EP3673035A1

EP3673035A1 - Improved care properties of polyester textiles ii

Info

Publication number: EP3673035A1
Application number: EP18758569.0A
Authority: EP
Inventors: Nina Mussmann; Susanne Wieland; Daniela HERBST; Margret VAN LIER; Ines Baranski; Alexander Schulz; Boray TORUN; Christina SCHÖNDELING
Original assignee: Henkel AG and Co KGaA
Current assignee: Henkel AG and Co KGaA
Priority date: 2017-08-24
Filing date: 2018-08-16
Publication date: 2020-07-01
Also published as: DE102017214870A1; WO2019038164A1

Abstract

The invention relates to the field of enzyme technology, in particular the anti-pilling action of enzymes, as used, for example, in washing and cleaning agents. The invention relates to an agent, in particular a washing or cleaning agent, which contains a cutinase, as defined herein. The invention further relates to a method for cleaning textiles and to the use of the agent according to the invention for removing soiling. The invention further relates to the use of a cutinase, as described herein, for reducing pilling effects in an agent, preferably a washing or cleaning agent.

Description

Improved care properties of polyester textiles II

The present invention is in the field of enzyme technology, in particular the anti-pilling action of enzymes, as used, for example, in detergents or cleaners. The invention relates to an agent, in particular washing or cleaning agent, which contains a cutinase as defined herein. Furthermore, the present invention relates to a method for the cleaning of textiles and the use of the agent according to the invention for the removal of stains. Furthermore, the invention is directed to the use of a cutinase for reducing pilling effects and graying in an agent, preferably a detergent or cleaning agent.

For multiple wash textiles of any kind with time a pilling. Pilling refers to the formation of nodules or lint in fabrics. These small lint arise especially with short-fiber substances. Long-fiber and twisted fibers, on the other hand, produce less pilling. Generally, these nodules are caused by loose fibers in the fabric or those that have come loose from the fabric. Due to their smooth surface, synthetic fibers tend to pilling rather than natural fibers because synthetic fibers can be released from the fabric faster than rough natural fibers. In woolen fabrics, these fibers "matt" mainly by mechanical friction and form nodules on the surface.

The main effect of pilling is a visual impairment. Due to the formation of nodules on the surface, fabrics look quickly needed and older than they are. In addition, colored textiles seem less luminous. In contrast, the functionality of the substance is hardly or not at all affected. Pilling takes place especially on mechanically stressed areas, usually these are shoulder and waistband area. Due to the continuous thinning of the material, these stressed areas are in particular at risk of forming or even breaking holes. The unwanted pilling has the consequence that accordingly impaired textiles of the

Consumers are sorted out faster and thrown away than would be necessary on the basis of the functionality of the textile.

Furthermore, textiles tend to gray during washing. This is because in the washing process both dirt and detached pigments are released from colored clothing. Although it is attempted by various detergent ingredients in the

Nevertheless, it can often not be prevented that the dirt / pigments settle on the clothing and remain there. This is the so-called graying effect. This is particularly strong in some synthetic fibers such as polyamide, but also pronounced polyester. A technical solution to reduce the pilling effect is currently available only for cotton textiles. In this case, cellulases are used in the detergent to reduce the pilling effect (DE 69632910 T3). This means that cellulases are used in the detergent to give it anti-pilling or anti-gray effects, making it look longer than new. Cellulases, however, work exclusively on cotton textiles. For other textiles, such as

Polyester textiles, there is no comparable way to reduce pilling. Therefore, it is desirable and there is a demand for solutions that reduce the pilling of textiles, especially textiles containing synthetic fibers such as polyester, to make clothes look as new as possible for as long as possible. The colors should remain strong, the shape should be preserved and the surfaces should remain smooth and undamaged.

Surprisingly, the inventors of the present invention found that a

Cutinase identified in a foliage compost by a metagenomic approach (Sulaiman et al., "Isolation of a Novel Cutinase Homologue with Polyethylene Terephthalate Activity from Leaf-Branch Compost by Using a Metagenomic Approach", Appl. Environ.Microbiol 2012, Vol. 78, No. 5: 1556-1562), is active under washing process conditions and has various care properties for PET textiles. This is surprising to the extent that previously known cutinases and PET esterases tend to be higher

Temperatures (> = 60 ° C) are active, and also are only able to dissolve PET very slowly. However, the cutinase used in this case shows a rapid PET degradation at 50 ° C. On the one hand, it has been found that the enzyme prevents pilling on new polyester textiles or supports this effect in combination with a cellulase on polyester / cotton-blend textiles. On the other hand already formed pills can be reduced, i. It can cause a so-called "Renew effect." Furthermore, the Cutinase prevents the

Graying of white laundry and fading / graying of colored laundry. In addition, the Cutinase shows a direct cleaning performance on stains on PET textiles. It has also been found that all of these positive washing properties are achieved without significantly damaging the fiber. By making the textiles look new longer, they are worn longer and replaced less quickly. This leads to a reduction of the CO2 footprint as less polyester is used.

Therefore, in a first aspect, the present invention is directed to an agent, in particular a detergent or cleaning agent, characterized in that it contains a cutinase having at least 65% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length.

In a further aspect, the present invention is directed to processes for the purification of textiles, characterized in that in at least one process step inventive agent is applied. The textiles are preferably polyester-containing textiles or consist of polyester.

In yet another aspect, the present invention is further directed to the use of an agent as described herein, preferably a detergent or cleaning agent, more preferably a liquid detergent, to remove soils.

In addition, another aspect of the invention involves the use of the cutinase described herein to reduce pilling effects and / or increase the anti-gray activity of an agent, preferably a detergent or cleaning agent, more preferably a liquid detergent, the agent containing the Contains cutinase.

A cutinase (EC 3.1.1.74) or cutin hydrolase is an enzyme that belongs to the a / ß-hydrolases and hydrolyzes cutin. Among other things, cutinase is formed by some phytopathogenic fungi and bacteria (through the cutinase the fungi are able to break down the ester bond of the cutin in the cuticle of the plants and thus penetrate into the plants).

In various preferred embodiments of the invention, the cutinase is a cutinase having 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 present in the agent according to the invention comprises that indicated in SEQ ID NO: 1

Amino acid sequence or consists essentially thereof or consists thereof. In various embodiments of the invention, the invention also includes cutinases derived from the

Amino acid sequence according to SEQ ID NO: 1, for example by means of mutagenesis derived. In various other embodiments, the invention also includes cutinases obtainable by expression of the nucleotide sequence of SEQ ID NO: 3. In one aspect of the invention, the invention also encompasses the nucleotide sequence according to SEQ ID NO: 3 and

Nucleotide sequences corresponding to the nucleotide sequence given in SEQ ID NO: 3 over at least 80% of its total length, 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% are identical, with the proviso in that the native sequence coding for LC cutinase is excluded.

In various embodiments of the invention, the cutinase comprises a

Amino acid sequence corresponding to the amino acid sequence given in SEQ ID NO: 1 over its total 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.

In various other embodiments, the means is characterized in that

(a) the cutinase is obtainable from a cutinase as defined above as a parent molecule by single or multiple conservative amino acid substitution; and or

(b) the cutinase is obtainable from a cutinase as defined above as the parent molecule by fragmentation, deletion, insertion or substitution mutagenesis and a

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 matches the parent molecule.

The agents according to the invention preferably contain the cutinase in an amount of 0.00001-1% by weight, more preferably in an amount of 0.0001-0.5% by weight, particularly preferably in an amount of 0.001-0.1 Wt .-%, each based on the active protein.

The identity of nucleic acid or amino acid sequences is determined by a sequence comparison. This sequence comparison is based on the BLAST algorithm established and commonly used in the prior art (see, for example, Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ. (1990) "Basic local alignment search 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 in principle accomplished by similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences of each other be assigned. A tabular assignment of the respective positions is referred to as alignment. Another algorithm available in the prior art is the FASTA algorithm. Sequence comparisons (alignments), in particular multiple sequence comparisons, are created with computer programs. For example, the Clustal series (see, for example, Chenna et al., 2003, Multiple Sequence Alignment with the Clinical 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. Also possible are alignment comparisons (alignments) with the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the default parameters whose AlignX module for sequence comparisons is based on ClustalW. Such a comparison also allows a statement about the similarity of the compared sequences to each other. It is usually given in percent identity, that is, the proportion of identical nucleotides or amino acid residues at the same or in an alignment corresponding positions. The broader concept of homology involves conserved amino acid substitutions in the consideration of amino acid sequences, that is, amino acids with similar chemical activity, since these usually have similar chemical properties within the protein

Exercise activities. Therefore, the similarity of the compared sequences may also be given in percent homology or percent similarity. Identity and / or homology information can be made about whole polypeptides or genes or only over individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by matches in the sequences. Such areas often have identical functions. They can be small and comprise only a few nucleotides or amino acids. Often, such small regions exert essential functions for the overall activity of the protein. It may therefore be useful to relate sequence matches only to individual, possibly small areas. Unless otherwise indicated, identity or homology information in the present application, however, refers to the total length of the particular nucleic acid or amino acid sequence indicated.

In various embodiments, the cutinase comprises an amino acid sequence corresponding to the amino acid sequence given in SEQ ID NO: 1 over its total length of 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 % is homologous.

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 which comprises an amino acid sequence corresponding to the amino acid sequences given in SEQ ID NO: 1, ie at least 70%. , 75%, 80%, 85%, 90%, 95% of the reference anti-pilling benefits. The anti-pilling performance can be determined in a washing system containing a detergent in a dosage between 4.5 and 7.0 grams per liter of wash liquor and the cutinase, wherein the cutinases to be compared are used in concentration (based on active protein) and the anti-pilling performance is determined as described herein. For example, the washing process for 60 minutes at a temperature of 60 ° C and the water have a water hardness between 15.5 and 16.5 ° (German hardness). The concentration of cutinase in the washing agent intended for this washing system is from 0.00001 to 1% by weight, preferably from 0.0001 to 0.5% by weight, particularly preferably from 0.001 to 0.1% by weight, based on active, purified protein. A preferred liquid detergent for such a washing system is composed as follows (all figures in weight percent): 4.4% alkyl benzene sulfonic acid, 5.6% anionic surfactants, 2.4% C12-C18 Na salts of fatty acids, 4.4 % non-ionic surfactants, 0.2% phosphonates, 1, 4% citric acid, 0.95% NaOH, 0.01% antifoam, 2% glycerol, 0.08% preservatives, 1% ethanol, 1, 6% enzyme mix ( Protease, amylase, cellulase, mannase), remainder demineralised water. Preferably, the 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. Preference is given to washing in a pH range between pH 8 and pH 10.5, preferably between pH 8 and pH 9.

In the context of the invention, the determination of the anti-pilling performance at 60 ° C under

Use of a liquid detergent as indicated above, wherein the washing process is preferably carried out for 60 minutes.

The anti-pilling performance can be tracked by visual matching. In this case, a panel of inspectors assigns a scale of 1-5 to the laundry to be examined. The value = 1 stands for very heavily pilled laundry, while the value = 5 is not assigned to pilled laundry.

The activity-equivalent use of the respective cutinase ensures that, even if the ratio of active substance to total protein (the values of the specific activity) diverge, the respective enzymatic properties, for example the anti-pilling performance, are compared. In general, a low specific activity can be compensated by adding a larger amount of protein.

Proteins can be grouped into groups of immunologically related proteins by reaction with an antiserum or 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 each other that they are recognized by an antiserum or specific antibodies. Another one

The subject of the invention is therefore formed by cutinases which are characterized by having at least one, and more preferably two, three or four, identical antigenic determinants with a cutinase used in an agent according to the invention. Due to their immunological similarity, such cutinases are structurally so similar to the cutinases used in the agents according to the invention that a similar function is to be assumed as well. Further cutinases used in the agents according to the invention can, in comparison to the cutinase described in SEQ ID NO: 1, further amino acid changes, in particular

Amino acid substitutions, insertions or deletions. Such cutinases are, for example, by targeted genetic modification, i. by mutagenesis, further developed and optimized for specific applications or specific properties (for example, in terms of catalytic activity, stability, etc.). Furthermore, nucleic acids encoding the cutinases used can be introduced into recombination approaches and thus used to generate completely novel cutinases or other polypeptides.

The goal is to introduce into the known molecules targeted mutations such as substitutions, insertions or deletions, for example, to improve the cleaning performance of enzymes of the invention. For this purpose, in particular the surface charges and / or the isoelectric point of the molecules and thereby their interactions with the substrate can be changed. Thus, for example, the net charge of the enzymes can be changed in order to influence the substrate binding, in particular for use in detergents and cleaners. Alternatively or additionally, the stability of the cutinase can be further increased by one or more corresponding mutations, thereby improving its cleaning performance.

Advantageous properties of individual mutations, e.g. individual substitutions can complement each other. A cutinase which 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.

Another object of the invention is therefore an agent containing a cutinase, which is characterized in that it is obtainable from a cutinase as described above as the starting molecule by one or more conservative amino acid substitution. The term

"conservative amino acid substitution" means the replacement of one

Amino acid residue against another amino acid residue, which exchange does not lead to a change in polarity or charge at the position of the exchanged amino acid, z. B. the replacement of a nonpolar amino acid residue against another nonpolar

Amino acid residue. Conservative amino acid substitutions within the scope of the invention include, for example: G = A = S, l = 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 modified cutinases to the cutinase of SEQ ID NO: 1 is preferably as defined above.

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

Fragmentation, deletion, insertion or substitution mutagenesis and a

Amino acid sequence 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 are contiguous amino acids consistent with the parent molecule.

Thus, for example, it is possible to delete individual amino acids at the termini or in the loops of the enzyme, without this losing or reducing the hydrolytic activity. Furthermore, such fragmentation, deletion, insertion or substitution mutagenesis can also reduce, for example, the allergenicity of the enzymes concerned and thus improve their overall applicability. Advantageously, the enzymes retain even after the

Mutagenesis their hydrolytic activity, i. their hydrolytic activity is at least equal to that of the starting enzyme, i. 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 show beneficial effects. Both single and multiple contiguous amino acids can be substituted for other amino acids.

In various embodiments, the cutinase may have one or more additional amino acids N- or C-terminal in addition to the sequence shown in SEQ ID NO: 1. In certain embodiments, such N-terminal peptides may be the naturally occurring signal peptides for the cutinase or even 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 of SEQ ID NO: 1 are also applicable to the cutinase having the sequence of SEQ ID NO: 2.

An object of the invention is an agent characterized by containing a cutinase as defined herein. The agent is preferably a washing or cleaning agent.

All percentages associated with those described herein

Compositions / agents are made, unless explicitly stated otherwise to wt .-%, each based on the respective mixture / the respective means.

In the context of the present invention are fatty acids or fatty alcohols or their derivatives - unless otherwise stated - representative of branched or unbranched carboxylic acids or alcohols or their derivatives having preferably 6 to 22 carbon atoms. In particular, the oxo alcohols or their derivatives, which are obtainable, for example, by the RoELEN's oxo synthesis, can also be used correspondingly. Whenever alkaline earth metals are referred to below as counterions for monovalent anions, this means that the alkaline earth metal is present only in half - as sufficient to charge balance - amount of substance as the anion.

This invention includes all conceivable types of detergents or cleaners, both concentrates and undiluted agents, for use on a commercial scale, in the washing machine or in hand washing. These include, for example

Detergents for textiles, carpets or natural fibers, for which the term laundry detergent is used. The washing and cleaning agents in the context of the invention also include washing aids, which in manual or machine textile washing to the actual

Detergent be added to achieve a further effect. Furthermore, laundry detergents and cleaners in the context of the invention also include textile pre-treatment and post-treatment agents, ie those agents with which the laundry item is brought into contact before the actual laundry, for example to dissolve stubborn soiling, and also agents which are in one of the actual Textile laundry downstream step to give the laundry further desirable properties such as comfortable grip, crease resistance or low static charge. Among the latter, i.a. calculated the fabric softener.

The washing or cleaning agents according to the invention, which may be in the form of powdered solids, in densified particle form, as homogeneous solutions, gels or suspensions, may contain, in addition to the above-described cutinase, all known ingredients customary in such agents, preferably at least one further ingredient in the Means is present. The agents according to the invention may in particular contain surfactants, builders, bleaches, in particular peroxygen compounds, or bleach activators. In addition, they may contain water-miscible organic solvents, further enzymes, sequestering agents, electrolytes, pH regulators and / or further auxiliaries, such as optical brighteners, graying inhibitors, foam regulators, as well as dyes and fragrances, and combinations thereof.

In particular, a combination of the agent according to the invention with one or more further ingredient (s) is advantageous, since such an agent in preferred inventive

Embodiments has improved cleaning performance by resulting synergisms. In particular, by combining the agent according to the invention with a surfactant and / or a builder (builder) and / or a peroxygen compound and / or a bleach activator, such a synergism can be achieved.

Advantageous ingredients of agents according to the invention are disclosed in International

Patent application WO2009 / 121725, starting there on page 5, penultimate paragraph, and ending on Page 13 after the second paragraph. This disclosure is incorporated herein by reference and the disclosure is incorporated herein by reference.

These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art from a study of the following detailed description and claims. Any feature of one aspect of the invention may be employed in any other aspect of the invention. Further, it is to be understood that the examples contained herein are intended to describe and illustrate the invention, but not to limit it, and in particular that the invention is not limited to these examples. All percentages are by weight unless otherwise specified, based on the total weight of the composition. Numeric ranges specified in the format "from x to y" include the above values.If multiple preferred numeric ranges are specified in this format, it is understood that all ranges resulting from the combination of the various endpoints, also be recorded.

In addition to the cutinase, the compositions according to the invention preferably also contain at least one compound from the class of surfactants, in particular selected from anionic and nonionic, but also cationic, zwitterionic or amphoteric surfactants.

Suitable surfactants are, for example, anionic surfactants of the formula (I)

In this formula (I), R represents a linear or branched unsubstituted alkylaryl group. Y stands for a monovalent cation or the n-th part of an n-valent cation, the alkali metal ions being preferred, and Na ⁺ or K ⁺ being preferred, Na ^{+ being} extremely preferred. Other cations Y ⁺ may be selected from NhV, Mn ²⁺ , and mixtures thereof.

"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.

In various embodiments, such surfactants are selected from linear or branched alkylbenzenesulfonates of the formula A-1 in which R ^' and R ^" together contain from 9 to 19, preferably from 1 to 15, and in particular from 1 to 13, carbon atoms A particularly preferred representative can be described by the formula A-1a:

In various embodiments, the compound of formula (I) is preferably the sodium salt of a linear alkyl benzene sulfonate.

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

In various embodiments, the compositions according to the invention preferably contain at least one anionic surfactant of the formula

R -O- (AO) _n -SO ₃ - X ⁺ (II).

In this formula (II), R is a linear or branched, substituted or

unsubstituted alkyl, aryl or alkylaryl radical, preferably a linear, unsubstituted alkyl radical, more preferably a fatty alcohol radical. Preferred radicals R are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl,

Octadecyl, nonadecyl, eicosyl and mixtures thereof, wherein the even number of C atoms are preferred. Particularly preferred radicals R 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. AO represents an ethylene oxide (EO) or propylene oxide (PO) moiety, preferably an ethylene oxide moiety. The index n stands for an integer from 1 to 50, preferably from 1 to 20 and especially from 2 to 10. Most preferably, n stands for the numbers 2, 3, 4, 5, 6, 7 or 8. X stands for a monovalent cation or the nth part of an n-valent cation, the alkali metal ions are preferred, and Na ⁺ or K ⁺ including Na, with Na ^{+ being} extremely preferred. Other cations X + may be selected from NhV, V Zn ²⁺ , 1H ² Mg ²⁺ , ¹ H Ca ²⁺ , ¹ Mn ²⁺ , and mixtures thereof.

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 = 1 1 to 19, n = 2, 3, 4, 5, 6, 7 or 8. Particularly preferred representatives are Na-Ci2-14

Fatty alcohol ether sulfates with 2 EO (k = 1 1-13, n = 2 in formula A-2).

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

Further usable anionic surfactants are the alkyl sulfates of the formula

R ² -O-S0 ₃ X ⁺ (III).

In this formula (III), R ^{2 is} a linear or branched, substituted or

unsubstituted alkyl radical, preferably a linear, unsubstituted alkyl radical, more 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, the representatives having an even number of C Atoms are preferred. Particularly preferred radicals R ² are derived from C 12-18 fatty alcohols, for example coconut oil fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or C 10 C 20 oxo alcohols. Y stands for a monovalent cation or the nth part of an n-valent cation, the alkali metal ions being preferred, and Na ⁺ or K ⁺ being preferred, Na ^{+ being} extremely preferred. Other cations Y + may be selected from NhV,

Mn ²⁺ , and mixtures thereof. In various embodiments, these surfactants are selected from fatty alcohol sulfates of Formula A-3

J _^ L ^ SO ^" Na ⁺

(A-3) with k = 1 1 to 19. Very particularly preferred representatives are Na-Ci2-14 fatty alcohol sulfates (k = 1 1-13 in formula A-3).

In various embodiments, the agent may contain, in addition to the anionic surfactants described above, in particular those of the formulas (I) - (III), or alternatively at least one other surfactant. Suitable alternative or additional surfactants are in particular further anionic surfactants, nonionic surfactants and mixtures thereof, but also cationic, zwitterionic and amphoteric surfactants.

In various embodiments, the agents comprise at least one nonionic surfactant, in particular at least one fatty alcohol alkoxylate.

Suitable nonionic surfactants are those of the formula

R ³ -O- (AO) _m -H (IV) in which

R ^{3 is} a linear or branched, substituted or unsubstituted alkyl radical,

AO for an ethylene oxide (EO) or propylene oxide (PO) grouping,

m stands for integers from 1 to 50.

In the abovementioned formula (IV), R ^{3 is} 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 and mixtures thereof, wherein the even number of C atoms are preferred. 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. AO represents an ethylene oxide (EO) or propylene oxide (PO) moiety, preferably an ethylene oxide moiety. The subscript m is an integer from 1 to 50, preferably from 1 to 20 and especially from 2 to 10. Most preferably, m is the numbers 2, 3, 4, 5, 6, 7 or 8.

In summary, preferably used fatty alcohol alkoxylates are compounds of the formula with k = 1 1 to 19, m = 2, 3, 4, 5, 6, 7 or 8. Very particularly preferred representatives are C12-18 fatty alcohols with 7 EO (k = 1 1-17, m = 7 in formula ( V)).

Other nonionic surfactants which may be included in the described compositions 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.

Suitable amphoteric surfactants are, for example, betaines of the formula (R 1) XR 1 XR 3 N-chloroCOO-, in which R ^{i is} an alkyl radical having 8 to 25, preferably 10 to 21 carbon atoms interrupted by hetero atoms or heteroatom groups and R ^iv and R ^{v are} identical or different alkyl radicals 1 to 3 carbon atoms, in particular Cio-Cis-alkyl dimethylcarboxymethylbetain and Cn-Ci7-alkylamidopropyl-dimethylcarboxymethylbetain.

Suitable cationic surfactants are i.a. the quaternary ammonium compounds of the formula

(R ^VI ) (R ^vii ) (R ^viii ) (R ^ix ) N ⁺ X ^" , in which R ^vi to R ^ix for four identical or different, in particular two long and two short-chain, alkyl radicals and X ^" for an anion , in particular a halide ion, for example, didecyldimethylammonium chloride, Alkylbenzyldidecylammoniumchlorid and mixtures thereof. Further suitable cationic surfactants are the quaternary surface-active compounds, in particular with a sulfonium, phosphonium, iodonium or

Arsonium group, which are also known as antimicrobial agents. Through the use of quaternary surface-active compounds with antimicrobial action, the agent can be designed with an antimicrobial effect or its possibly existing antimicrobial effect due to other ingredients can be improved. In various embodiments, the total amount of the surfactants based on the weight of the composition is 2 to 30% by weight, preferably 5 to 25% by weight, more preferably 10 to 20% by weight, most preferably 14 to 18% by weight. wherein the (linear) alkylbenzenesulfonates at most in an amount of 0.001 to 30 wt .-%, preferably 0.001 to 10 wt .-%, more preferably 2 to 6 wt .-%, more preferably 3 - 5 wt .-%, based on the weight of the agent.

Detergents or cleaners according to the invention may contain other enzymes in addition to the cutinase. These may be hydrolytic enzymes or other enzymes in a concentration effective for the effectiveness of the agent. One embodiment of the invention thus represents agents comprising one or more enzymes. Preferred enzymes are all enzymes which can develop a 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, and mixtures thereof. Enzymes are in the middle

advantageously each in an amount of 1 x 10 ^{~ 8} to 5 wt .-% based on active protein. Each enzyme is increasingly preferred in an amount of 1 x 10 -3 ^{~ 7} wt .-%, of 0.00001-1 wt .-%, of 0.00005 to 0.5 wt .-%, from 0.0001 to 0, 1 wt .-% and particularly preferably from 0.0001 to 0.05 wt .-% in inventive compositions, based on active protein. Particularly preferably, the enzymes show synergistic cleaning performance against certain stains or stains, ie the enzymes contained in the middle composition mutually 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 composition according to the invention.

The amylase (s) is 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 one-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.

The proteases used are preferably alkaline serine proteases. They act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are located inside peptides or proteins and thereby cause degradation of proteinaceous soils on the items to be cleaned. Their pH optimum is usually in the clearly alkaline range. The protein concentration can be determined by known methods, for example the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method. In this regard, the determination of the active protein concentration takes place via a titration of the active sites using a suitable irreversible inhibitor (for proteases, for example phenylmethylsulfonyl fluoride (PMSF)) and determination of the residual activity (compare M. Bender et al., J. Am. Chem. Soc , 24 (1966), pp. 5890-5913).

In the cleaning agents described herein, the enzymes to be used may also be formulated together with accompanying substances, for example from the fermentation. In liquid

Formulations, the enzymes are preferably used as enzyme liquid formulation (s).

The enzymes are usually not provided in the form of the pure protein, but rather in the form of stabilized, storable and transportable preparations. To this

Prefabricated preparations include, for example, the solid preparations obtained by granulation, extrusion or lyophilization or, especially in the case of liquid or gel-form detergents, solutions of the enzymes, advantageously as concentrated as possible, low in water and / or added with stabilizers or further auxiliaries.

Alternatively, the enzymes may be encapsulated for both the solid and liquid dosage forms, for example by spray-drying or extruding the enzyme solution together with a preferably natural polymer or in the form of capsules, for example those in which the enzymes are entrapped as in a solidified gel or in those of the core-shell type, in which an enzyme-containing core with a water, air and / or

Chemical-impermeable protective layer is coated. In deposited layers, further active ingredients, for example stabilizers, emulsifiers, pigments, bleaches or dyes, may additionally be applied. Such capsules are applied by methods known per se, for example by shaking or rolling granulation or in fluid-bed processes. Advantageously, such granules, for example by applying polymeric

Film former, low-dust and storage-stable due to the coating.

Furthermore, it is possible to assemble two or more enzymes together so that a single granule has several enzyme activities.

In various embodiments, the agent according to the invention may comprise one or more enzyme stabilizers. Therefore, the agent according to the invention can also have a

Enzyme stabilizer, for example, selected from the group consisting of sodium formate, sodium sulfate, lower aliphatic alcohols and boric acid and their esters and salts. Of course, two or more of these compounds may be used in combination become. The salts of the compounds mentioned can also be used in the form of hydrates, such as, for example, sodium sulfate decahydrate.

The term "lower aliphatic alcohols" as used herein includes monoalcohols, diols, and higher alcohols having up to 6 carbon atoms. As belonging to the group of lower aliphatic alcohols, in particular polyols, for example, glycerol, (mono) ethylene glycol, (Mono) Propylene glycol or sorbitol, without the invention being limited to these.

In addition to the at least one enzyme stabilizer selected from the above group, an agent of the invention may also contain at least one further stabilizer.

Such stabilizers are known in the art.

Reversible protease inhibitors protect the enzymes contained in a detergent or cleanser from proteolytic degradation by reversibly inhibiting the enzymatic activity of the proteases contained in the agent. As reversible protease inhibitors benzamidine hydrochloride, boronic acids or their salts or esters are frequently used, including in particular derivatives with aromatic groups, such as ortho, meta or para-substituted

Phenylboronic, in particular 4-formylphenyl-boronic acid, or the salts or esters of said compounds. Also, peptide aldehydes, that is oligopeptides with a reduced C-terminus, especially those of 2 to 50 monomers are used for this purpose. Among the peptidic reversible protease inhibitors include ovomucoid and leupeptin.

Other enzyme stabilizers are amino alcohols such as mono-, di-, triethanol- and -propanolamine and mixtures thereof, aliphatic carboxylic acids up to C12, such as succinic acid, other dicarboxylic acids or salts of said acids. End-capped fatty acid amide alkoxylates are also suitable for this purpose. Some organic acids used as builders can additionally stabilize an enzyme. Also calcium and / or magnesium salts are used for this purpose, such as calcium acetate.

Polyamide oligomers or polymeric compounds such as lignin, water-soluble vinyl copolymers or cellulose ethers, acrylic polymers and / or polyamides stabilize the enzyme preparation, inter alia, against physical influences or pH fluctuations. Polyamine N-oxide-containing polymers act simultaneously as enzyme stabilizers and as

Dye transfer inhibitors. Other polymeric stabilizers are linear Cs-ds polyoxyalkylenes. Also, alkylpolyglycosides can stabilize the enzymatic components of the agent according to the invention and, preferably, are capable of additionally increasing their performance. networked N-containing compounds preferably perform a dual function as soil release agents and as enzyme stabilizers. Hydrophobic, nonionic polymer stabilizes in particular an optionally contained cellulase.

Reducing agents and antioxidants increase the stability of the enzymes to oxidative degradation; For example, sulfur-containing reducing agents are familiar, for example sodium sulfite and reducing sugars.

In one embodiment, the compositions according to the present invention are liquid and contain water as the main solvent, i. they are aqueous agents. The water content of the aqueous composition of the present invention is usually 15 to 70% by weight, preferably 20 to 60% by weight. In various embodiments, the water content is more than 5% by weight, preferably more than 15% by weight and particularly preferably more than 50% by weight, in each case based on the total amount of agent.

In addition, non-aqueous solvents may be added to the composition. Suitable non-aqueous solvents include mono- or polyhydric alcohols, alkanolamines or glycol ethers, provided that they are miscible with water in the specified concentration range.

The solvents are preferably selected from ethanol, n-propanol, i-propanol, butanols, glycol, propanediol, butanediol, methylpropanediol, glycerol, diglycol, propyldiglycol, butyldiglycol, hexyleneglycol, 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 thereof

Solvent.

The one or more non-aqueous solvents is usually contained in an amount of 0.1 to 10% by weight, preferably 1 to 8% by weight, based on the total composition.

In addition to the components mentioned so far, the compositions according to the invention may contain further ingredients which further improve the performance and / or aesthetic properties of the cleaning agent. These include, for example, additives for improving the flow and drying behavior, for adjusting the viscosity and / or for stabilization, as well as other cleaning agents and additives customary in detergents, such as UV stabilizers, perfume, pearlescing agents, dyes, corrosion inhibitors, preservatives, bittering agents, organic Salts, disinfectants, structuring polymers, defoamers, encapsulated ingredients (eg encapsulated perfume), pH adjusters and skin feel-improving or nourishing additives.

An agent according to the invention, in particular washing or cleaning agent, preferably contains at least one water-soluble and / or water-insoluble, organic and / or

inorganic builders (builders).

Among the builders which can generally be used are, in particular, the aminocarboxylic acids and their salts, zeolites, silicates, carbonates, organic (co) builders and, where there are no ecological prejudices against their use, also the phosphates. Preferably, however, the agents are phosphate-free.

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 and also

Polyaspartic acid, polyphosphonic acids, in particular Aminotris (methylenphosphonsäure), ethylenediaminetetrakis (methylenephosphonic acid) and 1-hydroxyethane-1, 1-diphosphonic acid, polymeric hydroxy compounds such as dextrin and polymeric (poly) carboxylic acids, polymeric acrylic acids, methacrylic acids, maleic acids and copolymers thereof, which also small amounts of polymerizable substances without carboxylic acid functionality may contain polymerized. Suitable, although less preferred, compounds of this class are copolymers of acrylic or methacrylic acid with vinyl ethers, such as vinylmethyl ethers, vinyl esters, ethylene, propylene and styrene, in which the acid content is at least 50% by weight. The

Organic builder substances can be used, in particular for the preparation 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, in particular their alkali metal salts.

Organic builders may, if desired, be included in amounts of up to 40% by weight, more preferably up to 25% by weight, and preferably from 1% to 8% by weight. Quantities close to the stated upper limit are preferably used in paste-form or liquid, in particular water-containing, agents according to the invention. invention

Aftertreatment agents, such as e.g. Softener, may optionally also be free of organic builder.

As water-soluble inorganic builder materials are in particular alkali metal silicates and, if there are no concerns about their use, also polyphosphates, preferably

Sodium triphosphate, into consideration. As water-insoluble, water-dispersible inorganic Builder materials, 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 agents, in particular from 1 wt .-% to 5 wt .-%, are used , Among these are the detergent quality crystalline sodium aluminosilicates, especially zeolites A, P and

optionally X, preferred. Amounts near the above upper limit are preferably used in solid, particulate agents. Suitable aluminosilicates have, in particular, no particles with a particle size greater than 30 μm, and preferably consist of at least 80% by weight of particles having a size of less than 10 μm.

Suitable substitutes or partial substitutes for the said aluminosilicate are crystalline alkali silicates which may be present alone or in a mixture with amorphous silicates. The alkali metal silicates useful as builders in the compositions according to the invention preferably have a molar ratio of alkali metal oxide to SiO 2 below 0.95, in particular from 1: 1, 1 to 1: 12, and may be present in amorphous or crystalline form. Preferred alkali metal silicates are the sodium silicates, in particular the amorphous sodium silicates, with a molar ratio of Na 2 O: SiO 2 of from 1: 2 to 12.8. Crystalline silicates which may be present alone or in a mixture with amorphous silicates are preferably crystalline phyllosilicates of the general formula Na.sub.2SixO.sub.2.sup.x + H.sub.2O.sub.2, in which x, the so-called modulus, is a number from 1.9 to 4 and y is a number from 0 is up to 20 and preferred values for x are 2, 3 or 4. Preferred crystalline phyllosilicates are those in which x in the abovementioned general formula assumes the values 2 or 3. In particular, both beta- and delta-sodium disilicates (Na 2 Si 2 O y H 2 O) are preferred. Also prepared from amorphous alkali silicates, practically anhydrous crystalline alkali silicates of the abovementioned general formula in which x is a number from 1, 9 to 2.1, can be used in inventive compositions. In a further preferred embodiment of the composition according to the invention, a crystalline sodium layer silicate with a modulus of 2 to 3 is used, as can be prepared from sand and soda. Crystalline sodium silicates with a modulus in the range of 1.9 to 3.5 are used in a further preferred embodiment of compositions according to the invention. If alkali metal aluminosilicate, in particular zeolite, is also present as an additional builder substance, the weight ratio of aluminosilicate to silicate, in each case based on anhydrous active substances, is preferably 1:10 to 10: 1. In agents containing both amorphous and crystalline alkali metal silicates, the weight ratio of amorphous alkali metal silicate to crystalline alkali metal silicate is preferably 1: 2 to 2: 1 and especially 1: 1 to 2: 1.

Builders are, if desired, in the inventive compositions preferably in amounts of up to 60 wt .-%, in particular from 5 wt .-% to 40 wt .-%, included. Particularly preferred are water-soluble builders in liquid formulations. invention

Aftertreatment agents, such as fabric softeners, are preferably free of inorganic builder. For the purposes of the present invention, polymeric thickeners are the polycarboxylates which have a thickening effect as polyelectrolytes, preferably homopolymers and copolymers of acrylic acid, in particular acrylic acid copolymers such as acrylic acid-methacrylic acid copolymers, and the polysaccharides, in particular heteropolysaccharides, and other customary thickening polymers.

Suitable polysaccharides or heteropolysaccharides are the polysaccharide gums, for example gum arabic, agar, alginates, carrageenans and their salts, guar, guar gum, tragacanth, gellan, Ramzan, dextran or xanthan and their derivatives, e.g. propoxylated guar, as well as their mixtures. Other polysaccharide thickeners, such as starches or cellulose derivatives, may be used alternatively, but preferably in addition to a polysaccharide gum, for example starches of various origins and starch derivatives, e.g. Hydroxyethyl starch, starch phosphate esters or starch acetates, or carboxymethyl cellulose or its sodium salt, methyl, ethyl, hydroxyethyl, hydroxypropyl, hydroxypropylmethyl or hydroxyethyl methyl cellulose or cellulose acetate.

Acrylic acid polymers suitable as polymeric thickeners are, for example

high molecular weight with a polyalkenyl, in particular an allyl ether of sucrose, pentaerythritol or propylene, crosslinked homopolymers of acrylic acid (INCI Carbomer), which are also referred to as carboxyvinyl polymers.

However, 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 ester, preferably formed with C 1-4 alkanols (INCI acrylates copolymer), to which approx 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) crosslinked high molecular weight acrylic acid copolymers, such as those crosslinked with an allyl ether of sucrose or pentaerythritol copolymers of Cio-30-alkyl acrylates with one or more monomers from the group of acrylic acid, methacrylic acid and their simple, preferably with Ci-4-alkanols formed esters (INCI acrylates / C 10-30 alkyl acrylate crosspolymer).

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 composition.

To stabilize the agent according to the invention, in particular at high surfactant content, one or more dicarboxylic acids and / or salts thereof can be added, in particular a composition of Na salts of adipic, succinic and glutaric acid, as described, for example, in US Pat Trade name Sokalan ^® DSC is available. The use is advantageously carried out 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 it is possible to dispense with their use, this is the agent according to the invention

preferably free from dicarboxylic acid (salts) n.

The detergents according to the invention can be compared with reference detergents in order to determine the increased anti-pilling performance of the compositions according to the invention. Such

Washing system can be composed as follows (all figures in weight percent):

Reference agent: 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% defoamer, 2.0% glycerol, 0.08% preservatives, 1% ethanol, 1, 6% enzyme mix (protease, amylase, cellulase, mannase), balance demineralized water. Composition according to the invention: 4.4% of alkylbenzenesulfonic acid, 5.6% of other anionic surfactants, 2.4% of C12-C18 Na salts of fatty acids (soaps), 4.4% of nonionic surfactants, 0.2% of phosphonates, 1, 4% citric acid, 0.95% NaOH, 0.01% defoamer, 2.0% glycerol, 0.08% preservatives, 1% ethanol, 1, 6% enzyme mix (protease, amylase, cellulase, mannose), 0.009% cutinase , Rest demineralized water. Preferably, the 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. Preference is given to washing in a pH range between pH 8 and pH 10.5, preferably between pH 8 and pH 9.

The abovementioned embodiments of the present invention comprise all solid, powdery, liquid, gelatinous or paste-like administration forms of agents according to the invention which, if appropriate, may also consist of several phases and may be present in compressed or uncompressed form. The agent can be present as 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. The solid dosage forms of the composition also include extrudates, granules, tablets or pouches. Alternatively, the agent can also be liquid, gelatinous 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 present as a one-component system. Such funds consist of one phase. Alternatively, an agent can also consist of several phases, ie be, for example, one or two or more phases. Such an agent is therefore divided into several components (multi-component system). Another object of the invention is a process for the cleaning of textiles, which is characterized in that in at least one process step, an inventive agent is applied. The textiles preferably contain or consist of polyester.

In various embodiments, the method described above is characterized in that the agent according to the invention at a temperature of 0-100 ^° C, preferably 0-80 ^° C, more preferably 30-70 and most preferably at 40-60 is used.

These include both manual and mechanical processes, with mechanical processes being preferred. Methods for cleaning textiles are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned and washed off after the contact time, or that the items to be cleaned are otherwise treated with a detergent or a solution or dilution of this product. All conceivable washing or cleaning methods can be enriched in at least one of the method steps to the application 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 means according to the invention are also applicable to this subject of the invention , Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive method.

Since enzymes naturally already have a catalytic activity and they also unfold in media that otherwise have no cleaning power, such as in bare buffer, a single and / or the only step of such a method is that the only cleaning active component is a cutinase with the Pollution is brought into contact, preferably in a buffer solution or in water. This represents a further embodiment of this subject of the invention.

Alternative embodiments of this subject matter of the invention are also processes for the treatment of textile raw materials or for textile care, in which at least one

Process step, an inventive agent is active. Below are methods for

Textile raw materials, fibers or textiles with synthetic components preferred, and especially for those with polyester.

Furthermore, the invention also encompasses the use of the agent described herein, for example as detergents or cleaners as described above, for the (improved) removal of stains, for example textiles, in particular polyester textiles. Finally, the invention also relates to the use of a cutinase for reducing pilling effects of an agent, preferably a detergent, more preferably a liquid detergent, wherein the agent contains the cutinase. The cutinase is a cutinase as defined herein. In various embodiments of use, the cutinase is present in an amount of 0.00001-1 wt%, preferably in an amount of 0.0001-0.5 wt%, more preferably in an amount of 0.001-0.1 Wt .-%, contained in the agent. In further

According to various embodiments, the cutinase, which causes a reduction of the pilling effect, is applied to textiles, in particular textiles consisting of polyester or polyester.

All facts, objects and embodiments which are described for agents according to the invention and the cutinase are also applicable to the other subjects of the invention. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive method and the uses of the invention.

Examples

Example 1: Cloning and Expression

The gene was made codon-optimized for expression in E. coli (SEQ ID NO: 3), and then cloned into the Ndel and Xho I sites of Novagen's PET-21b vector to form a fusion with C-terminal a 6x histidine tag is formed. The sequencing-confirmed plasmid is transformed by conventional transformation protocols into electrocompetent cells E. coli BL21 (DE3) CodonPlus RIPL (Agilent Technologies).

The cultivation is carried out in LB medium at 37 ° C, with an induction with 0, 1 mM IPTG at an OD of 0.6 and then lowered to 16 ° C expression temperature.

The cells are harvested by centrifugation and resuspended in Lysis buffer (50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 20 mM Imidazole). The cell disruption is carried out by means of ultrasound, followed by centrifugation (15,000 x g, 20 min, 4 ° C). The supernatant contains the LC cutinase with HisTag.

Purification via NiNTA (Qiagen, Hilden, DE) is carried out according to the protocol of the manufacturer Qiagen.

Example 2: Examination by means of QCM-D

The degradation kinetics of the polyesterases described here were analyzed by QCM-D (quartz crystal microbalance with dissipation monitoring). The preparation of the polyester model substrates was carried out from commercially available AT-Cut QCM-D crystals (Biolin Scientific) with a typical resonance frequency of 5 MHz and a gold-terminated electrode. By means of a spin coating process these crystals were modified with a polyester thin film.

At the beginning of the measurement, the modified crystals were equilibrated in a flow-through with Tris-HCl buffer (volume flow 60 μΙ-min ^_ ) and a constant temperature (T = 50 ° C) measuring cell until a stable baseline was reached (Fig. T = 0h to t = 0.5h).

Subsequently, the Tris-HCl buffer submitted was exchanged for a buffer solution containing (c = 0.15 mg / ml) cutinase (SEQ ID NO: 1) (FIG. 1: t = 0.5 h) and after the dead time as a consequence of Film degradation occurring mass decrease recorded (Fig. 1: t = 0.55h to t = 1, 1 h). From the results shown in Figure 1 you can clearly see the rapidly occurring mass decrease, caused by the cutinase. Example 3: PET film degradation test

Substrate: PET film: 0.25 mm thick, amorphous, clear from GoodFellow Cambridge Limited, ES301445

Execution in 2 mL tubes

PET film (0.5 cm x 2.5 cm) was washed with (1) 1, 7 mL 0, 1% SDS (w / v), 50 ° C, 30 min, 400 rpm; (2) 1, 5 mL of ethanol abs., 50 ° C, 5 min, 700 rpm; (3) Dried 1, 7 mL of double-distilled water, 50 ° C, 5 min, 700 rpm and 48 h at 50 ° C to constant and weighed. This was followed by incubation (48-72 h at 55 ° C.) with defined amount of cutinase according to SEQ ID NO: 1 (5, 25, 50 μg) in the total volume 1.7 mL in detergent matrix (see below, dosage 4.7 g / L).

After removal of the incubation supernatant, the PET film was washed with (1) 1, 7 mL 0, 1% SDS (w / v) + 0.5% Triton X-100 (w / v), 50 ° C, 30 min, 400 rpm; (2) 1, 5 mL ethanol abs., 50 ° C, 5 min, 700 rpm, (3) 1, 7 mL double-distilled water, 50 ° C, 5 min, 700 rpm and 48 h at 50 ° C until Constance dried and weighed. The weight loss was determined.

Result:

The weight loss is given in comparison to the untreated film after 44 h incubation at 50 ° C.

Detergent containing 25 μg cutinase: - 0.57 mg weight loss

Detergent containing 50 μg cutinase: - 1, 67 mg weight loss

It can be seen clearly a concentration-dependent PET degradation, caused by the cutinase in the detergent matrix.

Example 4: Washing test

Used detergent matrix

This is a commercial detergent matrix (without optical brightener, perfume and dyes) that was used for the wash test:

Wt% wt%

Active substance in the active substance in the

Chemical name raw material formulation

Water demin. 100 remainder

Alkylbenzenesulfonic acid 96 4.4

Anionic surfactants 70 5.6

C12-C18 fatty acid Na salt 30 2,4 Nonionic surfactants 100 4.4

Phosphonates 40 0.2

Citric acid 100 1, 4

NaOH 50 0.95

Defoamer t.q. 0.01

Glycerol 100 2

Preservative 100 0.08

Ethanol 93 1

Without opt. Brightener, dye, perfume

and enzymes

Dosage 4.7 g / L

Washing test to determine the anti-pilling performance of enzymes

In a commercial washing machine, 20 identical tests are carried out in succession. The textiles to be assessed are various polyesters and mixed textiles, which are once new and once pre-pilled. After the 20 attempts, the

Pillreduktion of the pre-pilled fabrics and the pilling of the new tissues visually assessed.

The pre-pilled tissues are washed 20 times at 40 ° C in

commercially available washing machines.

After each wash cycle, the entire laundry is dried in the dryer. Washing conditions:

Water at 16 ° dH, 2.5 kg clean wash, 60 ° C normal program, 80 g detergent as described above per machine

Dosage of the cutinase to be examined: 4 mg of 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 matching 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 considered significant.

The cutinase according to the invention significantly improves the pill appearance.

Claims

claims

1. agent, in particular a detergent or cleaning agent, characterized in that it contains a cutinase having at least 65% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over the entire length thereof.

2. The composition according to claim 1, characterized in that the cutinase a

Amino acid sequence corresponding to the amino acid sequence given in SEQ ID NO: 1 over the total length thereof 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.

3. The agent according to claim 1 or 2, characterized in that

(1) the cutinase from a cutinase according to claim 1 or 2 is obtainable as a starting molecule by one or more conservative amino acid substitution; and or

(2) The cutinase from a cutinase according to claim 1 or 2 as the starting molecule

is obtainable by fragmentation, deletion, insertion or substitution mutagenesis and comprises an amino acid sequence 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 matches the parent molecule.

The agent of any one of claims 1 to 3, wherein the cutinase is present in an amount of

0.00001-1% by weight, preferably in an amount of 0.0001-0.5% by weight, more preferably in an amount of 0.001-0.1% by weight, in the composition.

5. The agent according to one of claims 1 to 4, characterized in that

a. at least one additional ingredient selected from the group consisting of surfactants, builders, bleaches, bleach activators, water-miscible organic solvents, other enzymes, sequestering agents, electrolytes, pH regulators, optical brighteners, grayness inhibitors, foam regulators, dyes and fragrances, and combinations contains thereof; and or

b. it is in solid or liquid, preferably liquid, form.

6. A process for the cleaning of textiles, characterized in that in at least one process step, an agent according to any one of claims 1 to 5 is applied.

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

8. Use of an agent according to any one of claims 1 to 5 for the removal of

Soiling, in particular of polyester-containing textiles.

9. Use of a cutinase which has at least 65% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length, in order to reduce pilling effects and / or increase the anti-gray effect of an agent, preferably a detergent, in particular preferably a liquid detergent, wherein the agent contains the cutinase.

10. The use according to claim 9, wherein

a. the cutinase as defined in claim 2 or 3; and or

b. the cutinase is contained in an amount as defined in claim 4 in the agent; and or

c. the agent is as defined in claim 5.