connection with the washing or cleaning agents described herein refer to wt.%, in each case based on the total weight of the composition. Furthermore, such quantities relating to at least one ingredient always refer to the total amount of that type of ingredient contained in the composition, unless explicitly stated otherwise. This means that such quantities, e.g. in connection with "at least one peptide," refer to the total amount of peptides contained in the composition, unless explicitly stated otherwise.

[0027] Numerical values ​​stated without decimal places refer to the full value specified with one decimal place. For example, "99%" stands for "99.0%."

[0028] Numerical ranges specified in the format "in / from x to y" include the specified values. If multiple preferred numerical ranges are specified in this format, it is understood that all ranges resulting from the combination of the different endpoints are also included.

[0029] “Approximately” or “about” as used herein with reference to numerical values ​​means the corresponding value ±10%, preferably ±5%.

[0030] In the context of the present invention, the term "washing or cleaning agent" as used herein preferably includes both concentrates and undiluted agents for use on a commercial scale, in washing machines or for hand washing or cleaning. These include, for example, detergents for textiles, carpets, or natural fibers, for which the term "washing agent" is used. These also include, for example, dishwashing detergents for dishwashers 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 automatic dishwashing detergents, this also includes, for example, scouring agents, glass cleaners, toilet air fresheners, etc.Detergents and cleaning agents also include washing aids, which are added to the detergent during manual or machine washing to achieve an additional effect. Furthermore, in the context of the invention, detergents and cleaning agents also include textile pre- and post-treatment agents, i.e. agents with which the laundry is brought into contact before the actual washing, e.g., to dissolve stubborn soils, and also agents that impart further desirable properties to the laundry, such as a pleasant feel, crease resistance, or low static charge, in a step following the actual textile washing. Fabric softeners, among others, are counted among the latter agents.

[0031] According to the invention, the washing or cleaning agent comprises at least one peptide comprising or consisting of an amino acid sequence with 5 to 50 amino acids, preferably 10 to 30 amino acids, more preferably 18 to 25 amino acids, in particular 20 to 24 amino acids, e.g. 20, 21, 23 or 24 amino acids.

[0032] According to the invention, the amino acid sequence of the at least one peptide comprises

[0033] (a) at least 5 histidine residues (H), preferably at least 6 H, more preferably at least 10 H, in particular at least 12 H, at least five further amino acid residues, preferably at least 8 further amino acid residues, e.g. at least 10, 12, 14, 16 or 18 further amino acid residues, which are uncharged amino acid residues, preferably selected from A, G, P, F, I, W, S, V, L, Y and Q, in particular selected from A, G and P, and the amino acid sequence of the at least one peptide has a net charge at neutral pH of -2 to +6, preferably from 0 to +4, more preferably from 0 to +2, in particular from 0; and / or

[0034] (b) the amino acid sequence of the at least one peptide has at least 80%, preferably at least 81%, more preferably at least 82%, even more preferably at least 83%, even more preferably at least 84%, even more preferably at least 85%, even more preferably at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-5, preferably with one of the amino acid sequences mentioned in SEQ ID NO: 1 or SEQ ID NO: 4.

[0035] 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 largely linear structure, which is smaller than a natural protein. According to the invention, it has an amino acid sequence of 5 to 50 amino acids. The amino acids are specified in the context of this invention in the 1-letter code, where, for example, H stands for histidine, R for arginine, A for alanine, and L for leucine. It is further understood that, unless otherwise stated, the amino acids in an amino acid sequence disclosed herein are linked via peptide bonds, and the sequence is preferably listed in N- to C-terminal orientation. If an amino acid is not specified in more detail in the context of this invention, any amino acid is usually meant, typically one of the 20 naturally occurring proteinogenic amino acids, i.e.one of glycine (G), alanine (A), valine (V), leucine (L), isoleucine (I), phenylalanine (F), serine (S), threonine (T), proline (P), methionine (M), cysteine ​​(C), histidine (H), lysine (K), arginine (R), glutamine (Q), asparagine (N), aspartic acid (D), glutamic acid (E), tyrosine (Y) and tryptophan (W).

[0036] In various embodiments, the peptide has a total charge of -2 to +6, preferably from 0 to +4, more preferably from 0 to +2, especially 0. The total charge of the peptide is based on the number of positively and negatively charged amino acids in the peptide, in particular on the residues arginine (R), lysine (K), aspartic acid (D), and glutamic acid (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 one lysine residue and one glutamic acid residue would therefore have a total charge of 0.

[0037] Positively charged or basic amino acids (depending on pH) typically include R and K. H is not considered a positively charged amino acid in the context of this invention.

[0038] Amino acids such as H, G, A, C, I, L, M, F, V, P, S, T, W, Y, N and Q are typically uncharged, i.e. neutral, amino acids.

[0039] Typical acidic or negatively charged amino acids (depending on the pH value) are D and E.

[0040] In the context of the present invention, the term “N-terminus” or “N-terminal” describes the end of the amino acid chain of the peptide according to the invention, which has a free amino group.

[0041] In the context of the present invention, the term “C-terminus” or “C-terminal” describes the end of the amino acid chain of the peptide according to the invention which has a free carboxyl group.

[0042] 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 from the N-terminus to the C-terminus, unless otherwise described.

[0043] In various embodiments, the amino acid sequence of the at least one peptide may comprise at least one arginine residue (R), preferably within the last 8 C-terminal amino acids, more preferably within the last 4 C-terminal amino acids. In various embodiments, the amino acid sequence of the at least one peptide may also comprise at least two arginine residues (R) within the last 8 C-terminal amino acids.

[0044] In various other embodiments, the amino acid sequence of the at least one peptide may comprise at least one lysine residue (K), preferably within the last 8 C-terminal amino acids, more preferably within the last 4 C-terminal amino acids, in particular within the last 2 C-terminal amino acids. In some embodiments, R and K residues may also occur in the C-terminus as defined above, with the total number R+K then typically being 2, 3 or 4. In various embodiments, the amino acid sequence of the at least one peptide does not comprise any negatively charged amino acid residues within the first 8 N-terminal amino acid residues and / or the last 8 C-terminal amino acid residues, preferably within the first 4 N-terminal amino acid residues and / or the last 4 C-terminal amino acid residues.In particular, the first 8 N-terminal amino acid residues and / or the last 8 C-terminal amino acid residues, preferably the first 4 N-terminal amino acid residues and / or the last 4 C-terminal amino acid residues, do not include the amino acid residues E and D.

[0045] Preferably, the C-terminus of the amino acid sequence of the at least one peptide, comprising the last 3-5 amino acids, preferably the last 6 amino acids and in particular the last 8 amino acids, has a neutral or positive net charge, preferably a neutral net charge.

[0046] It is further preferred that the N-terminus of the amino acid sequence of the at least one peptide comprising the first 3-5 amino acids, preferably the first 6 amino acids and in particular the first 8 amino acids, has a neutral net charge.

[0047] The feature that the peptide has a neutral or positive net charge at the "C-terminus, which comprises the last 3-5 amino acids," means that the C-terminal 3-5 amino acids comprise as many or more positively charged amino acids than negatively charged amino acids. In various embodiments, this feature is met, for example, if the C-terminal 3-5 amino acids have 1 or 2 positively charged amino acids, i.e., K or R, and no or as many negatively charged amino acids, such as E or D. If the C-terminus contains a negatively charged amino acid, the number of positively charged amino acids must be at least 1 or 2 for the net charge to remain neutral or positive.

[0048] In various embodiments, the amino acid sequence of the at least one peptide does not comprise any charged amino acid residues within the first 8 N-terminal amino acid residues. In particularly preferred embodiments, the amino acid sequence of the at least one peptide does not comprise any charged amino acid residues at all.

[0049] It is particularly preferred that the amino acid sequence of the at least one peptide comprises at least one of the sequence motifs AHHH, AAHA, or AHHHAAHA, preferably in an N- to C-terminal orientation. Optionally, the sequence motifs mentioned can occur multiple times in the amino acid sequence; in particular, the amino acid sequence of the at least one peptide comprises or consists of the sequence motif (AHHHAAHA)3, preferably in an N- to C-terminal orientation.

[0050] In various embodiments, the amino acid sequence of the at least one peptide comprises at least the sequence motif GHHPH, preferably in an N- to C-terminal orientation. Optionally, said sequence motif can occur multiple times in the amino acid sequence; in particular, the amino acid sequence comprises or consists of (GHHPH)2, (GHHPH)3, or (GHHPH)4, preferably in an N- to C-terminal orientation.

[0051] Furthermore, the amino acid sequence of the at least one peptide can contain at least one aromatic amino acid, preferably selected from W, Y or F, at any position, e.g., at least 2 or at least 3 or at least 4 or at least 5 aromatic amino acids. If, in some embodiments, the peptide contains an aromatic amino acid, an uncharged amino acid is preferably located next to such an aromatic amino acid. In various embodiments, however, two aromatic amino acids can also be located next to one another, e.g., W and Y. However, in various embodiments, it is particularly preferred that the at least one peptide does not comprise an aromatic amino acid.

[0052] In various embodiments, the at least one peptide consists of at least 60% amino acid residues with a high alpha-helix-forming potential, wherein these amino acid residues are preferably selected from E, A, L, M, Q, K, R, F, I, H and W, more preferably from E, A, L, Q, K, R, F, I, H and W, in particular from A, F, I, and H. In various embodiments, the peptide can also consist of at least 65%, at least 69%, at least 80%, at least 81% or 100% amino acid residues with a high alpha-helix-forming potential.

[0053] In particular, the aromatic amino acids phenylalanine (F) and tryptophan (W) are used as helix formers in the peptide sequence of the at least one peptide of the washing or cleaning agent according to the invention.

[0054] In various embodiments, the at least one peptide has a helical structure. An example of such a peptide is a peptide that comprises or consists of, but is not limited to, the amino acid sequence shown in SEQ ID NO:1.

[0055] However, it is also possible for the amino acid sequence to comprise helix-breaking amino acid residues, in particular glycine (G) and / or proline (P). Such peptides do not have a helical structure, which in the context of this invention is referred to as a "flexible structure." An example of such a peptide is a peptide that comprises or consists of the amino acid sequence according to SEQ ID NO:4, but is not limited thereto.

[0056] Furthermore, in the context of this invention, there are peptides that have a mixed structure of helical and flexible regions.

[0057] The washing or cleaning agent according to the invention preferably comprises at least one peptide which comprises or consists of an amino acid sequence which has at least 80%, preferably at least 81%, more preferably at least 82%, even more preferably at least 83%, even more preferably at least 84%, even more preferably at least 85%, even more preferably at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.5% or 100% sequence identity with one of the following amino acid sequences:

[0058] • AHHHAAHAAHHHAAHAAHHHAAHA (SEQ ID NO:1),

[0059] • FIHHIIGWISHGVRAIHRAIH (SEQ ID NO:2),

[0060] • GLFHAIAHFIHGGWHGLIHGWYG (SEQ ID NO:3),

[0061] • GHHPHGHHPHGHHPHGHHPH (SEQ ID NO:4) or

[0062] • GHGLGHGHEQQHGLGHGHKF (SEQ ID NO:5), in particular with one of the amino acid sequences AHHHAAHAAHHHAAHAHAHHHAAHA (SEQ ID NO:1) or GHHPHGHHPHGHHPHGHHPH (SEQ ID NO:4).

[0063] A peptide that has at least 80% sequence identity with one of the amino acid sequences 1-5 but does not match it is called a variant.

[0064] The term "variant," as used herein, refers to variants of the at least one peptide that retain the functionality of the parent peptide, 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 be in the range of 80% relative to the total length of the parent peptide, 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%.

[0065] In preferred embodiments, the washing or cleaning agent comprises at least one peptide having an amino acid sequence that comprises or consists of one of the amino acid sequences listed in SEQ ID NOs: 1-5. It is particularly preferred that the one amino acid sequence comprises or consists of one of the amino acid sequences listed in SEQ ID NO: 1 or SEQ ID NO: 4.

[0066] 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, pp. 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 Research 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 NTIR Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the specified standard parameters; its AlignX module for sequence comparisons is based on ClustalW. Unless otherwise stated, the sequence identity stated herein is determined using the BLAST algorithm.

[0067] 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 peptide / 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 peptides, 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. However, such small regions often perform essential functions for the overall activity of the peptide / protein. It may therefore be useful to refer sequence matches only to individual, possibly small regions. Unless otherwise stated, statements of identity or homology in this application refer to the entire length of the respective amino acid sequence indicated.

[0068] 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., 177 (1948), pp. 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.

[0069] The at least one peptide comprised in the washing or cleaning agent according to the invention may have amino acid modifications, in particular amino acid substitutions, insertions, or deletions. Such peptides are further developed, for example, by targeted genetic modification, ie, by mutagenesis methods, and optimized for specific applications or with regard to specific properties (e.g., with regard to their stability, binding, etc.).

[0070] For example, targeted mutations such as substitutions, insertions, or deletions can be introduced into known molecules to alter certain properties. This can be achieved by altering the surface charges and / or the isoelectric point of the molecules, and thus their interactions with certain compounds. For example, the net charge of the peptides can be altered to influence their binding and / or adhesion behavior. Alternatively or additionally, one or more corresponding mutations can increase the stability of the peptide. Advantageous properties of individual mutations, such as individual substitutions, can complement each other.

[0071] The following convention is used to describe substitutions that affect exactly one amino acid position (amino acid exchanges): first, the naturally occurring amino acid is named using the internationally used one-letter code, followed by the corresponding sequence position and finally the inserted amino acid. Multiple exchanges within the same peptide chain are separated by slashes. In the case of insertions, additional amino acids are named after the sequence position. In the case of deletions, the missing amino acid is replaced by a symbol, e.g., an asterisk or a dash, or an A is indicated in front of the corresponding position. For example, P9T describes the substitution of proline at position 9 with threonine, P9TH the insertion of histidine after the amino acid threonine at position 9 and P9* or AP9 the deletion of proline at position 9.This nomenclature is known to those skilled in the field of enzyme technology.

[0072] Thus, the washing or cleaning agent according to the invention can also comprise peptides which are characterized in that they are obtainable from a peptide as described above as the starting molecule, e.g. from a molecule with one of the amino acid sequences according to SEQ ID NOs: 1-5, preferably SEQ ID NO: 1 or SEQ ID NO: 4, on which e.g. one or more amino acid substitutions, including single or multiple conservative amino acid substitutions, have been carried out, the resulting peptide having at least 80% sequence identity with one of the amino acid sequences according to SEQ ID NOs: 1-5, preferably SEQ ID NO: 1 or SEQ ID NO: 4.

[0073] The term "conservative amino acid substitution" means the exchange (substitution) of one amino acid residue for another amino acid residue, whereby this exchange does not result in a change in the polarity or charge at the position of the exchanged amino acid, e.g., the exchange of a nonpolar amino acid residue for another nonpolar amino acid residue. Conservative amino acid substitutions within the scope of the invention include, for example: G=A=S, I=V=L=M, D=E, N=Q, K=R, Y=F, S=T, G=A=I=V=L=M=Y=F=W=P=S=T.

[0074] In preferred embodiments, the peptide of the invention can also be modified. Preferred modifications can include, for example, coupling the peptide of the invention 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.

[0075] All of the above features and embodiments can be implemented individually or in any combination.

[0076] Furthermore, the at least one peptide comprised in the washing or cleaning agent 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, in particular 2 to 10 repeats, e.g. 2, 3, 4, 5 or 6 repeats of the at least one peptide. The polypeptide can comprise or consist of such multimers. The term “polypeptide” in this context refers in particular to peptides which comprise 100 or more amino acids. The term “larger peptides” preferably refers to peptides with at least 40 amino acids, unless otherwise described.

[0077] In various embodiments, the at least one peptide of the washing or cleaning agent 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.

[0078] The peptides described herein can, in various embodiments, be chemically synthesized and / or produced recombinantly by protein design. Short peptides are now easily synthesized, e.g., using solid-phase synthesis such as the Merrifield solid-phase synthesis. Longer peptides and polypeptides, on the other hand, are often also produced recombinantly in the host organism, e.g., in bacteria or yeast.

[0079] It is preferable to produce the peptides for the washing or cleaning agent according to the invention using recombinant processes. These include all genetic engineering or microbiological processes based on the introduction of the genes for the peptides of interest into a host organism suitable for production and their transcribing and translation by this host organism (collectively referred to as biotechnological processes 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 comprising the gene and promoter, and possibly other genetic elements, is typically referred to as an expression cassette.However, it does not necessarily have to exist as a physical unit.

[0080] The peptides of the washing or cleaning agent according to the invention are particularly preferably produced as polypeptides (multimers) and subsequently cleaved into the functional peptides. Very particularly preferred multimers have 1 to 30 peptide units (each according to the invention), each separated from one another by spacers of 1 to 10 amino acids in length (e.g., 1, 2, 3, or 4 amino acids). Alternatively, the spacers can also be or comprise cleavage sites for specific proteases / peptidases, in particular endopeptidases, or form such a cleavage site together with parts of the peptide.

[0081] Using methods that are generally known today, such as chemical synthesis or the polymerase chain reaction (PCR) in conjunction with standard molecular biological and / or protein chemical methods, it is possible for a person skilled in the art to produce the corresponding nucleic acids up to complete genes based on known DNA and / or amino acid sequences and then to use these for the synthesis of peptides and polypeptides in suitable host cells.

[0082] In particularly preferred embodiments, the peptide described herein is produced by biotechnological methods as described above.

[0083] Embodiments of the present invention may also be cell-free expression systems in which peptide biosynthesis is replicated in vitro. Such expression systems are also established in the prior art.

[0084] The in vivo synthesis of a peptide for the washing or cleaning agent according to the invention, i.e., by living cells, requires the transfer of the corresponding gene into a host cell, the so-called transformation. In principle, all organisms are suitable as host cells, i.e., prokaryotes, eukaryotes, or cyanophyta. Preferred host cells are those that are genetically easy to handle, e.g., with regard to transformation with the expression vector and its stable establishment, e.g., unicellular fungi such as yeasts 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 peptides.Often, the optimal expression systems for a specific case must be determined experimentally from the wealth of different systems available today. Each peptide described herein can be obtained from a variety of host organisms in this way.

[0085] Suitable host cells include those whose activity can be regulated by genetic regulatory elements, which may be provided on the expression vector, for example, but may also be present in these cells from the outset. These cells can be stimulated to express proteins, for example, through the controlled addition of chemical compounds that serve as activators, by changing the cultivation conditions, or upon reaching a certain cell density. This enables highly economical production of the peptides of interest.

[0086] Preferred host cells are prokaryotic or bacterial cells. Bacteria are generally characterized by shorter generation times and lower demands on cultivation conditions compared to eukaryotes. This allows for the establishment of cost-effective processes for obtaining the peptides of the washing or cleaning agent according to the invention. In Gram-negative bacteria, such as E. coli, a large number of peptides are secreted into the periplasmic space, i.e., the compartment between the two membranes enclosing the cells. This can be advantageous for specific applications. Gram-positive bacteria, such as Bacilli or Actinomycetes or other representatives of the Actinomycetales, in contrast, do not have an outer membrane, so that secreted peptides are immediately released into the nutrient medium surrounding the cells, from which, according to another preferred embodiment, the expressed peptides can be directly purified.

[0087] A variation of this principle is represented by expression systems in which additional genes, e.g., those provided on other vectors, influence the production of the peptides described herein. These can be modifying gene products or those that are to be co-purified with the peptide described herein.

[0088] Due to the extensive experience gained, for example, with regard to molecular biological methods and culturability with coliform bacteria, these represent preferred embodiments. Particularly preferred are those of the genera Escherichia coli, in particular non-pathogenic strains suitable for biotechnological production.

[0089] Eukaryotic cells can also be suitable for producing the peptides described herein. Examples of these are fungi such as actinomycetes or yeasts such as Saccharomyces or Kluyveromyces. This can be particularly advantageous, for example, if the peptides are to undergo specific modifications in connection with their synthesis that enable such systems. All of the elements already explained above can be combined to form processes for producing the at least one peptide of the washing or cleaning agents according to the invention. These processes for producing the peptides described herein preferably represent further aspects of the present invention. A multitude of possible combinations of process steps are conceivable for each peptide described herein. Optimal conditions could be determined experimentally by the person skilled in the art for each specific case.

[0090] Preferably, the at least one peptide comprised in the washing or cleaning agent according to the invention is suitable for adhesion and / or binding to dyes, in particular it is a dye transfer inhibitor.

[0091] In the context of this invention, "adhesion" refers to an interaction between the peptide and a surface, allowing the peptide to adhere to the surface. Thus, an "adhesive peptide" refers to a peptide that has the ability to interact with and / or adhere to a specific surface. The adhesive peptides described herein preferably exhibit 10-fold, more preferably 20-fold, 50-fold, or 100-fold higher adhesion to a given surface than any alternative peptide of comparable length that was not developed for this purpose and does not meet the sequence specifications described herein.

[0092] The term “binding” in the context of this invention preferably refers to “covalent bonds” between the peptide and a surface.

[0093] It is particularly preferred that the at least one peptide of the washing or cleaning agent according to the invention reduces or prevents dye transfer to textiles, in particular by binding and / or adhering to dyes, and in particular protects the textiles from discoloration. Thus, the washing or cleaning agent is preferably used as a detergent in a washing process, in particular in machine or hand washing.

[0094] In various embodiments, the peptide described herein can be used in the washing or cleaning agent according to the invention, without being limited thereto, in a concentration of 0.00001 to 5 wt.%, e.g. in a concentration of 0.0001 to 2 wt.% or 0.001 to 1 wt.%.

[0095] In preferred embodiments, the washing or cleaning agent is a detergent. Examples of agents that fall under the term washing or cleaning agent have already been mentioned above.

[0096] The washing or cleaning agent according to the invention is particularly suitable for use on textiles made of plastic and / or with a plastic component (mixed fabric) and / or made of a natural fiber such as cotton. The term "mixed fabric" preferably refers to textiles made of at least one natural fiber and at least one plastic fiber (plastic component).

[0097] 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.

[0098] In preferred embodiments, the washing or cleaning agent according to the invention comprises at least one surfactant.

[0099] Anionic, cationic, non-ionic and / or amphoteric surfactants can be used as surfactants in the washing or cleaning agent according to the invention, without being limited thereto.

[0100] In preferred embodiments, the at least one surfactant is present in an amount of 0.5 to 60 wt.%, e.g. 0.5 to 50 wt.% or 2 to 45 wt.%, preferably 0.6 to 45 wt.%, e.g. 0.7 to 30 wt.% or 0.8 to 20 wt.%, 1 to 15 wt.% or 3 to 44 wt.%, based on the total weight of the washing or cleaning agent.

[0101] In preferred embodiments, the washing or cleaning agent according to the invention comprises at least one anionic surfactant.

[0102] Anionic surfactants are important components of detergents and cleaning agents because they remove a wide variety of textile soils and are particularly effective against greasy soils. They are widely available commercially and demonstrate good cleaning performance on soiled surfaces. The surfactants used can be of petrochemical, plant, or microbiological origin.

[0103] Suitable anionic surfactants of the sulfonate type include, for example, Cg-n-alkylbenzenesulfonates and olefinsulfonates, i.e., mixtures of alkene and hydroxyalkanesulfonates and disulfonates, such as those obtained, for example, from Cs-monoolefins with a terminal or internal double bond by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acidic hydrolysis of the sulfonation products. Also suitable are alkanesulfonates obtained from Cs-alkanes, for example, by sulfochlorination or sulfoxidation with subsequent hydrolysis or neutralization. Esters of α-sulfofatty acids (estersulfonates), e.g., the α-sulfonated methyl esters of hydrogenated coconut, palm kernel, or tallow fatty acids, are also suitable.

[0104] Other suitable anionic surfactants are sulfated fatty acid glycerol esters. Fatty acid glycerol esters are understood to be the mono-, di-, and triesters, as well as mixtures thereof, as obtained by esterification of a monoglycerol with 1 to 3 mol of fatty acid or by transesterification of triglycerides with 0.3 to 2 mol of glycerol. Preferred sulfated fatty acid glycerol esters are the sulfonation products of saturated fatty acids with 6 to 22 carbon atoms, e.g., caproic acid, caprylic acid, capric acid, myristic acid, lauric acid, palmitic acid, stearic acid, or behenic acid.

[0105] Preferred alk(en)yl sulfates are the alkali metal salts, especially the sodium salts, of the sulfuric acid half-esters of C12-18 fatty alcohols, e.g., coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or C10-20 oxo alcohols, and those half-esters of secondary alcohols of these chain lengths. Also preferred are alk(en)yl sulfates of the stated chain length that contain a synthetic, petrochemically produced straight-chain alkyl radical, which exhibit degradation behavior similar to that of equivalent compounds based on oleochemical raw materials. For washing purposes, C18-e-alkyl sulfates and C12-15-alkyl sulfates, as well as C18-s-alkyl sulfates, are preferred. 2,3-Alkyl sulfates are also suitable anionic surfactants.

[0106] Sulfuric acid monoesters of straight-chain or branched C7-2i alcohols ethoxylated with 1 to 6 mol of ethylene oxide, such as 2-methyl-branched C8-n alcohols with an average of 3.5 mol of ethylene oxide (EO) or C8-s fatty alcohols with 1 to 4 EO, are also suitable. In various embodiments, the washing or cleaning agent according to the invention can contain 0.01 to 5 wt.% of an ethoxylated fatty alcohol sulfate.

[0107] Other suitable anionic surfactants are the salts of alkyl sulfosuccinic acid, which are also referred to as sulfosuccinates or sulfosuccinic acid esters and are monoesters and / or diesters of sulfosuccinic acid with alcohols, preferably fatty alcohols and especially ethoxylated fatty alcohols. Preferred sulfosuccinates contain C8-11 fatty alcohol residues or mixtures thereof. Particularly preferred sulfosuccinates contain a fatty alcohol residue derived from ethoxylated fatty alcohols. Sulfosuccinates whose fatty alcohol residues are derived from ethoxylated fatty alcohols with a narrow homolog distribution are particularly preferred. It is also possible to use alk(en)ylsuccinic acid, preferably with 8 to 18 carbon atoms in the alk(en)yl chain, or salts thereof.

[0108] If a fatty acid soap is contained in the washing or cleaning agent, saturated and unsaturated fatty acid soaps are suitable, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, (hydrogenated) erucic acid and behenic acid, as well as soap mixtures derived in particular from natural fatty acids, e.g. coconut, palm kernel, olive oil or tallow fatty acids.

[0109] The anionic surfactants, including soaps, if present, can preferably be present in the form of their sodium, potassium, or magnesium salts. The anionic surfactants are preferably present in the form of their sodium salts.

[0110] In various embodiments, the at least one surfactant may comprise an anionic surfactant, for example, but not limited to, a linear or branched alkylbenzenesulfonate and / or a sodium lauryl ether sulfate and / or alpha-olefin sulfonate.

[0111] In various embodiments, the washing or cleaning agent according to the invention comprises 0.3 to 50 wt.% anionic surfactant, e.g. 1 to 45 wt.% or 3 to 40 wt.%, based on the total weight of the washing or cleaning agent.

[0112] In various embodiments, the at least one surfactant comprises a nonionic surfactant, e.g., without being limited thereto, a nonionic surfactant from the group of alkoxylated fatty alcohols, alkoxylated fatty acid alkyl esters, fatty acid amides, alkoxylated fatty acid amides, polyhydroxy fatty acid amides, alkylphenol polyglycol ethers, amine oxides, alkyl polyglucosides and mixtures thereof, more preferably from the group of alcohol ethoxylates, even more preferably a C s-alcohol ethoxylate having 7 EO units. The nonionic surfactant is preferably present in an amount of 0.5 to 50 wt.%, more preferably from 0.6 to 45 wt.%, e.g. from 0.7 to 30 wt.% or 0.8 to 20 wt.% or 1 to 15 wt.%, based on the total weight of the washing or cleaning agent.

[0113] Non-ionic surfactants used are preferably alkoxylated, advantageously ethoxylated, in particular primary alcohols with preferably 8 to 18 C atoms and an average of 1 to 12 mol of ethylene oxide (EO) per mole of alcohol, in which the alcohol radical can be linear or preferably methyl-branched in the 2-position or can contain linear and methyl-branched radicals in the mixture, as are usually present in oxo alcohol radicals. In particular, however, alcohol ethoxylates with linear radicals from alcohols of native origin with 12 to 18 C atoms, e.g. from coconut, palm, tallow or oleyl alcohol, and an average of 2 to 8 EO per mole of alcohol are preferred. The preferred ethoxylated alcohols include, for example, C12-14 alcohols with 3 EO, 4 EO or ? EO, Cg-n-alcohol with 7 EO, Cs-alcohols with 3 EO, 5 EO, 7 EO or 8 EO, Cs-alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C12-14 alcohol with 3 EO and C12-18 alcohol with 7 EO.The stated degrees of ethoxylation represent statistical averages, which can be a whole or fractional number for a specific product. Preferred alcohol ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples of these are tallow fatty alcohol with 14 EO, 25 EO, 30 EO or 40 EO. Nonionic surfactants that contain EO and PO groups together in the molecule can also be used according to the invention. Block copolymers with EO-PO block units or PO-EO block units can be used, as can EO-PO-EO copolymers or PO-EO-PO copolymers. Mixed alkoxylated nonionic surfactants can of course also be used, in which EO and PO units are distributed randomly rather than in blocks. Such products are obtained by the simultaneous action of ethylene and propylene oxide on fatty alcohols.

[0114] In addition, alkyl glucosides of the general formula RO(G)x can also be used as further nonionic surfactants, in which R is a primary straight-chain or methyl-branched, in particular 2-methyl-branched, aliphatic radical having 8 to 22, preferably 12 to 18, carbon atoms, and G is the symbol representing a glycoside unit having 5 or 6 carbon atoms, preferably glucose. The degree of oligomerization x, which indicates the distribution of monoglycosides and oligoglycosides, is any number between 1 and 10; preferably, x is between 1.2 and 1.4.

[0115] Another class of preferred nonionic surfactants, which are used either as the sole nonionic surfactant or in combination with other nonionic surfactants, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably with 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters.

[0116] Nonionic surfactants of the amine oxide type, e.g., N-cocoalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and fatty acid alkanolamides may also be suitable. The amount of these nonionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, in particular no more than half that amount.

[0117] Other suitable surfactants are polyhydroxy fatty acid amides of the formula (I), R 1

[0118] R _CO-N-[T] (|) in which RCO represents an aliphatic acyl radical having 6 to 22 carbon atoms, R 1represents hydrogen, an alkyl or hydroxyalkyl radical having 1 to 4 carbon atoms, and [T] represents a linear or branched polyhydroxyalkyl radical having 3 to 10 carbon atoms and 3 to 10 hydroxyl groups. Polyhydroxy fatty acid amides are known substances that can usually be obtained by reductive amination of a reducing sugar with ammonia, an alkylamine, or an alkanolamine, followed by acylation with a fatty acid, a fatty acid alkyl ester, or a fatty acid chloride.

[0119] The group of polyhydroxy fatty acid amides also includes compounds of formula (II), in which R represents a linear or branched alkyl or alkenyl radical having 7 to 12 carbon atoms, R 1 represents a linear, branched or cyclic alkyl radical or an aryl radical with

[0120] 2 to 8 carbon atoms and R 2represents a linear, branched or cyclic alkyl radical or an aryl radical or an oxyalkyl radical having 1 to 8 carbon atoms, with C 1-4 alkyl or phenyl radicals being preferred, and [T] represents a linear polyhydroxyalkyl radical whose alkyl chain is substituted by at least two hydroxyl groups, or alkoxylated, preferably ethoxylated or propoxylated derivatives of this radical. [T] is preferably obtained by reductive amination of a sugar, e.g. glucose, fructose, maltose, lactose, galactose, mannose or xylose. The N-alkoxy- or N-aryloxy-substituted compounds can then be converted into the desired polyhydroxy fatty acid amides by reaction with fatty acid methyl esters in the presence of an alkoxide as catalyst.

[0121] However, it may be preferred for the washing or cleaning agent to have a washing or cleaning agent matrix based purely on nonionic surfactants. In particular, with regard to the environmental friendliness of the washing or cleaning agent, it may be preferred for the washing or cleaning agent to contain predominantly surfactants from renewable raw materials and for the proportion of synthetic surfactants to be as low as possible or even zero.

[0122] Suitable cationic surfactants include the quaternary ammonium compounds of the formula (R i )(R ii )(R iii )(R iv )N + X', in the R' to R ivrepresent four identical or different, in particular two long- and two short-chain, alkyl radicals and X- represents an anion, in particular a halide ion, e.g. didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride, alkyldimethylhydroxyethylammonium chloride, bromide or methylsulfate, in particular with Ci2-alkyl, and mixtures thereof. The washing or cleaning agents can, in various embodiments, contain cationic surfactants in amounts, based on the total weight of the washing or cleaning agent, of 0.001 to 10 wt.%, preferably 0.01 to 5 wt.%, in particular 0.1 to

[0123] 3 wt.%. Suitable amphoteric surfactants (zwitterionic surfactants) include, for example, betaines, alkylamidoalkylamines, alkyl-substituted amino acids, acylated amino acids, or biosurfactants, of which betaines are preferred within the scope of the invention.

[0124] In a preferred embodiment, the washing or cleaning agent according to the invention contains at least one enzyme.

[0125] The washing or cleaning agent of the present invention may comprise at least one enzyme or a combination of different enzymes to ensure sufficient cleaning action. Enzymes are preferably used in liquid, more preferably in liquid, aqueous washing or cleaning agents.

[0126] Enzymes preferably used according to the invention are amylases, proteases, (hemi)cellulases, peroxidases and / or lipases, without being limited thereto.

[0127] Amylases can be added, for example, to remove starch and glycogen. Alpha-, beta-, and gamma-amylases (α-, β-, γ-amylases), as well as glucoamylases and maltogenic amylases, can be used according to the invention. The amylases can originate from any source, such as bacteria, fungi, pancreatic glands of animal origin, germinated grains, yeasts, etc. Genetically modified amylases can also be used, possibly even preferably, in the washing or cleaning agents according to the invention.

[0128] The amylase enzymes can be present in the washing or cleaning agents according to the invention in an amount of 0.00001 to 5 wt.%, preferably 0.0001 to 1 wt.%, more preferably 0.0005 to 0.5 wt.% and in particular 0.01 to 0.4 wt.%, based on the total weight of the washing or cleaning agent.

[0129] In addition to amylases, proteases can also be added to the detergents or cleaning agents according to the invention to cleave proteins and peptide residues. Proteases are particularly suitable for the hydrolytic cleavage and removal of protein residues, especially dried-on protein residues.

[0130] Proteases suitable according to the invention are proteinases (endopeptidases) and peptidases (exopeptidases). Usable proteases can be of plant, animal, bacterial, and / or fungal origin. Suitable proteases are, in particular, serine, cysteine, aspartate, and metalloproteases. Genetically modified proteases can also be used, possibly even preferably, in the washing or cleaning agents according to the invention.

[0131] Typically, proteases are used in the range of 0.00001 to 1.5 wt.%, preferably in the range of 0.0001 to 0.75 wt.%, based on the total weight of the washing or cleaning agents.

[0132] Furthermore, lipases can be added to detergents or cleaning agents according to the invention to remove stubborn greasy soils. Lipases are thus a bio-alternative to surfactants and can, for example, support the cleaning action of surfactants in amounts of 0.0001 to 1 wt.%. Suitable lipases can be obtained from plants (e.g., castor oil species), microorganisms, and animal sources, such as pancreatic lipases. The aforementioned enzymes can be added individually or in any desired combination of mixtures with one another to the detergents and cleaning agents according to the invention. Amylases, in particular α-amylases, and proteases are particularly preferred for use in detergents and cleaning agents according to the invention.

[0133] The addable enzymes can optionally be combined with any other enzymes to further improve the cleaning performance of the detergents or cleaning agents. Other enzymes suitable according to the invention include, but are not limited to, reductases, oxidases, ligninases, cutinases, pectinases, xylanases, phenoloxidases, lipoxygenases, tannases, pentosanases, malanases, glucanases, arabinosidases, and any mixtures of these enzymes.

[0134] In a preferred embodiment, the at least one enzyme is used in the washing and cleaning agent according to the invention in an amount of 0.00001 to 5 wt.%, preferably 0.0001 to 2 wt.%, more preferably 0.001 to 1.5 wt.%, based on the total weight of the washing or cleaning agent.

[0135] Amylases are known to be stabilized by the addition of calcium chloride ions. Boric acid / borates / perborates, in combination with glycerol and / or PEG, as well as nonionic surfactants with available hydroxyl groups, are other suitable stabilizing agents.

[0136] Further suitable additives for the washing or cleaning agent according to the invention can be selected from, for example, builders, bleaching agents, bleach catalysts, bleach activators, electrolytes, pH adjusters, perfumes, perfume carriers, fluorescent agents, dyes, dye transfer inhibitors (DTI polymers), hydrotropes, foam inhibitors / defoamers, silicone oils, soil release polymers / soil repellent polymers, graying inhibitors, shrinkage inhibitors, crease inhibitors, antimicrobial agents, solvents, germicides, fungicides, antioxidants, preservatives, corrosion inhibitors, antistatic agents, bittering agents, ironing aids, repellents and impregnating agents, skin-care agents, swelling and slip-resistant agents, complexing agents, softening components and UV absorbers and mixtures thereof, in particular solvents such as water and / or organic solvents, thickeners, Stabilizers, soil release polymers / soil repellent polymers,Fragrances or perfumes, complexing agents, pH adjusters, foam inhibitors / defoamers and / or mixtures thereof.

[0137] In a preferred embodiment, the washing or cleaning agent according to the invention comprises the at least one additive in an amount of 0.0001 to 30 wt.%, preferably 0.1 to 20 wt.%, more preferably 1 to 10 wt.%, based on the total weight of the washing or cleaning agent. Water is preferably not included in this concentration and can be added in addition to the washing or cleaning agent according to the invention.

[0138] The washing or cleaning agent preferably contains at least one perfume or fragrance, or optionally a mixture of different perfumes or fragrances as the at least one additive.

[0139] Individual fragrance compounds, e.g., synthetic products of the ester, ether, aldehyde, ketone, alcohol, and hydrocarbon type, can be used as perfume oils or fragrances within the scope of the present invention. However, mixtures of different fragrances are preferably used, which together produce an appealing fragrance. Such perfume oils can also contain natural fragrance mixtures, such as those obtainable from plant sources, e.g., pine, citrus, jasmine, patchouli, rose, or ylang-ylang oil. Suitable fragrances and perfumes, or mixtures thereof, are known to those skilled in the art of detergent or cleaning agent production.

[0140] In a preferred embodiment, the washing or cleaning agent contains one or more fragrances in an amount of usually up to 15% by weight, preferably 0.01 to 5% by weight, in particular 0.3 to 3% by weight, based on the total weight of the washing or cleaning agent.

[0141] The washing or cleaning agent according to the invention may further contain one or more builders.

[0142] In a further preferred embodiment, the washing or cleaning agent contains water-soluble and / or water-insoluble builder, in particular selected from alkali aluminosilicate, crystalline alkali silicate with a modulus above 1, monomeric polycarboxylate, polymeric polycarboxylate and mixtures thereof, in particular in amounts in the range from 2.5 to 30% by weight, based on the total weight of the washing or cleaning agent.

[0143] Water-soluble organic builder substances include, in particular, those from the class of polycarboxylic acids, especially citric acid and sugar acids, as well as polymeric (poly)carboxylic acids, especially the polycarboxylates accessible by oxidation of polysaccharides, polymeric acrylic acids, methacrylic acids, maleic acids, and copolymers thereof, which may also contain small amounts of polymerizable substances without carboxylic acid functionality. The relative molecular weight of homopolymers of unsaturated carboxylic acids is generally between 5,000 g / mol and 200,000 g / mol, and that of copolymers between 2,000 g / mol and 200,000 g / mol, preferably 50,000 g / mol to 120,000 g / mol, based on the free acid. A particularly preferred acrylic acid-maleic acid copolymer has a relative molecular weight of 50,000 g / mol to 100,000 g / mol.Suitable, although less preferred, compounds of this class are copolymers of acrylic acid or methacrylic acid with vinyl ethers, such as vinyl methyl ethers, vinyl esters, ethylene, propylene and styrene, in which the proportion of acid is at least 50% by weight.

[0144] Terpolymers which contain two carboxylic acids and / or their salts as monomers and vinyl alcohol and / or a vinyl alcohol derivative or a carbohydrate as the third monomer can also be used as water-soluble organic builder substances. The first acidic monomer or its salt is derived from a monoethylenically unsaturated C3-8 carboxylic acid and preferably from a C3-4 monocarboxylic acid, in particular from (meth)acrylic acid. The second acidic monomer or its salt can be a derivative of a C4-5 dicarboxylic acid, with maleic acid being particularly preferred. The third monomeric unit in this case is formed from vinyl alcohol and / or preferably an esterified vinyl alcohol. In particular, vinyl alcohol derivatives which are an ester of short-chain carboxylic acids, e.g. of C1-4 carboxylic acids, with vinyl alcohol are preferred. Preferred terpolymers contain 60 to 95% by weight, in particular 70 to 90% by weight.-% (meth)acrylic acid and / or (meth)acrylate, more preferably acrylic acid and / or acrylate, and maleic acid and / or maleate as well as 5 to 40 wt.%, preferably 10 to 30 wt.% vinyl alcohol and / or vinyl acetate. Very particular preference is given to terpolymers in which the weight ratio of (meth)acrylic acid and / or (meth)acrylate to maleic acid and / or maleate is between 1:1 and 4:1, preferably between 2:1 and 3:1 and in particular 2:1 and 2.5:1. Both the amounts and the weight ratios are based on the acids. The second acidic monomer or its salt can also be a derivative of an allylsulfonic acid which is substituted in the 2-position by an alkyl radical, preferably by a C 1-4 alkyl radical, or an aromatic radical, which is preferably derived from benzene or benzene derivatives. Preferred terpolymers contain 40 to 60 wt.%, in particular 45 to 55 wt.-% (meth)acrylic acid and / or (meth)acrylate, more preferably acrylic acid and / or acrylate, 10 to 30 wt.%, preferably 15 to 25 wt.% methallylsulfonic acid and / or methallylsulfonate, and as a third monomer, 15 to 40 wt.%, preferably 20 to 40 wt.% of a carbohydrate. This carbohydrate can be, for example, a mono-, di-, oligo-, or polysaccharide, with mono-, di-, or oligosaccharides being preferred, and sucrose being particularly preferred. The use of the third monomer presumably introduces predetermined breaking points into the polymer, which are responsible for its good biodegradability. These terpolymers generally have a relative molecular mass between 1,000 g / mol and 200,000 g / mol, preferably between 2,000 g / mol and 50,000 g / mol, and especially between 3,000 g / mol and 10,000 g / mol. They can be used, particularly for the production of liquid agents, in the form of aqueous solutions, preferably in the form of 30 to 50 wt.% aqueous solutions.All of the polycarboxylic acids mentioned are generally used in the form of their water-soluble salts, especially their alkali salts.

[0145] As water-insoluble, water-dispersible inorganic builder materials, crystalline or amorphous alkali aluminosilicates are used in particular, in amounts of up to 50 wt.%, preferably not more than 40 wt.%, and in liquid compositions in particular from 1 to 5 wt.%. Among these, crystalline aluminosilicates of detergent quality, in particular zeolite NaA and optionally NaX, are preferred. Amounts close to the stated upper limit are preferably used in solid, particulate compositions. Suitable aluminosilicates, in particular, contain no particles with a grain size larger than 30 μm and preferably consist of at least 80 wt.% particles with a size smaller than 10 μm. Their calcium binding capacity, which can be determined according to the information in German patent DE 2412837 A1, is in the range of 100 to 200 mg CaO per gram.Suitable substitutes or partial substitutes for the aluminosilicate mentioned are crystalline alkali silicates, which can be present alone or in a mixture with amorphous silicates. The alkali silicates usable as builders in the agents preferably have a molar ratio of alkali oxide to SiO2 of less than 0.95, in particular of 1:1.1 to 1:12, and can be amorphous or crystalline. Preferred alkali silicates are sodium silicates, in particular amorphous sodium silicates, with a molar Na2O:SiO2 ratio of 1:2 to 1:2.8. Those with a molar Na2O:SiO2 ratio of 1:1.9 to 1:2.8 are preferably added as a solid during production rather than in the form of a solution.As crystalline silicates, which can be present alone or in a mixture with amorphous silicates, preference is given to using crystalline layered silicates of the general formula Na2SixO2x+i yH2O, in which x, the so-called modulus, is a number from 1.9 to 4 and y is a number from 0 to 20, and preferred values ​​for x are 2, 3 or 4. Preferred crystalline layered silicates are those in which x in the general formula mentioned assumes the values ​​2 or 3. In particular, both β- and β-sodium disilicates (Na2Si2O5 yH2O) are preferred. Practically anhydrous crystalline alkali silicates of the above general formula, in which x is a number from 1.9 to 2.1, prepared from amorphous alkali silicates, can also be used in the agents described herein. In a further preferred embodiment of the agent according to the invention, a crystalline sodium layer silicate with a modulus of 2 to 3 is used, such as can be produced from sand and soda.Crystalline sodium silicates with a modulus in the range from 1.9 to 3.5 are used in a further preferred embodiment in detergents. Their alkali silicate content is preferably 1 to 50% by weight and in particular 5 to 35% by weight, based on the anhydrous active substance. If alkali aluminosilicate, in particular zeolite, is also present as an additional builder substance, the alkali silicate content is preferably 1 to 15% by weight and in particular 2 to 8% by weight, based on the anhydrous active substance. The weight ratio of aluminosilicate to silicate, in each case based on the anhydrous active substances, is then preferably 4:1 to 10:1. In agents which contain both amorphous and crystalline alkali silicates, the weight ratio of amorphous alkali silicate to crystalline alkali silicate is preferably 1:2 to 2:1 and in particular 1:1 to 2:1.

[0146] In addition to the aforementioned inorganic builder, other water-soluble or water-insoluble inorganic substances may be present in the agents used together with it or employed in the methods according to the invention. Suitable in this context are alkali metal carbonates, alkali metal bicarbonates, and alkali metal sulfates, as well as mixtures thereof. Such additional inorganic material may be present in amounts of up to 30% by weight.

[0147] In preferred embodiments, the washing or cleaning agent according to the invention can contain at least one complexing agent. Complexing agents are also known as chelating agents or sequestering agents. Typically, a complexing agent can bind metal ions to prevent them from reacting with other components of a composition. For example, they can be added to washing or cleaning compositions to complex Ca and Mg ions to soften the water. Other complexing agents can preferably also contribute to the washing or cleaning performance.

[0148] Suitable complexing agents include condensed phosphates, phosphonates, and / or aminocarboxylic acids.

[0149] Examples of condensed phosphates include, but are not limited to, sodium and potassium orthophosphate, sodium and potassium pyrophosphate, sodium tripolyphosphate, and sodium hexametaphosphate.

[0150] Examples of phosphonic acids, phosphonates or derivatives thereof include, but are not limited to, 2-phosphonobutane-1,2,4-tricarboxylic acid (PBTC), 1-hydroxyethane-(1,1-diphosphonic acid) (HEDP), aminotrimethylenephosphonic acid (ATMP), 2-hydroxyethyliminobis-(methylenephosphonic acid), diethylenetriaminepenta-(methylenephosphonic acid) (DTPMP), ethylenediaminetetra-(methylenephosphonic acid) (EDTMP), hexamethylenediamine-(tetramethylenephosphonic acid), bis(hexamethylene)triamine-(pentamethylenephosphonic acid), phosphoric acid or suitable salts thereof.

[0151] In a preferred embodiment, the washing or cleaning agent according to the invention contains 1-hydroxyethane-(1,1-diphosphonic acid) (HEDP) or a suitable salt thereof.

[0152] Suitable aminocarboxylic acid materials containing little or no NTA include, but are not limited to, N-hydroxyethylaminodiacetic acid, ethylenediaminetetraacetic acid (EDTA), hydroxyethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid (DTPA), N-hydroxyethylethylenediaminetriacetic acid (HEDTA), methylglycinediacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), ethylenediaminesuccinylic acid (EDDS), 2-hydroxyethyliminodiacetic acid (HEIDA), iminodisuccinylic acid (IDS), 3-hydroxy-2-2'-iminodisuccinylic acid (HIDS) and other similar acids or salts thereof having an amino group with a carboxylic acid substituent.

[0153] In a preferred embodiment, however, the washing or cleaning agent is substantially free of aminocarboxylic acids.

[0154] If complexing agents are to be used in the washing or cleaning agent according to the invention, they are preferably used in an amount of 0.01 to 30 wt.%, more preferably 0.1 to 20 wt.%, even more preferably 0.2 to 15 wt.%, based on the total weight of the washing or cleaning agent.

[0155] The preferred solvent in the washing or cleaning agents according to the invention is water, but organic solvents can also be present in the washing or cleaning agents and partially replace the water.

[0156] Suitable organic solvents are, for example, saturated or unsaturated, preferably saturated, branched or unbranched C1-20 hydrocarbons, preferably C2-15 hydrocarbons, with one or more hydroxyl groups, preferably one hydroxyl group, and optionally one or more ether functions COC, ie oxygen atoms interrupting the carbon atom chain.

[0157] Preferred solvents are the C1-6 alcohols, in particular ethanol, n-propanol or isopropanol as well as the C2-6 alkylene glycols and poly-C2-3 alkylene glycol ethers - optionally etherified on one side with a C1-6 alkanol - with an average of 1 to 9 identical or different, preferably identical, alkylene glycol groups per molecule, in particular the poly-C2-3 alkylene glycol ethers etherified on one side with a C1-6 alkanol with an average of 1 to 9, preferably 2 to 3, ethylene or propylene glycol groups, e.g. PPG-2 methyl ether (dipropylene glycol monomethyl ether).

[0158] Beispielhafte Lösungsmittel sind die folgenden gemäß INCI benannten Verbindungen: Alcohol (Ethanol), Buteth-3, Butoxydiglycol, Butoxyethanol, Butoxyisopropanol, Butoxypropanol, n- Butylalcohol, t-Butylalcohol, Butylenglycol, Butyloctanol, Diethylenglycol, Dimethoxydiglycol, Dimethylether, Dipropylenglycol, Ethoxydiglycol, Ethoxyethanol, Ethylhexandiol, Glycol, Hexandiol, 1 ,2,6-Hexantriol, Hexylalcohol, Hexylenglycol, Isobutoxypropanol, Isopentyldiol, Isopropylalcohol (iso- Propanol), 3-Methoxybutanol, Methoxydiglycol, Methoxyethanol, Methoxyisopropanol, Methoxymethylbutanol, Methoxy PEG-10, Methylal, Methylalcohol, Methylhexylether, Methylpropandiol, Neopentylglycol, PEG-4, PEG-6, PEG-7, PEG-8, PEG-9, PEG-6 Methylether, Pentylenglycol, PPG-7, PPG-2-Buteth-3, PPG-2 Butylether, PPG-3 Butylether, PPG-2 Methylether, PPG-3 Methylether, PPG-2 Propylether, Propandiol, Propylalcohol (n-Propanol), Propylenglycol, Propylenglycolbutylether, Propylenglycolpropylether, Tetrahydrofurfurylalcohol,Trimethylhexanol, together with aliphatic or aromatic alcohols, e.g. methanol, ethanol, n-propanol, n-butanol, tert-butanol or phenol, or carboxylic acids, e.g. acetic or carbonic acid, etherified or esterified monomers or homo- or heteropolymers, in particular monomers and homodi- and trimers, C2-4-alkylene glycols.

[0159] In a preferred embodiment of the invention, the washing or cleaning agents contain one or more hydrophobic components. The hydrophobic components not only improve the cleaning effect against hydrophobic contaminants such as greasy soils, but in multi-phase washing or cleaning agents also have a positive effect on phase separation and its reversibility. Suitable hydrophobic components are, for example, dialkyl ethers with identical or different C4 to C8 alkyl radicals, in particular linear dioctyl ether; hydrocarbons with a boiling range of 100 to 300°C, in particular 140 to 280°C, e.g. aliphatic hydrocarbons with a boiling range of 145 to 200°C, isoparaffins with a boiling range of 200 to 260°C; essential oils, in particular limonene and pine oil extracted from pine roots and stumps; and also mixtures of these hydrophobic components, in particular mixtures of two or three of the hydrophobic components mentioned.Preferred mixtures of hydrophobic components are mixtures of various dialkyl ethers, of dialkyl ethers and hydrocarbons, of dialkyl ethers and essential oils, of hydrocarbons and essential oils, of dialkyl ethers and hydrocarbons and essential oils, and of these mixtures. The washing or cleaning agents can contain hydrophobic components in amounts, based on the total weight of the washing or cleaning agent, of 0.01 to 20 wt.%, preferably 0.1 to 14 wt.%, more preferably 0.5 to 10 wt.%, even more preferably 0.8 to 7 wt.%.

[0160] If the detergents or cleaning agents according to the invention are formulated in multiple phases, they may contain one or more phase separation agents. Suitable phase separation agents, in addition to citric acid and citrates, include alkali metal and alkaline earth metal halides, especially chlorides, and sulfates and nitrates, especially sodium and potassium chloride and sulfate, as well as ammonium chloride and sulfate, or mixtures thereof.

[0161] Such salts, as strong electrolytes that increase ionic strength, support phase separation through the salt effect. Sodium chloride has proven particularly effective in this regard, while sodium sulfate and especially magnesium sulfate have a lesser phase-separating effect. The detergents or cleaning agents may contain phase-separating agents in amounts, based on the total weight of the detergent or cleaning agent, of 0.01 to 30 wt.%, preferably 0.1 to 20 wt.%, e.g., 1 to 15 wt.% or 1 to 5 wt.%.

[0162] To adjust the viscosity, the washing or cleaning agent according to the invention may contain one or more thickeners, preferably in an amount of 0.01 to 5% by weight, more preferably 0.05 to 2.5% by weight, even more preferably 0.1 to 1% by weight. Suitable thickeners are, for example, organic natural thickeners (agar-agar, carrageenan, tragacanth, gum arabic, alginates, pectins, polyoses, guar flour, locust bean gum, starch, dextrins, gelatin, casein), organic modified natural substances (carboxymethylcellulose and other cellulose ethers, hydroxyethyl and propylcellulose and the like, kernel flour ethers), organic fully synthetic thickeners (polyacrylic and polymethacrylic compounds, vinyl polymers, polycarboxylic acids, polyethers, polyimines, polyamides) and inorganic thickeners (polysilicic acids, clay minerals such as montmorillonites, zeolites, silicas).

[0163] Polyacrylic and polymethacrylic compounds include, for example, the high-molecular homopolymers of acrylic acid crosslinked with a polyalkenyl polyether, in particular an allyl ether of pentaerythritol or propylene (INCI name according to the International Dictionary of Cosmetic Ingredients of The Cosmetic, Toiletry, and Fragrance Association (CTFA): Carbomer), which are also referred to as carboxyvinyl polymers.Furthermore, the following acrylic acid copolymers fall under this category: (i) copolymers of two or more monomers from the group of acrylic acid, methacrylic acid and their simple esters, preferably formed with C 1-4 -alkanols (INCI Acrylates Copolymer), which include, for example, the copolymers of methacrylic acid, butyl acrylate and methyl methacrylate (CAS name according to the Chemical Abstracts Service: 25035-69-2) or of butyl acrylate and methyl methacrylate (CAS 25852-37-3); (ii) crosslinked high molecular weight acrylic acid copolymers, which include, for example, the copolymers of C 10-30 alkyl acrylates crosslinked with an allyl ether of pentaerythritol with one or more monomers from the group of acrylic acid, methacrylic acid and their simple esters, preferably formed with C 1-4 -alkanols (INCI Acrylates / C 10-30 Alkyl Acrylate Crosspolymer). In addition to the thickening effect, these compounds can have other effects in detergents, such as protection against graying.

[0164] In a preferred embodiment, the polyacrylic and polymethacrylic compounds suitable as thickeners have a weight-average molecular weight of >100,000 g / mol, preferably <500,000 g / mol.

[0165] Preferred thickeners are polysaccharides and heteropolysaccharides, especially polysaccharide gums, e.g., gum arabic, agar, alginates, carrageenans and their salts, guar, guaran, tragacanth, gellan, ramsan, dextran, or xanthan gum and their derivatives, e.g., propoxylated guar, and mixtures thereof. Other polysaccharide thickeners, such as starches or cellulose derivatives, can be used alternatively, but preferably in addition, to a polysaccharide gum, e.g., starches of various origins and starch derivatives, e.g., hydroxyethyl starch, starch phosphate esters, or starch acetates, or carboxymethylcellulose or its sodium salt, methyl, ethyl, hydroxyethyl, hydroxypropyl, hydroxypropylmethyl, or hydroxyethylmethyl cellulose, or cellulose acetate.

[0166] Polysaccharides and heteropolysaccharides suitable as thickeners preferably have a weight-average molecular weight of >1,500 g / mol, more preferably >5,000 g / mol, even more preferably >50,000 g / mol. In general, their weight-average molecular weight is <250,000 g / mol. A particularly preferred polymer is the microbial anionic heteropolysaccharide xanthan gum, which is produced by Xanthomonas campestris and some other species under aerobic conditions with a molecular weight of 2 to 15x10 6 g / mol is produced.

[0167] In various embodiments, the washing or cleaning agent according to the invention can contain, in addition to the at least one peptide as dye transfer inhibitor, further dye transfer inhibitors, preferably DTI (dye transfer inhibiting) polymers, although this embodiment is not preferred.

[0168] Suitable DTI polymers include, for example, homo- or copolymers based on vinylic, nitrogen-containing, preferably heterocyclic monomers, e.g., N-vinylpyrrolidone, N-vinylimidazole, N-vinylcaprolactam, and 4-vinylpyridine. These compounds are typically not biodegradable.

[0169] Examples of commercially available DTIs are known from US 20120225025 A1 from BASF.

[0170] Further examples of DTI polymers include, but are not limited to, polyvinylpyrrolidone (e.g., Sokalan® HP 50 / BASF, PVP-K-Typen® / ISP), vinylpyrrolidone-vinylimidazole copolymers (e.g., Sokalan® HP 56 / BASF), poly(4-vinylpyridine-N-oxide) (e.g., Chromabond® S-403E / ISP), and poly(4-vinylpyridine-N-carboxymethyl-betaine) (e.g., Chromabond® S 400 / ISP).

[0171] In a preferred embodiment, the washing or cleaning agent according to the invention is in liquid, gel-like or powder-like form, preferably in liquid, aqueous form.

[0172] The washing or cleaning agent according to the invention is preferably a washing agent, a laundry aftertreatment agent or a laundry care agent, more preferably a washing agent.

[0173] In a preferred embodiment, the washing or cleaning agents according to the invention are liquid washing or cleaning agents, more preferably liquid, aqueous washing or cleaning agents, even more preferably single-phase, liquid, aqueous washing or cleaning agents.

[0174] Furthermore, an insoluble solid component can also be present as a separate solid phase in single-phase detergents or cleaning agents. When such detergents or cleaning agents according to the invention are shaken, an emulsion of the liquid phase temporarily forms, which disperses the solid phase within it.

[0175] Multiphase formulations are not preferred in the context of this invention, but are not excluded.

[0176] In the context of this invention, “aqueous” means that water is the main solvent in the washing or cleaning agent according to the invention.

[0177] However, the detergent or cleaning agent may contain water-soluble organic solvents, such as alcohols, in addition to water. The term "liquid" preferably refers to a composition that flows at room temperature (approx. 20°C) and ambient pressure (approx. 1013 mbar at sea level). This term can also include gel-like and pasty compositions.

[0178] The viscosity of the liquid washing or cleaning agents at 20°C is preferably 5 to 100,000 mPa s, more preferably 10 to 5,000 mPa s, even more preferably 10 to 200 mPa s, measured with a Brookfield rotational viscometer of the LVT or LVDV-II+ type with a small sample adapter at a speed of 30 min -1The Brookfield spindle used as the measuring body should be selected so that the torque is within a favorable range and the measuring range is not exceeded. In this context, spindle 31 is preferred, and – if necessary for viscosities above approximately 240 mPa s – spindle 25 is preferred.

[0179] The pH value of the washing or cleaning agents according to the invention is preferably 2 to 12, preferably 6 to 10, more preferably 7 to 9, e.g. 8-8.5, both in concentrated form and in diluted application solution.

[0180] To adjust such a pH, acids can be added to the washing or cleaning agents according to the invention. Suitable acids are inorganic acids, e.g. mineral acids, e.g. hydrochloric acid, and organic acids, e.g. saturated or unsaturated C 1-6 mono-, di- and tricarboxylic acids and hydroxycarboxylic acids with one or more hydroxyl groups, such as citric acid, maleic acid, formic acid and acetic acid, aminosulfuric acid, C 6-22 fatty acids and anionic sulfonic acids, and mixtures thereof. Particularly preferred acids are citric acid, more preferably used in the form of its monohydrate citric acid x 1 H 2 O, and the anionic sulfonic acids, as well as combinations of citric acid with one or more anionic sulfonic acids, in particular with alkylarylsulfonic acids.The citric acid advantageously combines acid phase separation aid and builder properties, while the anionic sulfonic acids act simultaneously as acid and anionic surfactant.

[0181] In addition, one or more alkalis may be used, e.g. alkali metal, alkaline earth metal and ammonium hydroxides and carbonates and ammonia or amines, preferably sodium and potassium hydroxide and alkanolamines, with monoethanolamine being particularly preferred.

[0182] Since, for example, pH-altering substances are often introduced into the washing or cleaning liquor in large quantities during the washing or cleaning process, it is preferable to add appropriate buffer substances, e.g., acetates, hydrogen phosphates, hydrogen sulfates, soda, or alkali metal bicarbonates, to the washing or cleaning agent according to the invention at the application dilution to stabilize or buffer the pH. Particularly suitable buffer systems are potassium hydrogen phthalate / sodium hydroxide, potassium dihydrogen phosphate / sodium hydroxide, and the like.

[0183] However, solid detergents and cleaning agents are also encompassed in the context of this invention. A substance is referred to as "solid" if it exists in a solid state at room temperature (approx. 20°C) and ambient pressure (approx. 1,013 mbar at sea level). The detergents and cleaning agents according to the invention, especially if they are liquid or pasty, can be produced by simply mixing the ingredients in an automatic mixer.

[0184] In a preferred embodiment, the agents are preferably in liquid, gel, or paste form, preferably as a portion in a fully or partially water-soluble coating, more preferably in single-dose portions. The portioning facilitates dosing for the consumer.

[0185] The detergents can be packaged in foil pouches, for example. Pouches made of water-soluble foil eliminate the need for consumers to tear open the packaging. This allows for convenient dosing of a single portion, sufficient for one wash cycle, by placing the pouch directly into the washing machine or by dropping it into a specific amount of water, e.g., a bucket, bowl, or hand basin. The foil pouch surrounding the wash portion dissolves without leaving any residue when a certain temperature is reached.

[0186] In the prior art, there are numerous processes for producing water-soluble detergent portions, which in principle can also be used in the context of the present invention.

[0187] However, the washing or cleaning agent according to the invention can also be provided unportioned in liquid, gel, paste or solid form in storage bottles or packages.

[0188] The general production and composition of detergents and cleaning agents is generally known to those skilled in the art and can be carried out using any suitable process.

[0189] Exemplary washing and cleaning agent compositions as well as suitable ingredients are described, for example, in WO 01 / 44433 A1 or WO 2016 / 091650 A1.

[0190] An exemplary composition of a detergent according to the invention, in particular a liquid detergent, comprises, in addition to the peptides described herein, the following components:

[0191] water; and

[0192] Surfactants, in particular anionic and / or non-ionic surfactants; and / or thickeners; and / or stabilizers; and / or organic solvents; and / or enzymes; and / or fragrances; and / or complexing agents, e.g. phosphonates, in particular HEDP; and / or pH adjusters, in particular citric acid, NaOH and / or monoethanolamine (MEA); and / or optionally further dye transfer inhibitors, in particular DTI polymers; and / or soil-release polymers / soil-repellent polymers; and / or antifoams. A washing or cleaning agent according to the invention particularly preferably comprises, in addition to the peptides according to the invention, the following components: at least one surfactant, preferably in a concentration of 0.5 to 60 wt.%; and / or at least one stabilizer, preferably in a concentration of 0.001 to 20 wt.%, e.g. 0.1 to 5 wt.%; and / or at least one complexing agent, preferably in a concentration of 0.01 to 30 wt.%, in particular 0.1 to 10 wt.% or 0.2 to 5 wt.-%; and / or at least one organic solvent, preferably in a concentration of 0.1 to 30 wt.%, e.g. 0.5 to 25 wt.%; and / or at least one soil-release polymer / soil-repellent polymer, preferably in a concentration of 0.01 to 20 wt.%, e.g. 0.05 to 5 wt.%; and / or at least one enzyme, preferably in a concentration of 0.00001 to 5 wt.%; and / or at least one fragrance or perfume and / or at least one fragrance storage substance, preferably in a concentration of 0.0001 to 15 wt.%; and / or at least one pH adjuster, e.g. MEA, NaOH or citric acid, preferably in a concentration of 0.01 to 25 wt.%, e.g. 0.05 to 20 wt.%; and / or at least one antifoam, preferably in a concentration below 5 wt.%, e.g. below 2 wt.% or below 1 wt.%; and / or.

[0193] Water; the concentration information always refers to the total weight of the detergent or cleaning agent.

[0194] In a further aspect, the invention relates to a method for cleaning textiles, comprising at least one step in which a washing or cleaning agent according to the invention is applied. The method preferably relates to a machine washing process, in particular in a washing machine, or a hand washing process. The peptide described herein preferably acts as a dye transfer inhibitor and reduces or prevents dye transfer to textiles during the washing process.

[0195] In a further aspect, the invention relates to the use of a peptide as a dye transfer inhibitor, wherein the peptide comprises or consists of an amino acid sequence having 5 to 50 amino acid residues, preferably 10 to 30 amino acid residues, in particular 18 to 25 amino acid residues, e.g., 20 to 24 amino acid residues, wherein

[0196] (a) the amino acid sequence comprises at least 5 histidine residues (H), preferably at least 6 H, more preferably at least 10 H, in particular at least 12 H, at least five further amino acid residues, preferably at least 8 further amino acid residues, e.g. at least 10, 12, 14, 16 or 18 further amino acid residues, which are uncharged amino acid residues, preferably selected from A, G, P, F, I, W, S, V, L, Y and Q, in particular selected from A, G and P, and has a net charge at neutral pH of -2 to +6, preferably from 0 to +4, more preferably from 0 to +2, in particular from 0;and / or (b) the amino acid sequence has at least 80%, preferably at least 81%, more preferably at least 82%, even more preferably at least 83%, even more preferably at least 84%, even more preferably at least 85%, even more preferably at least 86%, or at least 87% or at least 88% or at least 89% or at least 90% or at least 91% or at least 92% or at least 93% or at least 94% or at least 95% or at least 96% or at least 97% or at least 98%, even more preferably at least 99% or at least 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-5, preferably with one of the amino acid sequences mentioned in SEQ ID NO: 1 or SEQ ID NO: 4.;

[0197] It is particularly preferred for use that the at least one peptide is a peptide as described herein, in particular the at least one peptide comprised in the washing or cleaning agent according to the invention.

[0198] In preferred embodiments, the use of the peptide reduces or prevents dye transfer to textiles, preferably during the washing or cleaning process, more preferably as a component of a washing or cleaning agent. In particular, the textiles are protected from discoloration by the presence of the peptide, which preferentially binds and / or adheres to dyes and acts in particular as a dye transfer inhibitor.

[0199] All facts, subject matter, and embodiments described for the washing or cleaning agent according to the invention also apply to the method according to the invention for cleaning textiles. Furthermore, all described features and embodiments relating to the at least one peptide in the washing or cleaning agent according to the invention also apply to the use of a peptide as a dye transfer inhibitor. Therefore, express reference is made here to the disclosure at the appropriate point, with the note that this disclosure also applies to the method according to the invention and to the use according to the invention, and vice versa.

[0200] The invention is illustrated below by examples, but is not limited to them.

[0201] Examples

[0202] Example 1

[0203] Table 1 : Histidine-rich peptides tested as dye transfer inhibitors:

[0204] Example 2: Detergent

[0205] Table 2: Example detergent composition.

[0206] Dosage: 3.5 g / L; pH 8.2-8.4 Example 3: Color inhibition test

[0207] The washing test is carried out according to the Hohenstein method.

[0208] A wash liquor was prepared from a dye transfer inhibitor-free liquid detergent A (3.5 g / l). This wash liquor was added to the dyes (Table 3) and the white textile pieces (6 cm x 16 cm) made of cotton (wfk, (Wfk 11 A)) and polyamide (EMPA). The wash process was carried out at 60°C for 30 minutes. For comparison, otherwise identical wash liquors containing, in addition to detergent A, one of the synthetically produced peptides as described above (Peptide 1:B, Peptide 2:C, Peptide 3:D, Peptide 4:E, Peptide 5:F) were tested under the same conditions. The bleeding of the white accompanying textiles was assessed according to DIN EN ISO 105-A04 on a scale of 1 (strong staining) to 5 (no staining). The results are presented in the table below.

[0209] Table 3: Results for dye transfer inhibition.

[0210] It can be seen that, compared to the detergent without the peptides essential to the invention, the white textiles were less stained when washed with the peptide. In particular, peptide 1 and peptide 4 demonstrate DTI performance for both cotton and polyamide.

Claims

Patent claims 1 . Washing or cleaning agent comprising at least one peptide comprising or consisting of an amino acid sequence with 5 to 50 amino acids, preferably 10 to 30 amino acids, in particular 18 to 25 amino acids, wherein (a) the amino acid sequence comprises at least 5 histidine residues (H), preferably at least 6 H, more preferably at least 10 H, in particular at least 12 H, at least five further amino acid residues, preferably at least 8 further amino acid residues, which are uncharged amino acid residues, preferably selected from A, G, P, F, I, W, S, V, L, Y and Q, in particular selected from A, G and P, and has a net charge at neutral pH of -2 to +6, preferably from 0 to +4, more preferably from 0 to +2, in particular from 0; and / or (b) the amino acid sequence has at least 80%, preferably at least 85%, more preferably at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-5, preferably with one of the amino acid sequences mentioned in SEQ ID NO: 1 or SEQ ID NO:

4.

2. The washing or cleaning agent according to claim 1, wherein the amino acid sequence of the at least one peptide comprises at least one arginine residue (R), preferably within the last 8 C-terminal amino acids, more preferably within the last 4 C-terminal amino acids; and / or at least one lysine residue (K), preferably within the last 8 C-terminal amino acids, more preferably within the last 4 C-terminal amino acids, in particular within the last 2 C-terminal amino acids; and / or does not comprise any negatively charged amino acid residues, preferably no E or D, within the first 8 N-terminal amino acid residues and / or the last 8 C-terminal amino acid residues, preferably within the first 4 N-terminal amino acid residues and / or the last 4 C-terminal amino acid residues; and / or has a neutral net charge at the N-terminus, comprising the first 3-5 amino acid residues;and / or has a neutral or positive net charge at the C-terminus, comprising the last 3-5 amino acid residues; 3. The washing or cleaning agent according to claim 1 or 2, wherein the amino acid sequence of the at least one peptide within the first 8 N-terminal amino acid residues does not comprise any charged amino acid residues; and / or comprises at least one of the sequence motifs AHHH, AAHA or AHHHAAHA, optionally multiple times, preferably the sequence motif (AHHHAAHA)3; and / or comprises the sequence motif GHHPH, preferably (GHHPH)2, (GHHPH)3, or (GHHPH)4.

4. The washing or cleaning agent according to any one of claims 1 to 3, wherein the amino acid sequence of the at least one peptide may contain at least one aromatic amino acid, preferably selected from W, Y or F.

5. The washing or cleaning agent according to any one of claims 1 to 4, wherein the at least one peptide consists of at least 60% amino acid residues with a high alpha-helix-forming potential, wherein these amino acid residues are preferably selected from E, A, L, M, Q, K, R, F, I, H and W, more preferably from E, A, L, Q, K, R, F, I, H and W, in particular from A, F, I, and H.

6. The washing or cleaning agent according to any one of claims 1 to 5, wherein the at least one peptide comprises or consists of an amino acid sequence of one of the amino acid sequences mentioned in SEQ ID NOs: 1-5, preferably an amino acid sequence of one of the amino acid sequences mentioned in SEQ ID NO: 1 or SEQ ID NO:

4.

7. The washing or cleaning agent according to any one of claims 1 to 6, wherein the at least one peptide is a peptide or polypeptide (multimer) comprising two or more of the peptides according to any one of claims 1 to 6.

8. The washing or cleaning agent according to claim 7, wherein the two or more peptides are 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, preferably selected from the group consisting of G, P, I, A and S or combinations thereof, in particular GPI or GAS.

9. The washing or cleaning agent according to any one of claims 1 to 8, wherein the at least one peptide is suitable for adhesion and / or binding to dyes, preferably is a dye transfer inhibitor.

10. The washing or cleaning agent according to any one of claims 1 to 9, wherein the washing or cleaning agent is a detergent.

11. The washing or cleaning agent according to any one of claims 1 to 10, wherein the washing or cleaning agent is used at a pH of 2-12, preferably 6 to 10, in particular 7 to 9.

12. A process for cleaning textiles comprising at least one step in which a washing or cleaning agent according to one of claims 1 to 11 is used.

13. Use of a peptide as a dye transfer inhibitor, wherein the peptide comprises or consists of an amino acid sequence having 5 to 50 amino acid residues, preferably 10 to 30 amino acid residues, in particular 18 to 25 amino acid residues, wherein (a) the amino acid sequence comprises at least 5 histidine residues (H), preferably at least 6 H, more preferably at least 10 H, in particular at least 12 H, at least five further amino acid residues, preferably at least 8 further amino acid residues, which are uncharged amino acid residues, preferably selected from A, G, P, F, I, W, S, V, L, Y and Q, in particular selected from A, G and P, and has a net charge at neutral pH of -2 to +6, preferably from 0 to +4, more preferably from 0 to +2, in particular from 0; and / or (b) the amino acid sequence has at least 80%, preferably at least 85%, more preferably at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-5, preferably with one of the amino acid sequences mentioned in SEQ ID NO: 1 or SEQ ID NO:

4.

14. The use according to claim 13, wherein the peptide is at least one peptide according to any one of claims 2 to 9.

15. The use according to claim 13 or 14, wherein the use of the peptide reduces or prevents the color transfer to textiles, preferably during the washing process, in particular protects the textiles from discoloration.

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