IMPROVED CARE PROPERTIES OF POLYESTER TEXTILES II

Description

[0001] The present invention lies in the field of enzyme technology, in particular the anti-pilling effect of enzymes, such as those used, for example, in washing or cleaning agents. The invention relates to an agent, in particular a washing or cleaning agent, which contains a cutinase as defined herein. Furthermore, the present invention relates to a method for cleaning textiles and the use of the agent according to the invention for removing soiling. Furthermore, the invention is directed to the use of a cutinase for reducing pilling and graying in an agent, preferably a washing or cleaning agent.

[0002] With repeated washing, textiles of all kinds will eventually pill. Pilling is the formation of small balls or fuzz in fabrics. These small balls of fuzz occur particularly in short-fiber fabrics. Long-fiber and twisted fibers, on the other hand, pill less. Generally, these balls are caused by loose fibers in the fabric or fibers that have detached from the weave. Synthetic fibers, due to their smooth surface, are more prone to pilling than natural fibers because synthetic fibers can be released from the fabric more quickly than rough natural fibers. In wool fabrics, these fibers "felt" primarily due to mechanical friction, forming balls on the surface.

[0003] The main effect of pilling is a visual impairment. The formation of pills on the surface quickly makes fabrics look used and older than they actually are. Additionally, colored textiles appear less vibrant. However, the functionality of the fabric is hardly or not at all impaired. Pilling occurs particularly in areas subject to high mechanical stress, usually the shoulder and waistband areas. Due to the continuous thinning of the fabric, these stressed areas are particularly at risk of developing holes or even tearing. This unwanted pilling results in affected textiles being rejected and thrown away by consumers faster than would be necessary based on the functionality of the textile.

[0004] Furthermore, textiles tend to turn gray during washing. This is because both dirt and detached pigments from colored clothing are released during the washing process. Despite attempts to keep these pigments in the wash solution using various detergent ingredients, it is often impossible to prevent the dirt / pigments from settling on the clothing and remaining there. This is the so-called graying effect. This is particularly pronounced with some synthetic fibers such as polyamide, but also polyester.

[0005] A technical solution to reduce the pilling effect is currently only available for cotton textiles. Cellulase is used in cleaning agents to reduce the pilling effect (DE 69632910 T3). This means that cellulase is used in the detergent to have an anti-pilling or anti-gray effect and thus ensure that clothing looks like new for longer. However, cellulase only works on cotton textiles. For other textiles, such as polyester textiles, there is no comparable option for reducing pilling. It is therefore desirable and there is a demand for solutions that reduce pilling in textiles, especially textiles that contain synthetic fibers such as polyester, in order to keep clothing looking new for as long as possible, i.e. the colors should remain vibrant, the shape should be retained and the surfaces should remain smooth and undamaged.

[0006] Surprisingly, the inventors of the present invention have found that a cutinase identified in leaf compost using a metagenomic approach (Sulaiman et al., "Isolation of a Novel Cutinase Homolog with Polyethylene Terephthalate-Degrading Activity from Leaf-Branch Compost by Using a Metagenomic Approach", Appl. Environ. Microbiol. March 2012, Vol. 78, No. 5: 1556-1562) is active under washing process conditions and exhibits various care properties for PET textiles. This is surprising in that previously known cutinases and PET esterases are more active at higher temperatures (>= 60°C) and are also only able to degrade PET very slowly. However, the cutinase used here shows rapid PET degradation at 50°C. It was found that the enzyme prevents or even reduces pilling on new polyester textiles.This effect is supported in combination with a cellulase on polyester / cotton blend textiles. Furthermore, it can reduce pills that have already formed, i.e., it can create a so-called "renew" effect. Furthermore, the cutinase prevents the graying of white laundry and the fading / graying of colored laundry. Furthermore, the cutinase demonstrates direct cleaning performance on stains on PET textiles. Furthermore, it was found that all of these positive washing properties are achieved without significant damage to the fiber. Because the textiles look newer for longer, they are worn longer and are replaced less quickly. This leads to a reduction in the CO2 footprint, as less polyester is used.

[0007] WO2015135757 discloses detergents containing PET esterases <65% according to SEQ ID NO:1, which are suitable for reducing pilling in polyester-containing textiles. Therefore, the present invention is directed to a detergent or cleaning agent characterized in that it contains a cutinase that has at least 65% sequence identity with the amino acid sequence given in SEQ ID NO:1 over its entire length.

[0008] In a further aspect, the present invention is directed to methods for cleaning textiles, characterized in that an agent according to the invention is used in at least one process step. The textiles are preferably polyester-containing textiles or are made of polyester.

[0009] In another aspect, the present invention is further directed to the use of a washing or cleaning agent as described herein, particularly preferably a liquid washing agent, for removing soiling.

[0010] Furthermore, a further aspect of the invention includes the use of the cutinase described herein for reducing pilling effects and / or increasing the anti-grey effect of a washing or cleaning agent, particularly preferably a liquid washing agent, wherein the agent contains the cutinase.

[0011] Cutinase (EC 3.1.1.74), also known as cutin hydrolase, is an enzyme belonging to the α / β-hydrolases family and hydrolyzes cutin. Cutinase is produced by some plant-pathogenic fungi and bacteria, among others (cutinase enables fungi to degrade the ester bond of cutin in the plant cuticle and thus penetrate the plant).

[0012] In various preferred embodiments of the invention, the cutinase is a cutinase which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO:1 over its entire length. In further preferred embodiments, the cutinase contained in the agent according to the invention comprises the amino acid sequence given in SEQ ID NO:1 or consists essentially thereof or consists thereof. In various embodiments of the invention, the invention also encompasses cutinases derived from the amino acid sequence according to SEQ ID NO:1, for example by means of mutagenesis. In various further embodiments, the invention also encompasses cutinases obtainable by expressing the nucleotide sequence according to SEQ ID NO:3.In one aspect of the invention, the invention also comprises the nucleotide sequence according to SEQ ID NO:3 and nucleotide sequences which are at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 98.8%, 99.0%, 99.2%, 99.4% or 99.6% identical to the nucleotide sequence given in SEQ ID NO:3 over its entire length. provided that the native sequence encoding LC cutinase is excluded.

[0013] In various embodiments of the invention, the cutinase comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO:1 over its entire length to at least 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 98.8%, 99.0%, 99.2%, 99.4% or 99.6% is identical or consists of such a sequence.

[0014] In various further embodiments, the agent is characterized in that (a) the cutinase is obtainable from a cutinase as defined above as the starting molecule by single or multiple conservative amino acid substitution; and / or (b) the cutinase is obtainable from a cutinase as defined above as the starting molecule by fragmentation, deletion, insertion or substitution mutagenesis and comprises an amino acid sequence which corresponds to the starting molecule over a length of at least 180, 190, 200, 210, 220, 230, 240, 245, 250, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263 or 264 contiguous amino acids.

[0015] The agents according to the invention preferably contain the cutinase in an amount of 0.00001 - 1 wt.%, more preferably in an amount of 0.0001 - 0.5 wt.%, particularly preferably in an amount of 0.001 - 0.1 wt.%, in each case based on the active protein.

[0016] The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the state-of-the-art and commonly used BLAST algorithm (see, for example, Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ (1990) "Basic local alignment search tool." J. Mol. Biol. 215:403-410, and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs"; Nucleic Acids Res., 25, pp. 3389-3402) and is essentially performed by matching similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences. A tabular assignment of the relevant positions is called alignment. Another algorithm available in the state of the art is the FASTA algorithm.Sequence alignments, especially multiple sequence alignments, are created using computer programs. Commonly used programs include the Clustal series (see, for example, Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31, 3497-3500), T-Coffee (see, for example, 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 alignments can also be performed using the computer program Vector NTI ®< 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.

[0017] Such a comparison also allows a statement to be made about the similarity of the compared sequences to one another. This is usually expressed as percent identity, i.e. the proportion of identical nucleotides or amino acid residues at the same positions or corresponding positions in an alignment. The broader term homology in amino acid sequences includes conserved amino acid substitutions, i.e. amino acids with similar chemical activity, since these usually exert similar chemical activities within the protein. Therefore, the similarity of the compared sequences can also be expressed as percent homology or percent similarity. Identity and / or homology statements can be made for entire polypeptides or genes, or just for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by similarities in the sequences.Such regions often exhibit identical functions. They can be small and comprise only a few nucleotides or amino acids. Such small regions often perform essential functions for the overall activity of the protein. It may therefore be useful to refer sequence matches only to individual, possibly small regions. Unless otherwise stated, however, statements of identity or homology in this application refer to the entire length of the respective nucleic acid or amino acid sequence.

[0018] In various embodiments, the cutinase comprises an amino acid sequence that is at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 98.8%, 99.0%, 99.2%, 99.4% or 99.6% homologous to the amino acid sequence given in SEQ ID NO:1 over its entire length.

[0019] In a further embodiment of the invention, the cutinase is characterized in that its anti-pilling performance is not significantly reduced compared to that of a cutinase comprising an amino acid sequence corresponding to the amino acid sequences given in SEQ ID NO:1, i.e., it has at least 70%, 75%, 80%, 85%, 90%, or 95% of the reference anti-pilling performance. The anti-pilling performance can be determined in a washing system containing a detergent at a dosage of between 4.5 and 7.0 grams per liter of wash liquor and the cutinase, wherein the cutinases to be compared are used at the same concentration (based on active protein), and the anti-pilling performance is determined as described herein. For example, the washing process can be carried out for 60 minutes at a temperature of 60°C, and the water can have a water hardness of between 15.5 and 16.5°C (German hardness).The concentration of cutinase in the detergent intended for this washing system is from 0.00001 to 1 wt.%, preferably from 0.0001 to 0.5 wt.%, particularly preferably from 0.001 to 0.1 wt.%, based on active, purified protein.

[0020] A preferred liquid detergent for such a washing system is composed as follows (all values ​​in percent by weight): 4.4% alkylbenzenesulfonic acid, 5.6% anionic surfactants, 2.4% C12-C18 sodium salts of fatty acids, 4.4% nonionic surfactants, 0.2% phosphonates, 1.4% citric acid, 0.95% NaOH, 0.01% antifoam, 2% glycerin, 0.08% preservatives, 1% ethanol, 1.6% enzyme mix (protease, amylase, cellulase, mannase), and the remainder: demineralized water. The preferred dosage of the liquid detergent is between 4.5 and 6.0 grams per liter of wash liquor, for example, 4.7, 4.9, or 5.9 grams per liter of wash liquor. Washing is preferably carried out in a pH range between pH 8 and pH 10.5, preferably between pH 8 and pH 9.

[0021] In the context of the invention, the anti-pilling performance is determined at 60°C using a liquid detergent as stated above, wherein the washing process is preferably carried out for 60 minutes.

[0022] Anti-pilling performance can be monitored through visual inspection. In this case, a panel of testers assigns a score on a scale of 1-5 to the laundry being tested. A score of 1 represents very heavily pilled laundry, while a score of 5 represents non-pilled laundry.

[0023] By using the same activity of each cutinase, it is ensured that even if there is a discrepancy in the ratio of active substance to total protein (the specific activity values), the respective enzymatic properties, such as anti-pilling performance, are compared. In general, a low specific activity can be compensated for by adding a larger amount of protein.

[0024] Proteins can be combined into groups of immunologically related proteins through reaction with an antiserum or a specific antibody. The members of such a group are characterized by having the same antigenic determinant recognized by an antibody. They are therefore structurally so similar to one another that they are recognized by an antiserum or specific antibodies. Another subject of the invention therefore relates to cutinases which are characterized by having at least one, and increasingly preferably two, three, or four, identical antigenic determinants with a cutinase used in an agent according to the invention. Due to their immunological similarities, such cutinases are structurally so similar to the cutinases used in the agents according to the invention that a similar function can be assumed.

[0025] Other cutinases used in the agents according to the invention may have further amino acid modifications, in particular amino acid substitutions, insertions, or deletions, compared to the cutinase described in SEQ ID NO:1. Such cutinases are further developed, for example, by targeted genetic modification, i.e., by mutagenesis methods, and optimized for specific applications or with regard to special properties (for example, with regard to their catalytic activity, stability, etc.). Furthermore, nucleic acids encoding the cutinases used can be incorporated into recombinant approaches and thus used to generate completely novel cutinases or other polypeptides.

[0026] The aim is to introduce targeted mutations such as substitutions, insertions, or deletions into the known molecules in order, for example, to improve the cleaning performance of enzymes according to the invention. For this purpose, in particular, the surface charges and / or the isoelectric point of the molecules and thus their interactions with the substrate can be altered. For example, the net charge of the enzymes can be altered in order to influence substrate binding, particularly for use in detergents and cleaning agents. Alternatively or additionally, one or more corresponding mutations can further increase the stability of cutinase and thereby improve its cleaning performance. Advantageous properties of individual mutations, e.g., individual substitutions, can complement each other.A cutinase that has already been optimized with regard to certain properties, for example with regard to its activity and / or its anti-pilling performance, can therefore be further developed within the scope of the invention.

[0027] The invention therefore further relates to an agent containing a cutinase, which is characterized in that it is obtainable from a cutinase as described above as the starting molecule by single or multiple conservative amino acid substitution. 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 lead to a change in the polarity or charge at the position of the exchanged amino acid, e.g., the exchange of a non-polar amino acid residue for another non-polar 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. The homology of the cutinases modified in this way to the cutinase with SEQ ID NO:1 is preferably as defined above.

[0028] Alternatively or additionally, the cutinase is characterized in that it is obtainable from a cutinase contained in an agent according to the invention as a starting molecule by fragmentation, deletion, insertion or substitution mutagenesis and comprises an amino acid sequence which corresponds to the starting molecule over a length of at least 180, 190, 200, 210, 220, 230, 240, 245, 250, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263 or 264 contiguous amino acids.

[0029] For example, it is possible to delete individual amino acids at the termini or in the loops of the enzyme without losing or reducing the hydrolytic activity. Furthermore, such fragmentation, deletion, insertion or substitution mutagenesis can also reduce the allergenicity of the enzymes in question and thus improve their overall usability. Advantageously, the enzymes retain their hydrolytic activity even after mutagenesis, i.e. their hydrolytic activity corresponds at least to that of the starting enzyme, i.e. in a preferred embodiment the hydrolytic activity is at least 80, preferably at least 90% of the activity of the starting enzyme. Other substitutions can also have advantageous effects. Both individual amino acids and several contiguous amino acids can be exchanged for other amino acids.

[0030] In various embodiments, the cutinase may have one or more further amino acids at the N- or C-terminal end in addition to the sequence given in SEQ ID NO:1. In certain embodiments, such N-terminal peptides may be the naturally occurring signal peptides for the cutinase or a single methionine residue. In such embodiments, the cutinase has, for example, the amino acid sequence given in SEQ ID NO:2. All embodiments disclosed above in the context of the mature cutinase according to SEQ ID NO:1 are also applicable to the cutinase with the sequence according to SEQ ID NO:2.

[0031] The invention relates to a washing or cleaning agent characterized by containing a cutinase as defined herein. Unless explicitly stated otherwise, all percentages given in connection with the compositions / agents described herein refer to wt. %, in each case based on the respective mixture / agent.

[0032] For the purposes of the present invention, fatty acids or fatty alcohols or their derivatives—unless otherwise stated—represent branched or unbranched carboxylic acids or alcohols or their derivatives, preferably with 6 to 22 carbon atoms. In particular, the oxo alcohols or their derivatives obtainable, for example, by the Roelen oxo synthesis can also be used accordingly.

[0033] Whenever alkaline earth metals are mentioned below as counterions for monovalent anions, this means that the alkaline earth metal is naturally present in only half the amount of the anion - sufficient to balance the charge.

[0034] This invention encompasses all conceivable types of detergents and cleaning agents, both concentrated and undiluted, for commercial use, in washing machines, or for hand washing. These include, for example, detergents for textiles, carpets, or natural fibers, for which the term "detergent" is used. The detergents and cleaning agents within the scope of the invention also include washing aids that are added to the detergent during manual or machine washing to achieve an additional effect.Furthermore, detergents and cleaning agents within the scope of the invention also include textile pre- and post-treatment agents, i.e., agents with which the laundry is brought into contact before the actual washing process, for example, to loosen stubborn dirt, as well as agents that impart further desirable properties to the laundry in a step following the actual textile washing process, such as a pleasant feel, crease resistance, or low static charge. Fabric softeners, among others, are included among the latter agents.

[0035] The washing or cleaning agents according to the invention, which can be in the form of powdered solids, in compacted particle form, as homogeneous solutions, gels, or suspensions, can contain, in addition to the cutinase described above, all known ingredients customary in such agents, with at least one further ingredient preferably being present in the agent. The agents according to the invention can contain, in particular, surfactants, builders, bleaching agents, in particular peroxygen compounds, or bleach activators. They can also contain water-miscible organic solvents, other enzymes, sequestering agents, electrolytes, pH regulators, and / or other auxiliaries such as optical brighteners, graying inhibitors, foam regulators, dyes, and fragrances, as well as combinations thereof.

[0036] In particular, a combination of the agent according to the invention with one or more other ingredients is advantageous, since in preferred embodiments of the invention, such an agent exhibits improved cleaning performance due to resulting synergisms. Such synergism can be achieved in particular by combining the agent according to the invention with a surfactant and / or a builder and / or a peroxygen compound and / or a bleach activator.

[0037] Advantageous ingredients of the compositions according to the invention are disclosed in the international patent application WO2009 / 121725, beginning on page 5, penultimate paragraph, and ending on page 13 after the second paragraph. This disclosure is expressly incorporated by reference, and the disclosure content therein is incorporated into the present patent application.

[0038] These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art from a study of the following detailed description and claims. It is understood that any feature of one aspect of the invention may be employed in any other aspect of the invention. Furthermore, it is understood that the examples contained herein are intended to describe and illustrate the invention, but not to limit it, and in particular, the invention is not limited to these examples. All percentages, unless otherwise indicated, are by weight based on the total weight of the composition. Numerical ranges given in the format "from x to y" include the stated values. Where multiple preferred numerical ranges are given in this format, it is understood that any ranges resulting from the combination of the various endpoints are also encompassed.

[0039] In addition to cutinase, the agents according to the invention preferably also contain at least one compound from the class of surfactants, in particular selected from anionic and non-ionic, but also cationic, zwitterionic or amphoteric surfactants.

[0040] Suitable surfactants are, for example, anionic surfactants of the formula (I) R-SO 3 -< Y +< (I).

[0041] In this formula (I), R represents a linear or branched unsubstituted alkylaryl radical. Y represents a monovalent cation or the nth part of an n-valent cation, preferred being alkali metal ions, including Na+< or K+<, with Na+< being most preferred. Further cations Y+< can be selected from NH4+<, ½Zn2+<, ½Mg2+<, ½Ca2+<, ½Mn2+<, and mixtures thereof.

[0042] "Alkylaryl," as used herein, refers to organic radicals consisting of an alkyl radical and an aromatic radical. Typical examples of such radicals include, but are not limited to, alkylbenzene radicals such as benzyl, butylbenzene radicals, nonylbenzene radicals, decylbenzene radicals, undecylbenzene radicals, dodecylbenzene radicals, tridecylbenzene radicals, and the like.

[0043] In various embodiments, such surfactants are selected from linear or branched alkylbenzenesulfonates of the formula A-1

[0044] in which R' and R" together contain 9 to 19, preferably 11 to 15 and in particular 11 to 13 C atoms. A particularly preferred representative can be described by the formula A-1a:

[0045] In various embodiments, the compound of formula (I) is preferably the sodium salt of a linear alkylbenzenesulfonate.

[0046] In agents according to the invention, the at least one compound from the class of anionic surfactants of formula (I) is contained in the washing or cleaning agent in an amount of 0.001 to 30 wt.%, preferably 0.001 - 10 wt.%, further preferably 2 - 6 wt.%, even more preferably 3 - 5 wt.%, in each case based on the total weight of the cleaning agent.

[0047] In various embodiments, the agents according to the invention preferably contain at least one anionic surfactant of the formula R 1< -O-(AO) n -SO 3 -< X +< (II).

[0048] In this formula (II), R 1< represents a linear or branched, substituted or unsubstituted alkyl, aryl, or alkylaryl radical, preferably a linear, unsubstituted alkyl radical, particularly preferably a fatty alcohol radical. Preferred radicals R 1< are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals, and mixtures thereof, with preference given to those having an even number of carbon atoms. Particularly preferred radicals R 1< are derived from C 12 -C 18 fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C 10 -C 20 oxo alcohols.

[0049] AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably for an ethylene oxide group. The index n stands for an integer from 1 to 50, preferably from 1 to 20 and in particular from 2 to 10. Very particularly preferably, n stands for the numbers 2, 3, 4, 5, 6, 7 or 8. X stands for a monovalent cation or the nth part of an n-valent cation, preferred are the alkali metal ions and among these Na +< or K +< , with Na +< being extremely preferred. Further cations X+ can be selected from NH 4 +< , ½ Zn 2+< , ½ Mg 2+< , ½ Ca 2+< , ½ Mn 2+< , and mixtures thereof.

[0050] In summary, agents in various embodiments thus contain at least one anionic surfactant selected from fatty alcohol ether sulfates of the formula A-2 with k = 11 to 19, n = 2, 3, 4, 5, 6, 7 or 8. Particularly preferred representatives are Na-C 12-14 fatty alcohol ether sulfates with 2 EO (k = 11-13, n = 2 in formula A-2).

[0051] In various embodiments, the cleaning agent contains the at least one anionic surfactant of formula (II) in an amount of 2-10 wt.%, preferably 3-8 wt.%, based on the total weight of the cleaning agent.

[0052] Other anionic surfactants that can be used are the alkyl sulfates of the formula R 2< -O-SO 3 -< X +< (III).

[0053] In this formula (III), R 2< represents a linear or branched, substituted or unsubstituted alkyl radical, preferably a linear, unsubstituted alkyl radical, particularly preferably a fatty alcohol radical. Preferred R 2< radicals are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals, and mixtures thereof, with preference being given to those having an even number of carbon atoms. Particularly preferred R 2< radicals are derived from C 12 -C 18 fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C 10 -C 20 oxo alcohols. Y represents a monovalent cation or the nth part of an n-valent cation, preferred are the alkali metal ions and among them Na +< or K +< , with Na +< being most preferred.Further cations Y +< can be selected from NH 4 +< , ½ Zn 2+< ,½ Mg 2+< ,½ Ca 2+< ,½ Mn 2+< , and mixtures thereof.

[0054] In various embodiments, these surfactants are selected from fatty alcohol sulfates of the formula A-3 with k = 11 to 19. Particularly preferred representatives are Na-C 12-14 fatty alcohol sulfates (k = 11-13 in formula A-3).

[0055] In various embodiments, the agent may contain at least one other surfactant in addition to the anionic surfactants described above, in particular those of formulas (I)-(III), or alternatively thereto. Alternative or additional surfactants include, in particular, other anionic surfactants, nonionic surfactants, and mixtures thereof, as well as cationic, zwitterionic, and amphoteric surfactants.

[0056] In various embodiments, the agents comprise at least one non-ionic surfactant, in particular at least one fatty alcohol alkoxylate.

[0057] Suitable non-ionic surfactants are those of the formula R 3< -O-(AO) m -H (IV), in which R 3< represents a linear or branched, substituted or unsubstituted alkyl radical, AO represents an ethylene oxide (EO) or propylene oxide (PO) group, m represents integers from 1 to 50.

[0058] In the above-mentioned formula (IV), R 3< represents a linear or branched, substituted or unsubstituted alkyl radical, preferably a linear, unsubstituted alkyl radical, particularly preferably a fatty alcohol radical. Preferred radicals R 2< are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals, and mixtures thereof, with preference being given to those having an even number of carbon atoms. Particularly preferred radicals R 3< are derived from C 12 -C 18 fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C 10 -C 20 oxo alcohols.

[0059] AO represents an ethylene oxide (EO) or propylene oxide (PO) group, preferably an ethylene oxide group. The index m represents an integer from 1 to 50, preferably from 1 to 20, and in particular from 2 to 10. Most preferably, m represents the numbers 2, 3, 4, 5, 6, 7, or 8.

[0060] In summary, the fatty alcohol alkoxylates to be used preferably are compounds of the formula with k = 11 to 19, m = 2, 3, 4, 5, 6, 7 or 8. Particularly preferred representatives are C 12-18 fatty alcohols with 7 EO (k = 11-17, m = 7 in formula (V)).

[0061] Further nonionic surfactants which may be contained in the described agents within the meaning of the present invention include, but are not limited to, alkyl glycosides, alkoxylated fatty acid alkyl esters, amine oxides, fatty acid alkanolamides, hydroxy mixed ethers, sorbitan fatty acid esters, polyhydroxy fatty acid amides and alkoxylated alcohols.

[0062] Suitable amphoteric surfactants are, for example, betaines of the formula (R iii< )(R iv< )(R v< )N +< CH 2 COO -< , in which R iii< is an alkyl radical optionally interrupted by heteroatoms or heteroatom groups having 8 to 25, preferably 10 to 21 carbon atoms and R iv< and R v< are identical or different alkyl radicals having 1 to 3 carbon atoms, in particular C 10 -C 18 alkyldimethylcarboxymethylbetaine and C 11 -C 17 alkylamidopropyldimethylcarboxymethylbetaine.

[0063] Suitable cationic surfactants include the quaternary ammonium compounds of the formula (R vi< )(R vii< )(R viii< )(R ix< )N +< X -< , in which R vi< to R ix< are four identical or different, in particular two long-chain and two short-chain, alkyl radicals and X -< is an anion, in particular a halide ion, for example didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride and mixtures thereof. Other suitable cationic surfactants are the quaternary surface-active compounds, in particular those containing a sulfonium, phosphonium, iodonium or arsonium group, which are also known as antimicrobial agents. By using quaternary surface-active compounds with antimicrobial action, the agent can be given an antimicrobial effect or its antimicrobial effect, which may already be present due to other ingredients, can be improved.

[0064] In various embodiments, the total amount of surfactants based on the weight of the agent is 2 to 30 wt.%, preferably 5 to 25 wt.%, more preferably 10 to 20 wt.%, most preferably 14 to 18 wt.%, wherein the (linear) alkylbenzenesulfonates are present at most in an amount of 0.001 to 30 wt.%, preferably 0.001 - 10 wt.%, further preferably 2 - 6 wt.%, more preferably 3 - 5 wt.%, based on the weight of the agent.

[0065] Detergents or cleaning agents according to the invention can contain other enzymes in addition to cutinase. These can be hydrolytic enzymes or other enzymes in a concentration appropriate for the effectiveness of the agent. One embodiment of the invention thus represents agents that comprise one or more enzymes. Preferred enzymes that can exhibit catalytic activity in the agent according to the invention are all enzymes that can exhibit catalytic activity in the agent according to the invention, in particular a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, xyloglucanase, β-glucosidase, pectinase, carrageenase, perhydrolase, oxidase, oxidoreductase or a lipase, as well as mixtures thereof. Enzymes are advantageously present in the agent in an amount of 1 x 10 -8 to 5 wt.%, based on active protein. Increasingly preferably, each enzyme is present in an amount of 1 x 10 -7 < -3 wt%, from 0.00001-1 wt%, from 0.00005-0.5 wt%, from 0.0001 to 0.1 wt%.-% and particularly preferably from 0.0001 to 0.05 wt.%, based on active protein, in agents according to the invention. The enzymes particularly preferably exhibit synergistic cleaning performance against certain soils or stains, i.e., the enzymes contained in the agent composition support each other in their cleaning performance. Synergistic effects can occur not only between different enzymes, but also between one or more enzymes and other ingredients of the agent according to the invention.

[0066] The amylase(s) is / are preferably an α-amylase. The hemicellulase is preferably a β-glucanase, a pectinase, a pullulanase, and / or a mannanase. The cellulase is preferably a cellulase mixture or a single-component cellulase, preferably or predominantly an endoglucanase and / or a cellobiohydrolase. The oxidoreductase is preferably an oxidase, in particular a choline oxidase, or a perhydrolase.

[0067] The proteases used are primarily alkaline serine proteases. They act as nonspecific endopeptidases, meaning they hydrolyze any acid amide bonds found within peptides or proteins, thereby breaking down protein-containing soils on the items being cleaned. Their pH optimum is usually in the significantly alkaline range.

[0068] The protein concentration can be determined using known methods, for example, the BCA method (bicinchoninic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method. The active protein concentration is determined by titrating the active sites using a suitable irreversible inhibitor (for proteases, for example, phenylmethylsulfonyl fluoride (PMSF)) and determining the residual activity (cf. M. Bender et al., J. Am. Chem. Soc. 88, 24 (1966), pp. 5890-5913).

[0069] In the cleaning agents described herein, the enzymes to be used can also be formulated together with accompanying substances, such as those from fermentation. In liquid formulations, the enzymes are preferably used as liquid enzyme formulation(s).

[0070] The enzymes are generally not provided in the form of pure protein, but rather in the form of stabilized, storable, and transportable preparations. These prefabricated preparations include, for example, solid preparations obtained by granulation, extrusion, or lyophilization or, particularly in the case of liquid or gel-like products, solutions of the enzymes, preferably as concentrated as possible, with little water content, and / or containing stabilizers or other additives.

[0071] Alternatively, the enzymes can be encapsulated for both solid and liquid dosage forms, for example by spray-drying or extrusion of the enzyme solution together with a preferably natural polymer, or in the form of capsules, for example those in which the enzymes are enclosed as if in a solidified gel, or in those of the core-shell type, in which an enzyme-containing core is coated with a water-, air-, and / or chemical-impermeable protective layer. Additional active ingredients, such as stabilizers, emulsifiers, pigments, bleaching agents, or dyes, can be applied in superimposed layers. Such capsules are applied using methods known per se, for example by shake or roll granulation or in fluid-bed processes. Such granules, for example by applying polymeric film formers, are advantageously low in dust and, due to the coating, are stable during storage.

[0072] Furthermore, it is possible to package two or more enzymes together so that a single granulate has multiple enzyme activities.

[0073] In various embodiments, the agent according to the invention can comprise one or more enzyme stabilizers. Therefore, the agent according to the invention can further contain an enzyme stabilizer, for example, selected from the group consisting of sodium formate, sodium sulfate, lower aliphatic alcohols, and boric acid, as well as their esters and salts. Of course, two or more of these compounds can also be used in combination. The salts of the aforementioned compounds can also be used in the form of hydrates, such as sodium sulfate decahydrate.

[0074] The term "lower aliphatic alcohols," as used herein, includes monoalcohols, diols, and higher-hydric alcohols with up to 6 carbon atoms. Polyols belonging to the group of lower aliphatic alcohols include, in particular, polyols, for example, glycerol, (mono)ethylene glycol, (mono)propylene glycol, or sorbitol, without the invention being limited to these.

[0075] In addition to the at least one enzyme stabilizer selected from the above group, a composition according to the invention may also contain at least one further stabilizer. Such stabilizers are known in the art.

[0076] Reversible protease inhibitors protect the enzymes contained in a detergent or cleaning agent from proteolytic degradation by reversibly inhibiting the enzymatic activity of the proteases contained in the agent. Benzamidine hydrochloride, boronic acids, or their salts or esters are frequently used as reversible protease inhibitors, especially derivatives with aromatic groups, such as ortho-, meta-, or para-substituted phenylboronic acids, especially 4-formylphenylboronic acid, or the salts or esters of the aforementioned compounds. Peptide aldehydes, i.e., oligopeptides with a reduced C-terminus, especially those consisting of 2 to 50 monomers, are also used for this purpose. Peptide reversible protease inhibitors include, among others, ovomucoid and leupeptin.

[0077] Other enzyme stabilizers include amino alcohols such as mono-, di-, triethanolamine, and propanolamine and their mixtures; aliphatic carboxylic acids up to C12, such as succinic acid; other dicarboxylic acids; or salts of these acids. End-capped fatty acid amide alkoxylates are also suitable for this purpose. Some organic acids used as builders can also stabilize an enzyme. Calcium and / or magnesium salts, such as calcium acetate, are also used for this purpose.

[0078] Polyamide oligomers or polymeric compounds such as lignin, water-soluble vinyl copolymers or cellulose ethers, acrylic polymers, and / or polyamides stabilize the enzyme preparation against, among other things, physical influences or pH fluctuations. Polyamine N-oxide-containing polymers act simultaneously as enzyme stabilizers and dye transfer inhibitors. Other polymeric stabilizers are linear C 8 -C 18 polyoxyalkylenes. Alkyl polyglycosides can also stabilize the enzymatic components of the inventive agent and, preferably, can additionally enhance their performance. Crosslinked N-containing compounds preferably fulfill a dual function as soil-release agents and enzyme stabilizers. Hydrophobic, nonionic polymers particularly stabilize any cellulase present.

[0079] Reducing agents and antioxidants increase the stability of enzymes against oxidative degradation; for example, sulfur-containing reducing agents, such as sodium sulfite and reducing sugars, are common for this purpose.

[0080] In one embodiment, the washing or cleaning agents according to the present invention are liquid and contain water as the main solvent, i.e., they are aqueous agents. The water content of the aqueous agent according to the invention is typically 15 to 70 wt.%, preferably 20 to 60 wt.%. In various embodiments, the water content is more than 5 wt.%, preferably more than 15 wt.%, and particularly preferably more than 50 wt.%, in each case based on the total amount of agent.

[0081] Non-aqueous solvents can also be added to the product. Suitable non-aqueous solvents include mono- or polyhydric alcohols, alkanolamines, or glycol ethers, provided they are miscible with water within the specified concentration range. The solvents are preferably selected from ethanol, n-propanol, i-propanol, butanols, glycol, propanediol, butanediol, methylpropanediol, glycerin, diglycol, propyl diglycol, butyl diglycol, hexylene glycol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, diethylene glycol ethyl ether, propylene glycol methyl ether, propylene glycol ethyl ether, propylene glycol propyl ether, dipropylene glycol monomethyl ether, dipropylene glycol monoethyl ether, methoxytriglycol, ethoxytriglycol, butoxytriglycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether, di-n-octyl ether and mixtures of these solvents.

[0082] The one or more non-aqueous solvents are usually present in an amount of 0.1 to 10 wt.%, preferably 1 to 8 wt.%, based on the total composition.

[0083] In addition to the components mentioned above, the agents according to the invention can contain other ingredients that further improve the application and / or aesthetic properties of the cleaning agent. These include, for example, additives to improve flow and drying properties, to adjust viscosity, and / or for stabilization, as well as other auxiliaries and additives commonly found in cleaning agents, such as UV stabilizers, perfume, pearlescent agents, dyes, corrosion inhibitors, preservatives, bittering agents, organic salts, disinfectants, structuring polymers, defoamers, encapsulated ingredients (e.g., encapsulated perfume), pH adjusters, and skin-feel-improving or conditioning additives.

[0084] A washing or cleaning agent according to the invention preferably contains at least one water-soluble and / or water-insoluble, organic and / or inorganic builder.

[0085] Generally applicable builders include, in particular, aminocarboxylic acids and their salts, zeolites, silicates, carbonates, organic (co)builders, and—where there are no environmental objections to their use—phosphates. However, these agents are preferably phosphate-free.

[0086] The water-soluble organic builder substances include polycarboxylic acids, in particular citric acid and sugar acids, monomeric and polymeric aminopolycarboxylic acids, in particular methylglycinediacetic acid, nitrilotriacetic acid and ethylenediaminetetraacetic acid as well as polyaspartic acid, polyphosphonic acids, in particular aminotris(methylenephosphonic acid), ethylenediaminetetrakis(methylenephosphonic acid) and 1-hydroxyethane-1,1-diphosphonic acid, polymeric hydroxy compounds such as dextrin as well as polymeric (poly)carboxylic acids, polymeric acrylic acids, methacrylic acids, maleic acids and copolymers thereof, which may also contain small amounts of polymerizable substances without carboxylic acid functionality. 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.The organic builders can be used, particularly for the production of liquid agents, in the form of aqueous solutions, preferably in the form of 30 to 50 percent by weight aqueous solutions. All of the acids mentioned are generally used in the form of their water-soluble salts, especially their alkali metal salts.

[0087] Organic builders can, if desired, be present in amounts of up to 40 wt.%, in particular up to 25 wt.%, and preferably from 1 wt.% to 8 wt.%. Amounts close to the stated upper limit are preferably used in paste-like or liquid, especially water-based, compositions according to the invention. Laundry aftertreatment compositions according to the invention, such as fabric softeners, can optionally also be free of organic builders.

[0088] Suitable water-soluble inorganic builder materials include, in particular, alkali metal silicates and, if there are no concerns about their use, also polyphosphates, preferably sodium triphosphate. Suitable water-insoluble, water-dispersible inorganic builder materials include, in particular, crystalline or amorphous alkali metal aluminosilicates, if desired, in amounts of up to 50 wt.%, preferably not more than 40 wt.%, and in liquid compositions, in particular from 1 wt.% to 5 wt.%. Among these, crystalline sodium aluminosilicates of detergent quality, in particular zeolite A, P, and optionally X, are preferred. Amounts close to the stated upper limit are preferably used in solid, particulate compositions. Suitable aluminosilicates, in particular, have no particles with a grain size exceeding 30 µm and preferably consist of at least 80 wt.% particles with a size below 10 µm.

[0089] 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 according to the invention preferably have a molar ratio of alkali oxide to SiO 2 of less than 0.95, in particular from 1:1.1 to 1:12, and can be amorphous or crystalline. Preferred alkali silicates are sodium silicates, in particular amorphous sodium silicates, with a molar Na 2 O:SiO 2 ratio of 1:2 to 1:2.8. As crystalline silicates, which can be present alone or in a mixture with amorphous silicates, crystalline layered silicates of the general formula Na 2 Si x O 2x+1 · y H 2 O are preferably used, 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 beta- and delta-sodium disilicates (Na 2 Si 2 O 5 y H 2 O) are preferred. Virtually anhydrous crystalline alkali silicates produced from amorphous alkali silicates of the above general formula, in which x is a number from 1.9 to 2.1, can also be used in agents according to the invention. In a further preferred embodiment of agents according to the invention, a crystalline sodium layered 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 of agents according to the invention.If alkali aluminosilicate, especially zeolite, is also present as an additional builder substance, the weight ratio of aluminosilicate to silicate, based on anhydrous active substances, is preferably 1:10 to 10:1. In agents containing both amorphous and crystalline alkali silicates, the weight ratio of amorphous alkali silicate to crystalline alkali silicate is preferably 1:2 to 2:1 and in particular 1:1 to 2:1.

[0090] Builder substances are, if desired, present in the compositions according to the invention preferably in amounts of up to 60% by weight, in particular from 5% to 40% by weight. Water-soluble builders are particularly preferred in liquid formulations. Laundry aftertreatment compositions according to the invention, such as fabric softeners, are preferably free of inorganic builders.

[0091] Polymeric thickeners within the meaning of the present invention are the polycarboxylates which act as polyelectrolytes to thicken, preferably homo- and copolymers of acrylic acid, in particular acrylic acid copolymers such as acrylic acid-methacrylic acid copolymers, and the polysaccharides, in particular heteropolysaccharides, as well as other customary thickening polymers.

[0092] Suitable polysaccharides or heteropolysaccharides are polysaccharide gums, for example gum arabic, agar, alginates, carrageenans and their salts, guar, guaran, tragacanth, gellan gum, ramsan gum, dextran or xanthan gum and their derivatives, e.g., propoxylated guar gum, as well as their mixtures. Other polysaccharide thickeners, such as starches or cellulose derivatives, can be used alternatively, but preferably in addition, to a polysaccharide gum. These include 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 hydroxyethylmethylcellulose, or cellulose acetate.

[0093] Acrylic acid polymers suitable as polymeric thickeners are, for example, high molecular weight homopolymers of acrylic acid (INCI Carbomer) crosslinked with a polyalkenyl polyether, in particular an allyl ether of sucrose, pentaerythritol or propylene, which are also referred to as carboxyvinyl polymers.

[0094] Particularly suitable polymeric thickeners are the following acrylic acid copolymers: (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 25035-69-2) or of butyl acrylate and methyl methacrylate (CAS 25852-37-3); (ii) cross-linked high molecular weight acrylic acid copolymers, which include, for example, copolymers of C 10-30 alkyl acrylates cross-linked with an allyl ether of sucrose or 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 / C10-30 Alkyl Acrylate Crosspolymer).

[0095] The content of polymeric thickener is usually not more than 8 wt.%, preferably between 0.1 and 7 wt.%, particularly preferably between 0.5 and 6 wt.%, in particular between 1 and 5 wt.% and most preferably between 1.5 and 4 wt.%, for example between 2 and 2.5 wt.%, based on the total weight of the agent.

[0096] To stabilize the agent according to the invention, particularly when the surfactant content is high, one or more dicarboxylic acids and / or their salts can be added, in particular a composition of sodium salts of adipic, succinic, and glutaric acid, as is available, for example, under the trade name Sokalan®< DSC. They are advantageously used in amounts of 0.1 to 8 wt.%, preferably 0.5 to 7 wt.%, in particular 1.3 to 6 wt.%, and particularly preferably 2 to 4 wt.%, based on the total weight of the cleaning agent. However, if their use can be dispensed with, the agent according to the invention is preferably free of dicarboxylic acids (salts).

[0097] The detergents according to the invention can be compared with reference detergents to determine the increased anti-pilling performance of the detergents according to the invention. Such a detergent system can be composed as follows (all data in percent by weight): Reference detergent: 4.4% alkylbenzenesulfonic acid, 5.6% other anionic surfactants, 2.4% C12-C18 Na salts of fatty acids (soaps), 4.4% nonionic surfactants, 0.2% phosphonates, 1.4% citric acid, 0.95% NaOH, 0.01% defoamers, 2.0% glycerin, 0.08% preservatives, 1% ethanol, 1.6% enzyme mix (protease, amylase, cellulase, mannase), the remainder demineralized water.Inventive agent: 4.4% alkylbenzenesulfonic acid, 5.6% other anionic surfactants, 2.4% C12-C18 sodium salts of fatty acids (soaps), 4.4% nonionic surfactants, 0.2% phosphonates, 1.4% citric acid, 0.95% NaOH, 0.01% defoamer, 2.0% glycerin, 0.08% preservatives, 1% ethanol, 1.6% enzyme mix (protease, amylase, cellulase, mannase), 0.009% cutinase, balance demineralized water. The preferred dosage of the liquid detergent is between 4.5 and 6.0 grams per liter of wash liquor, for example, 4.7, 4.9, or 5.9 grams per liter of wash liquor. Washing is preferably carried out in a pH range between pH 8 and pH 10.5, preferably between pH 8 and pH 9.

[0098] The aforementioned embodiments of the present invention encompass all solid, powdered, liquid, gel-like, or pasty dosage forms of washing or cleaning agents according to the invention, which may optionally also consist of multiple phases and may be present in compressed or uncompressed form. The agent may be in the form of a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l. Solid dosage forms of the agent also include extrudates, granules, tablets, or pouches. Alternatively, the agent may also be liquid, gel-like, or pasty, for example in the form of a non-aqueous liquid detergent or a non-aqueous paste, or in the form of an aqueous liquid detergent or a water-containing paste. Furthermore, the agent may be in the form of a one-component system. Such agents consist of one phase.Alternatively, a product can also consist of multiple phases, for example, single-phase, double-phase, or multi-phase. Such a product is therefore divided into several components (multi-component system).

[0099] The invention further relates to a process for cleaning textiles, characterized in that an agent according to the invention is used in at least one process step. The textiles preferably contain or consist of polyester. In various embodiments, the process described above is characterized in that the agent according to the invention is used at a temperature of 0-100°C, preferably 0-80°C, more preferably 30-70°C, and most preferably 40-60°C.

[0100] This includes both manual and mechanical processes, with mechanical processes being preferred. Processes for cleaning textiles are generally characterized by the fact that various cleaning-active substances are applied to the items to be cleaned in several process steps and are washed off after the contact time, or by the items to be cleaned being treated in some other way with a detergent or a solution or dilution of this detergent. All conceivable washing or cleaning processes can be enhanced in at least one of the process steps by the use of a washing or cleaning agent according to the invention and then represent embodiments of the present invention. All facts, objects, and embodiments described for agents according to the invention are also applicable to this subject matter of the invention.Therefore, explicit reference is made here to the disclosure at the corresponding point, with the note that this disclosure also applies to the above-mentioned processes according to the invention. Since enzymes naturally already possess catalytic activity and also exhibit this activity in media that otherwise have no cleaning power, such as in mere buffer, a single and / or the only step of such a process can consist of bringing a cutinase, as the sole cleaning-active component, into contact with the soil, preferably in a buffer solution or in water. This represents a further embodiment of this subject matter of the invention.

[0101] Alternative embodiments of this subject matter of the invention also include processes for treating textile raw materials or for textile care, in which an agent according to the invention is active in at least one process step. Among these, processes for textile raw materials, fibers, or textiles with synthetic components are preferred, and especially for those with polyester.

[0102] Furthermore, the invention also covers the use of the washing or cleaning agent described herein as described above for the (improved) removal of soiling, for example from textiles, in particular polyester textiles.

[0103] Finally, the invention also relates to the use of a cutinase for reducing pilling effects of a detergent, particularly preferably a liquid detergent, wherein the detergent contains the cutinase. The cutinase is a cutinase as defined herein. In various embodiments of the use, the cutinase is present in the detergent in an amount of 0.00001-1 wt.%, preferably in an amount of 0.0001-0.5 wt.%, particularly preferably in an amount of 0.001-0.1 wt.%. In further various embodiments, the cutinase, which reduces the pilling effect, is applied to textiles, in particular textiles made of polyester or comprising polyester. Examples Example 1: Cloning and expression

[0104] The gene was codon-optimized for expression in E. colisynthetically produced (SEQ ID NO:3), and then cloned into the NdeI and XhoI sites of the vector PET-21b from Novagen, creating a C-terminal fusion with a 6x histidine tag. The plasmid, confirmed by sequencing, is transformed into electrocompetent cells using standard transformation protocols. E. coli BL21(DE3)CodonPlus RIPL (Agilent Technologies).

[0105] Cultivation takes place in LB medium at 37°C, with induction with 0.1 mM IPTG at an OD of 0.6 and then a lowered expression temperature to 16°C.

[0106] The cells are harvested by centrifugation and resuspended in lysis buffer (50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 20 mM imidazole). Cell disruption is performed using ultrasonication, followed by centrifugation (15,000 xg, 20 min, 4°C). The supernatant contains the His-tagged LC cutinase.

[0107] Purification using NiNTA (Qiagen, Hilden, DE) is carried out according to the manufacturer Qiagen’s protocol. Example 2: Investigation using QCM-D

[0108] The degradation kinetics of the polyesterases described here were analyzed using QCM-D (quartz crystal microbalance with dissipation monitoring). The polyester model substrates were prepared starting from commercially available AT-cut QCM-D crystals (Biolin Scientific) with a typical resonance frequency of 5 MHz and a gold-terminated electrode. These crystals were modified with a polyester thin film using a spin-coating process.

[0109] At the beginning of the measurement, the modified crystals were equilibrated in a measuring cell flushed with Tris-HCl buffer (volume flow 60 µl·min -1< ) ​​and kept at a constant temperature (T=50°C) until a stable baseline was reached (Fig. t=0h to t=0.5h).

[0110] Subsequently, the Tris-HCl buffer was exchanged for a buffer solution containing cutinase (SEQ ID NO:1) (c= 0.15 mg / mL) ( Fig. 1 : t=0.5h) and the mass loss occurring after the dead time as a result of film degradation was recorded ( Fig. 1 : t=0.55h to t=1.1h) From the Figure 1 The results shown clearly show the rapid loss of mass caused by the cutinase. Example 3: PET film degradation test

[0111] Substrate: PET film: 0.25 mm thick, amorphous, transparent from GoodFellow Cambridge Limited, ES301445 Conducted in 2 mL tubes

[0112] PET film (0.5 cm x 2.5 cm) was washed with (1) 1.7 mL of 0.1% SDS (w / v), 50 °C, 30 min, 400 rpm; (2) 1.5 mL of absolute ethanol, 50 °C, 5 min, 700 rpm; (3) 1.7 mL of double-distilled water, 50 °C, 5 min, 700 rpm, and dried to constant value for 48 h at 50 °C and weighed. This was followed by incubation (48–72 h at 55 °C) with a fixed amount of cutinase according to SEQ ID NO:1 (5, 25, 50 µg) in a total volume of 1.7 mL in a detergent matrix (see below, dosage 4.7 g / L).

[0113] After removal of the incubation supernatant, the PET film was washed with (1) 1.7 mL of 0.1% SDS (w / v) + 0.5% Triton X-100 (w / v), 50 °C, 30 min, 400 rpm; (2) 1.5 mL of absolute ethanol, 50 °C, 5 min, 700 rpm; (3) 1.7 mL of double-distilled water, 50 °C, 5 min, 700 rpm; and dried to constant temperature for 48 h at 50 °C and weighed. The weight loss was determined. Result:

[0114] The weight loss is given compared to the untreated film after 44 h incubation at 50°C: Detergent with 25 µg cutinase: - 0.57 mg weight loss Detergent with 50 µg cutinase: - 1.67 mg weight loss

[0115] A concentration-dependent PET degradation caused by the cutinase in the detergent matrix is ​​clearly visible. Example 4: Washing test Detergent matrix used

[0116] This is a commercially available detergent matrix (without optical brighteners, perfumes and dyes) that was used for the washing test: Chemical name % wt. active substance in raw material % wt. active substance in the formulation demineralized water 100 rest Alkylbenzenesulfonic acid 96 4,4 Anionic surfactants 70 5,6 C12-C18 fatty acid sodium salt 30 2,4 Non-ionic surfactants 100 4,4 Phosphonates 40 0,2 citric acid 100 1,4 NaOH 50 0,95 Defoamers tq 0,01 Glycerin 100 2 Preservatives 100 0,08 Ethanol 93 1 Without optical brighteners, dyes, perfumes and enzymes Dosage 4.7 g / L Washing test to determine the anti-pilling performance of enzymes

[0117] Twenty identical tests are conducted consecutively in a standard washing machine. Various polyester and blended fabrics are used as the textiles to be evaluated, one of which is new and the other pre-pilled. After the 20 tests, the pill reduction of the pre-pilled fabrics and the pill formation of the new fabrics are visually assessed.

[0118] The pre-pilled fabrics are produced by 20 repeated washing cycles at 40°C in standard washing machines.

[0119] After each wash cycle, the entire laundry is dried in the dryer.

[0120] Washing conditions: Water with 16°dH, 2.5 kg of clean laundry, 60°C normal program, 80 g detergent as described above per machine Dosage of the cutinase to be tested: 4 mg active enzyme per washing machine Sample 1: only detergent as described above (comparison reference) Sample 2: detergent + 4 mg cutinase (SEQ ID NO:1) (according to the invention) Result after 20 washes on 100% polyester textile: Visual sampling of the pills, scale 1-5, very heavily pilled =1, not pilled = 5 Sample 1: 2.0 Sample 2: 2.7 A change of 0.5 units is to be regarded as significant.

[0121] The cutinase according to the invention significantly improves the pill appearance.

Claims

1. A detergent or cleaning agent, characterised in that it contains a cutinase that has at least 65% sequence identity with the amino acid sequence specified in SEQ ID NO:1 over its entire length.

2. The agent according to claim 1, characterised in that the cutinase comprises an amino acid sequence that is identical to the amino acid sequence specified in SEQ ID NO:1 over its entire length at least to an extent of 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 98.8%, 99.0%, 99.2%, 99.4% or 99.6%.

3. The agent according to claim 1 or 2, characterised in that (1) the cutinase is obtainable from a cutinase according to claim 1 or 2 as starting molecule by a single or multiple conservative amino acid substitution; and / or (2) the cutinase is obtainable from a cutinase according to claim 1 or 2 as starting molecule by fragmentation, deletion, insertion or substitution mutagenesis and comprises an amino acid sequence that matches the starting molecule over a length of at least 180, 190, 200, 210, 220, 230, 240, 245, 250, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263 or 264 interconnected amino acids.

4. The agent according to any one of claims 1 to 3, wherein the cutinase is contained in an amount of 0.00001 - 1 % by weight, preferably in an amount of 0.0001 - 0.5 % by weight, particularly preferably in an amount of 0.001 - 0.1 % by weight.

5. The agent according to any one of claims 1 to 4, characterised in that a. it contains at least one additional ingredient selected from the group consisting of surfactants, builders (structural materials), bleaching agents, bleach activators, water-miscible organic solvents, further enzymes, sequestering agents, electrolytes, pH regulators, optical brighteners, greying inhibitors, foam regulators, dyes and aromatic substances, and combinations hereof; and / or b. is present in solid or liquid, preferably liquid form.

6. A method for cleaning textiles, characterised in that an agent according to any one of claims 1 to 5 is used in at least one method step.

7. The method according to claim 6, characterised in that the textiles contain polyester or consist of polyester.

8. Use of an agent according to any one of claims 1 to 5 for removing soiling, in particular of polyester-containing textiles.

9. Use of a cutinase which has at least 65% sequence identity with the amino acid sequence specified in SEQ ID NO:1 over its entire length for reducing pilling effects and / or increasing the anti-greying effect of an agent, preferably a detergent, particularly preferably a liquid detergent, wherein the agent contains the cutinase.

10. The use according to claim 9, wherein a. the cutinase is as defined in claim 2 or 3; and / or b. the cutinase is contained in the agent in an amount as defined in claim 4; and / or c. the agent is as defined in claim 5.