DE102019210806A1 - Laundry detergent with a Bacillus gibsonii protease - Google Patents

Abstract

The invention relates to a laundry detergent, in particular a solid laundry detergent, comprising at least one protease which comprises an amino acid sequence which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length and which has an amino acid substitution in at least one of the positions which to positions 12, 43, 122, 127, 154, 156, 160, 211, 212 or 222, each based on the numbering according to SEQ ID NO: 1, and corresponding cleaning methods and uses of such textile detergents.

Description

The invention is in the field of enzyme technology. The invention relates in particular to a laundry detergent comprising at least one Bacillus gibsonii protease, the amino acid sequence of which has been modified, particularly with regard to its use in laundry detergents. Also part of the invention are the corresponding washing methods, the use of the agents described herein and the use of Bacillus gibsonii proteases in detergents and the use of Bacillus gibsonii proteases for removing protease-sensitive soiling from textiles.

The use of enzymes in detergents and cleaning agents has been established in the state of the art for decades. They serve to expand the range of services of the funds in question according to their special activities. These include in particular hydrolytic enzymes such as proteases, amylases, lipases and cellulases. The first three mentioned hydrolyze proteins, starch and fats and thus contribute directly to dirt removal. Cellulases are used in particular because of their tissue effect. Another group of detergent and cleaning agent enzymes are oxidative enzymes, in particular oxidases, which, optionally in conjunction with other components, preferably serve to bleach soiling or to generate the bleaching agents in situ. In addition to these enzymes, which are subject to continuous optimization, other enzymes are constantly being made available for use in detergents and cleaning agents in order to be able to optimally tackle special soiling, such as pectinases, ß-glucanases, mannanases or other hemicellulases (glycosidases) Hydrolysis of special vegetable polymers in particular.

The longest established enzymes contained in practically all modern, powerful detergents and cleaning agents are proteases. This makes them one of the technically most important enzymes of all. Among these, proteases of the subtilisin type (subtilases, subtilopeptidases, EC 3.4.21.62) are particularly important, which are serine proteases due to the catalytically active amino acids. They act as non-specific endopeptidases and hydrolyze any acid amide bonds that are inside peptides or proteins. Their pH optimum is usually in the clearly alkaline range. An overview of this family is offered, for example, in the article “Subtilases: Subtilisin-like Proteases” by R. Siezen, pages 75-95 in “Subtilisin enzymes”, edited by R. Bott and C. Betzel, New York, 1996. Subtilases are natural formed by microorganisms. Among these, the subtilisins formed and secreted by Bacillus species should be mentioned as the most important group within the subtilases.

In general, only selected proteases are suitable for use in liquid surfactant-containing preparations. Many proteases do not show sufficient catalytic performance in such preparations or they are not sufficiently stable. For the use of proteases in laundry detergents, a high catalytic activity and stability under conditions such as those presented during a washing process are therefore particularly desirable.

One goal in the development of detergent or cleaning agent formulations is therefore to change the enzymes contained in them using methods known from the prior art in a targeted or random manner and thus to optimize them for use in washing and cleaning agents. These include, for example, point mutagenesis, deletion or insertion mutagenesis or fusion with other proteins or protein parts.

The object was therefore to further improve the washing performance of laundry detergents.

Surprisingly, it has now been found that a Bacillus gibsonii protease, as defined herein, shows an improved cleaning performance on protease-sensitive soils compared to conventional proteases and is therefore particularly suitable for use in detergents.

In a first aspect, the present invention therefore relates to a laundry detergent comprising at least one protease which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length and which has an amino acid substitution in at least one of the positions corresponding to the positions 12, 43, 122, 127, 154, 156, 160, 211, 212 and 222, each based on the numbering according to SEQ ID NO: 1. The detergent according to the invention is preferably a solid laundry detergent. More preferably, the solid laundry detergent according to the invention in a 1% strength by weight solution in deionized water at 20 ° C. has a pH in a range from 7 to 12, in particular 8 to 12, preferably 9 to 11 and particularly preferably 10 to 11 .

In particular, textile detergents according to the invention also show performance advantages over other textile detergents if the textile detergents contain at least one additional enzyme of the same or a different type, e.g. amylase, cellulase, lipase, mannanase or pectinase, although the list of further enzymes is not complete. It is therefore preferred that the laundry detergents according to the invention contain at least one additional enzyme of the same type (ie a further protease) or of a different type.

The agents according to the invention also have an advantage over conventional textile detergents in particular when they contain bleach, in particular an inorganic or organic source of peroxide bleach. In preferred embodiments, a laundry detergent according to the invention contains 2 to 30% by weight, preferably 5 to 25% by weight and particularly preferably 10 to 20% by weight of sodium percarbonate. In further preferred embodiments, a laundry detergent according to the invention contains 1 to 10% by weight, preferably 1.5 to 7.5% by weight and particularly preferably 2 to 5% by weight of TAED. In particularly preferred embodiments, a laundry detergent according to the invention contains 10 to 20 wt.% Sodium percarbonate and / or 2 to 5 wt.% TAED.

Another object of the invention is a method for producing such a detergent.

Another object of the invention is the use of such a detergent for cleaning textiles.

Another object of the invention is a use of a protease which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length and which has an amino acid substitution in at least one of the positions corresponding to positions 12, 43, 122, 127 , 154, 156, 160, 211, 212 and 222, each based on the numbering according to SEQ ID NO: 1, for removing protease-sensitive soiling from textiles.

Particularly preferably, a Bacillus gibsonii protease is used in the agents, methods and uses according to the invention which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length and which has at least one of the amino acid substitutions Q12L, I43V, M122L, D127P, N154S, T156A, G160S, M211N, M211L, P212D, P212H or A222S in at least one of the positions corresponding to positions 12, 43, 122, 127, 154, 156, 160, 211, 212 and 222, each based on the numbering according to SEQ ID NO: 1, have.

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. Each feature from one aspect of the invention can be used in any other aspect of the invention. Furthermore, it goes without saying that the examples contained herein are intended to describe and illustrate the invention, but not to restrict it, and in particular the invention is not limited to these examples.

Unless otherwise stated, all percentages are percentages by weight. Numeric ranges specified in the format “from x to y” include the stated values. If several preferred numerical ranges are given in this format, it is understood that all ranges resulting from the combination of the various endpoints are also recorded. "At least one" as used herein means one or more, i.e. 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14 or more. The term “detergent”, as used herein, is synonymous with the term “textile detergent” or “agent” and denotes a composition for cleaning textiles as explained in the description. “About”, “about” or “approximately”, as used herein in relation to a numerical value, relate to the corresponding numerical value ± 10%, preferably ± 5%.

The present invention is based on the surprising finding of the inventors that a Bacillus gibsonii protease which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length and which has at least one amino acid substitution in at least one of the positions corresponding to the positions 12, 43, 122, 127, 154, 156, 160, 211, 212 or 222 of the protease from Bacillus gibsonii according to SEQ ID NO: 1, in particular at least one of those from Q12L, I43V, M122L, D127P, N154S , T156A, G160S, M211N, M211L, P212D, P212H or A222S existing group of selected amino acid substitution, shows an improved cleaning performance on protease-sensitive soiling compared to conventional proteases.

This is particularly surprising insofar as no such Bacillus gibsonii protease has been associated with improved cleaning performance in detergents, in particular solid laundry detergents.

The proteases used according to the invention have enzymatic activity, i.e. they are capable of hydrolyzing peptides and proteins, especially in detergents. A protease used according to the invention is therefore an enzyme which catalyzes the hydrolysis of amide / peptide bonds in protein / peptide substrates and is thereby able to cleave proteins or peptides. Furthermore, a protease used according to the invention is preferably a mature protease, i.e. the catalytically active molecule without signal and / or propeptide (s). Unless stated otherwise, the specified sequences also relate to mature (processed) enzymes.

In various embodiments of the invention the protease is a free enzyme. This means that the protease can act directly with all components of an agent and, if the agent is a liquid agent, that the protease is in direct contact with the agent's solvent (e.g. water). In other embodiments, an agent can contain proteases that form an interaction complex with other molecules or that contain an “envelope”. A single or multiple protease molecule (s) can be separated from the other components of the agent by a structure surrounding them. Such a separating structure can arise from, but is not limited to, vesicles such as a micelle or a liposome. The surrounding structure can also be a virus particle, a bacterial cell or a eukaryotic cell. In various embodiments, an agent can contain cells from Bacillus gibsonii or Bacillus subtilis which express the proteases according to the invention, or cell culture supernatants of such cells.

The Bacillus gibsonii protease used according to the invention contains in various embodiments at least one amino acid substitution selected from the group consisting of Q12L, I43V, M122L, D127P, N154S, T156A, G160S, M211N, M211L, P212D, P212H or A222S, each based on the numbering according to SEQ ID NO: 1 is selected. In further preferred embodiments, the protease used according to the invention contains one of the following amino acid substitution variants: (i) I43V; (ii) M122L, N154S, and T156A; (iii) M211N and P212D; (iv) M211L and P212D; (v) G160S; (vi) D127P, M211L and P212D; (vii) P212H; or (viii) Q12L, M122L and A222S, the numbering in each case being based on the numbering according to SEQ ID NO: 1.

In a further embodiment of the invention, the protease used according to the invention comprises an amino acid sequence which is at least 70% and increasingly preferably at least 71%, 72%, 73%, 74%, 75% of the total length of the amino acid sequence given in SEQ ID NO: 1 %, 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% and 98.8% is identical, and those in at least one of the positions corresponding to positions 12, 43, 122, 127, 154, 156, 160, 211, 212 or 222 in the number according to SEQ ID NO: 1, one or more of the amino acid substitutions 12L, 43V, 122L, 127P, 154S, 156A, 160S, 211N, 211L, 212D, 212H or 222S.

In connection with the present invention, the feature that a protease has at least one of the specified substitutions means that it contains at least one of the corresponding amino acids at the corresponding positions, ie not all of the 10 positions otherwise mutated or deleted, for example by fragmentation of the protease are.

Advantageous positions for sequence changes, in particular substitutions, of the protease from Bacillus gibsonii, which are preferably of importance when transferred to homologous positions of the proteases used according to the invention and which give the protease advantageous functional properties, are accordingly the positions which in an alignment are positions 12, 43, 122, 127, 154, 156, 160, 211, 212 and 222 in SEQ ID NO: 1, ie in the number according to SEQ ID NO: 1. The following amino acid residues are located in the wild-type molecule of the protease from Bacillus gibsonii at the positions mentioned: Q12, 143, M122, D127, N154, T156, G160, M211, P212 and A222.

The identity of nucleic acid or amino acid sequences is determined by a sequence comparison. This sequence comparison is based on the BLAST algorithm that is established and commonly used in the prior art (cf. Altschul et al. (1990) "Basic local alignment search tool", J. Mol. Biol. 215: 403-410 and Altschul et al. (1997) "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs", Nucleic Acids Res., 25: 3389-3402 ) and basically happens because similar Sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences are assigned to one another. A tabular assignment of the relevant positions is called an 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. The Clustal series, for example (cf.e.g. Chenna et al. (2003) "Multiple sequence alignment with the cluster series of programs", Nucleic Acid Res. 31: 3497-3500 ), T-Coffee (cf.e.g. Notredame et al. (2000) "T-Coffee: A novel method for multiple sequence alignments", J. Mol. Biol. 302: 205-217 ) or programs based on these programs or algorithms. Sequence comparisons (alignments) are also possible with the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the specified standard parameters, whose AlignX module for the sequence comparisons is based on ClustalW. Unless otherwise stated, the sequence identity given herein is determined using the BLAST algorithm.

Such a comparison also allows a statement about the similarity of the compared sequences to one another. It is usually given in percent identity, i.e. the proportion of identical nucleotides or amino acid residues in the same positions or in positions corresponding to one another in an alignment. The broader term of homology includes conserved amino acid exchanges in the case of amino acid sequences, 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 given as percent homology or percent similarity. Identity and / or homology information can be made over entire polypeptides or genes or only over individual areas. 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 only contain a few nucleotides or amino acids. Such small areas often have essential functions for the overall activity of the protein. It can therefore be useful to refer to sequence matches only to individual, possibly small areas. Unless otherwise stated, the identity or homology information in the present application relates to the total length of the nucleic acid or amino acid sequence specified in each case. In connection with the present invention, the statement that an amino acid position corresponds to a numerically designated position in SEQ ID NO: 1 means that the corresponding position is assigned to the numerically designated position in SEQ ID NO: 1 in an alignment as defined above.

The present invention also relates to a detergent with a protease, characterized in that the protease can be obtained from a protease according to the invention as the starting molecule by one or more conservative amino acid substitutions. The term "conservative amino acid substitution" means the exchange (substitution) of an amino acid residue for another amino acid residue, whereby this exchange does not lead to a change in 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.

Another object of the present invention is a detergent comprising a protease, characterized in that the protease can be obtained from a protease according to the invention as a starting molecule by fragmentation, deletion, insertion or substitution mutagenesis and comprises an amino acid sequence that extends over a length of at least 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 261, 262, 263, 264, 265, 266, 267, 268 or 269 contiguous amino acids match the parent molecule.

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 proteolytic activity. Furthermore, such fragmentation, deletion, insertion or substitution mutagenesis, for example, can also reduce the allergenicity of enzymes concerned and thus improve their overall usability. The enzymes advantageously retain their proteolytic activity even after mutagenesis, i.e. their proteolytic activity corresponds at least to that of the starting enzyme. Substitutions can also have beneficial effects. Both single and several connected amino acids can be exchanged for other amino acids.

• - Veränderung der Bindung von Metallionen, insbesondere der Calcium-Bindungsstellen, z.B. durch Austauschen einer oder mehrerer der an der Calcium-Bindung beteiligten Aminosäure(n) gegen eine oder mehrere negativ geladene Aminosäuren und/oder durch Einführen von Sequenzveränderungen in mindestens einer der Folgen der beiden Aminosäuren Arginin/Glycin;
• - Schutz gegen den Einfluss denaturierender Agentien wie Tensiden durch Mutationen, die eine Veränderung der Aminosäuresequenz auf oder an der Oberfläche des Proteins bewirken;
• - Austausch von Aminosäuren, die nahe dem N-Terminus liegen, gegen solche, die vermutlich über nicht-kovalente Wechselwirkungen mit dem Rest des Moleküls in Kontakt treten und somit einen Beitrag zur Aufrechterhaltung der globulären Struktur leisten.

A protease according to the invention can additionally be stabilized, in particular by one or more mutations, for example substitutions, or by coupling to a polymer. Because an increase in the stability during storage and / or during use, for example during the washing process, leads to the enzymatic activity lasts longer and thus the cleaning performance is improved. In principle, all stabilization options described and / or expedient in the prior art come into consideration. Stabilizations that are achieved via mutations of the enzyme itself are preferred, since such stabilizations do not require any further work steps following the recovery of the enzyme. Further stabilization options include:

• - Change in the binding of metal ions, in particular the calcium binding sites, for example by exchanging one or more of the amino acid (s) involved in calcium binding for one or more negatively charged amino acids and / or by introducing sequence changes in at least one of the consequences of the two amino acids arginine / glycine;
• - Protection against the influence of denaturing agents such as surfactants by mutations that cause a change in the amino acid sequence on or on the surface of the protein;
• - Replacement of amino acids that are close to the N terminus for those that presumably come into contact with the rest of the molecule via non-covalent interactions and thus contribute to maintaining the globular structure.

Preferred embodiments are those in which the enzyme is stabilized in several ways, since several stabilizing mutations act additively or synergistically.

Another object of the invention is a protease as described above, which is characterized in that it has at least one chemical modification. A protease with such a change is called a derivative, i.e. the protease is derivatized. In the context of the present application, derivatives are accordingly understood to mean those proteins whose pure amino acid chain has been chemically modified. Such derivatizations can occur, for example, in vivo by the host cell expressing the protein. In this regard, couplings of low molecular weight compounds such as lipids or oligosaccharides should be particularly emphasized. However, derivatizations can also be carried out in vitro, for example by chemically converting a side chain of an amino acid or by covalently binding another compound to the protein. For example, it is possible to couple amines to carboxyl groups of an enzyme to change the isoelectric point. Such a different compound can also be a further protein which is bound to a protein according to the invention, for example via bifunctional chemical compounds. Likewise, derivatization is to be understood as the covalent bond to a macromolecular carrier, or also a non-covalent inclusion in suitable macromolecular cage structures. Derivatizations can, for example, influence the substrate specificity or the strength of the bond to the substrate or cause a temporary blockage of the enzymatic activity if the coupled substance is an inhibitor. This can be useful e.g. for the period of storage. Such modifications can also affect the stability or the enzymatic activity. They can also serve to reduce the allergenicity and / or immunogenicity of the protein and thus, for example, to increase its skin tolerance. For example, couplings with macromolecular compounds, e.g. polyethylene glycol, can improve the protein in terms of stability and / or skin tolerance. In the broadest sense, derivatives of a protein according to the invention can also be understood to mean preparations of these proteins. Depending on its extraction, processing or preparation, a protein can be associated with various other substances, e.g. from the culture of the producing microorganisms. A protein can also have been specifically mixed with other substances, e.g. to increase its storage stability. All preparations of a protein according to the invention are therefore also in accordance with the invention. This is also independent of whether it actually displays this enzymatic activity in a certain preparation or not. This is because it may be desirable for it to have little or no activity during storage and to only develop its enzymatic function at the time of use. This can be controlled, for example, via corresponding accompanying substances.

Numerous proteases and in particular subtilisins are formed as so-called preproteins, i.e. together with a propeptide and a signal peptide, the function of the signal peptide usually being to ensure the release of the protease from the cell producing it into the periplasm or the medium surrounding the cell, and the propeptide is usually necessary for the protease to fold correctly. The signal peptide and the propeptide are usually the N-terminal part of the preprotein. The signal peptide is split off from the rest of the protease under natural conditions by a signal peptidase. This is followed by the correct final folding of the protease supported by the propeptide. The protease is then in its active form and cleaves the propeptide itself. After the propeptide has been cleaved off, the then mature protease, in particular subtilisin, exerts its catalytic activity without the originally present N-terminal amino acids. For technical applications in general and in particular within the scope of the invention, the mature (mature) proteases, ie those after their production processed enzymes, preferred over preproteins. The proteases can also be modified by the cells producing them after the production of the polypeptide chain, for example by attaching sugar molecules, formylations, aminations, etc. Such modifications are post-translational modifications and can but do not have to have an influence on the function of the protease.

“Variant”, as used herein, relates to natural or artificially generated variations of a native protease which has an amino acid sequence which is modified from the reference form. In addition to the amino acid changes explained above, proteases according to the invention can have further amino acid changes, in particular amino acid substitutions, insertions or deletions. Such proteases are, for example, further developed through targeted genetic modification, i.e. through mutagenesis processes, and optimized for specific purposes or with regard to special properties (e.g. with regard to their catalytic activity, stability, etc.). Furthermore, nucleic acids according to the invention can be introduced into recombination batches and thus used to generate completely new proteases or other polypeptides. The aim is to introduce specific mutations such as substitutions, insertions or deletions into the known molecules, e.g. to improve the cleaning performance of enzymes. 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. For example, the net charge of the enzymes can be changed in order to influence the substrate binding, especially for use in detergents and cleaning agents. As an alternative or in addition, one or more corresponding mutations can increase the stability or catalytic activity of the enzyme and thereby improve its cleaning performance. Advantageous properties of individual mutations, e.g. individual substitutions, can complement each other. A protease that has already been optimized with regard to certain properties can therefore be further developed within the scope of the invention, e.g. with regard to its stability towards surfactants and / or bleaching agents and / or other components.

The following convention is used for the description of substitutions that affect exactly one amino acid position (amino acid substitutions): first the naturally present amino acid is designated in the form of the internationally common single-letter code, then the associated sequence position and finally the inserted amino acid. Multiple exchanges within the same polypeptide chain are separated from one another by slashes. In the case of insertions, additional amino acids are named after the sequence position. In the case of deletions, the missing amino acid is replaced by a symbol, e.g. an asterisk or a dash, or a Δ is given in front of the corresponding position. For example, P14H describes the substitution of proline at position 14 by histidine, P14HT the insertion of threonine after the amino acid histidine at position 14 and P14 * or ΔP14 the deletion of proline at position 14. This nomenclature is known to those skilled in the field of enzyme technology.

The amino acid positions are defined by aligning the amino acid sequence of a protease used according to the invention with the amino acid sequence of the protease from Bacillus gibsonii, as indicated in SEQ ID NO: 1. Furthermore, the allocation of the positions is based on the mature (mature) protein. This assignment is also to be used in particular if the amino acid sequence of a protease used according to the invention comprises a higher number of amino acid residues than the protease from Bacillus gibsonii according to SEQ ID NO: 1. Starting from the positions mentioned in the amino acid sequence of the protease from Bacillus gibsonii, the change positions in a protease used according to the invention are those which are assigned to precisely these positions in an alignment.

A detergent according to the invention contains the protease increasingly preferably in an amount of 1 × 10 ^-8 to 5% by weight, from 0.0001 to 1% by weight, from 0.0005 to 0.5% by weight, from 0.001 up to 0.1% by weight, each based on active protein.

The protein concentration can be determined using known methods, e.g. the BCA method (bicinchoninic acid; 2,2'-bichinolyl-4,4'-dicarboxylic acid) or the biuret method ( Gornall et al., 1948, J. Biol. Chem., 177: 751-766 ) can be determined. The active protein concentration can be determined by titrating the active centers using a suitable irreversible inhibitor and determining the residual activity ( Bender et al., 1966, J. Am. Chem. Soc. 88 (24): 5890-5913 ) respectively.

Preferred embodiments of proteases according to the invention achieve such advantageous cleaning performance even at low temperatures, in particular in the temperature ranges between 10 and 60 ° C, preferably between 15 and 50 ° C and particularly preferably between 20 and 40 ° C.

In the context of the invention, cleaning performance is understood to mean the ability of an agent to partially or completely remove existing soiling, in particular the lightening performance of one or more soiling on textiles. Examples of such soiling are blood on cotton or chocolate-milk / soot on cotton, cocoa on cotton or porridge on cotton. Within the scope of the invention, both the detergent which comprises the protease or the washing liquor formed by this agent and the protease itself have a respective cleaning performance. The cleaning performance of the protease thus contributes to the cleaning performance of the agent or the washing liquor formed by the agent. The cleaning performance is preferably determined as indicated below.

The washing liquor is understood to be that solution containing the detergent which acts on the textiles and thus comes into contact with the soiling present on the textiles. The washing liquor is usually created when the washing process begins and the detergent is diluted with water, e.g. in a washing machine or in another suitable container.

The cleaning performance is determined in a washing system that contains a detergent in a dosage between 3.5 and 6.5 grams per liter of washing liquor and the protease. The proteases to be compared are used in the same concentration (based on active protein). The use of the respective protease for the same level of activity ensures that the respective enzymatic properties, e.g. the cleaning performance on certain soiling, are compared even if there is a gap in the ratio of active substance to total protein (the values of the specific activity). In general, a low specific activity can be compensated for by adding a larger amount of protein. Furthermore, the enzymes to be examined can also be used in the same amount of substance or amount by weight if the enzymes to be examined have a different affinity for the test substrate in an activity test. The expression “same amount of substance” in this context refers to a molar use of the enzymes to be examined. The expression “equal weight” refers to the use of the same weight of the enzymes to be examined.

The cleaning performance of the protease against blood staining is determined by measuring the degree of whiteness of the washed textiles. The washing process takes place for 70 minutes at a temperature of 40 ° C, the water having a water hardness between 13.5 and 16.5 ° (German hardness).

The concentration of the protease in the detergent intended for this washing system is 0.0001 to 0.1% by weight, preferably 0.0005 to 0.05% by weight and particularly preferably 0.001 to 0.02% by weight, based on on active protein.

A preferred liquid detergent for such a washing system is composed as follows (all data in percent by weight): 0.3-0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerin, 0 , 3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 5-15% nonionic surfactants, 5-15% anionic surfactants (LAS), 1% boric acid, 1-4% sodium citrate (dihydrate), 2- 4% soda, 2-6% coconut fatty acids, 0.5-2.5% HEDP (1-hydroxyethane (1,1-di-phosphonic acid)), 0-0.4% PVP (polyvinylpyrrolidone), 0- 0.15% optical brightener, 0-0.001% dye, the remainder demineralized water. The dosage of the liquid detergent is preferably between 3.5 and 6.0 grams per liter of wash liquor, e.g. 4.7, 4.9 or 5.9 grams per liter of wash liquor or about 55 g / job.

A preferred powder detergent for such a washing system is composed as follows (all data in percent by weight): 10-15% linear alkylbenzenesulfonate (sodium salt), 0-1.5% C ₁₂ -C ₁₈ fatty alcohol sulfate (sodium salt ), 2-5% C ₁₂ -C ₁₈ fatty alcohol with 7 EO, 0-2% soaps, 5-20% sodium carbonate, 4-10% amorphous sodium disilicate, 0.5-2% phosphonate (e.g. HEDP-Na4), 1-4% polyacrylate, 1-2% carboxymethyl cellulose, remainder: sodium sulfate, foam inhibitors, optical brighteners, fragrances, etc. The dosage of the powder detergent is preferably between 4.5 and 7.0 grams per liter of washing liquor, e.g. and particularly preferably 4 , 7 grams per liter of wash liquor, or 5.5, 5.9 or 6.7 grams per liter of wash liquor or about 65 g / job.

The degree of whiteness, i.e. the lightening of the soiling, as a measure of the cleaning performance, is preferably determined using optical measuring methods, preferably photometrically. A suitable device for this is e.g. the Minolta CM508d spectrometer. The devices used for the measurement are usually calibrated beforehand with a white standard, preferably a supplied white standard.

According to the invention, a detergent is to be understood as meaning all conceivable types of detergent, both concentrates and agents to be used undiluted, for use on a commercial scale, in the washing machine or for hand washing or cleaning. These include, for example, detergents for textiles, carpets or natural fibers, for which the term detergent is used. The detergents within the scope of the invention also include washing auxiliaries which are added to the actual detergent in manual or machine washing in order to achieve a further effect. Furthermore, detergents in the context of the invention also include textile pretreatment and aftertreatment agents, i.e. agents with which the item of laundry is brought into contact before the actual washing, e.g. to loosen stubborn dirt, and also agents that are used in a step following the actual textile washing give the laundry other desirable properties such as a pleasant grip, crease resistance or low static charge. The last-mentioned agents include fabric softeners.

The detergents according to the invention, which can be present as powdery or granular solids, in compacted or re-compacted particle form, as homogeneous solutions or suspensions, can contain, in addition to a protease according to the invention, all known ingredients common in such agents, with at least one further ingredient preferably being present in the agent is. The detergents according to the invention can contain, in particular, surfactants, builders, polymers, glass corrosion inhibitors, corrosion inhibitors, bleaching agents such as peroxygen compounds, bleach activators or bleach catalysts. They can also contain water-miscible organic solvents, other enzymes, enzyme stabilizers, sequestering agents, electrolytes, pH regulators and / or other auxiliaries such as optical brighteners, graying inhibitors, color transfer inhibitors, foam regulators, and dyes and fragrances and combinations thereof.

In particular, anionic surfactants, nonionic surfactants and mixtures thereof come into consideration.

The agents according to the invention can contain one or more surfactants, in particular anionic surfactants, nonionic surfactants and mixtures thereof, but also cationic, zwitterionic and / or amphoteric surfactants can be included. The agents preferably contain 5 to 70% by weight of surfactant, more preferably 5 to 55% by weight and more preferably 5 to 35% by weight of surfactant.

Suitable anionic surfactants are in particular soaps and those which contain sulfate or sulfonate groups with preferably alkali ions as cations. Preferred soaps are the alkali metal salts of saturated or unsaturated C _12-18 fatty acids. Such fatty acids can also be used in a form that is not completely neutralized. Suitable surfactants of the sulfate type are the salts of Schwefelsäurehalbester of C include _12-18 fatty alcohols and the sulfation of said nonionic surfactants with a low degree of ethoxylation. Suitable surfactants of the sulfonate type include, for example, C _9-14 alkyl benzene sulfonates, alkane sulfonates, from C _12-18 alkanes such as are obtained by sulfochlorination or sulfoxidation and subsequent hydrolysis or neutralization, C _12-18 olefin sulphonates, which in the reaction of corresponding monoolefins with sulfur trioxide are formed, mixtures of alkene and hydroxyalkane sulfonates, disulfonates obtained, for example, from C ₁₂ - ₁₈ receives monoolefins with terminal or internal double bond by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acidic hydrolysis of the sulfonation and α-sulfo fatty acid esters (ester sulfonates), which are formed during the sulfonation of fatty acid methyl or ethyl esters, for example α-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids. The agent preferably has 5 to 55% by weight, preferably 5 to 35% by weight, of anionic surfactant. The agent very preferably has 5 to 35% by weight of alkylbenzenesulfonate. In addition, the agent can preferably contain further anionic surfactants, in particular alkyl ether sulfates, and nonionic surfactants, in particular fatty alcohol alkoxylates. These can then make up the rest of the surfactants.

in der R' und R'' unabhängig H oder Alkyl sind und zusammen 6 bis 19, vorzugsweise 7 bis 15 und insbesondere 9 bis 13 C-Atome enthalten. Ein ganz besonders bevorzugter Vertreter ist Natriumdodecylbenzylsulfonat.Suitable alkylbenzenesulfonates are preferably selected from linear or branched alkylbenzenesulfonates of the formula

in which R 'and R''are independently H or alkyl and together contain 6 to 19, preferably 7 to 15 and in particular 9 to 13 carbon atoms. A very particularly preferred representative is sodium dodecylbenzyl sulfonate.

Alk (en) yl sulfates are the alkali and especially the sodium salts of Schwefelsäurehalbester of C _12-18 fatty alcohols, for example coconut oil fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol, or C ₁₀ - ₂₀ -oxo alcohols and those Semi-esters of secondary alcohols of these chain lengths are preferred. Also preferred are alk (en) yl sulfates of the chain length mentioned which contain a synthetic, straight-chain alkyl radical produced on a petrochemical basis and which have a degradation behavior similar to that of the appropriate compounds based on oleochemical raw materials. From the washing are the C _12-16 alkyl sulfates and C _12-15 alkyl sulfates and C ₁₄ - ₁₅ alkyl sulfates of preferably.

Also, the Schwefelsäuremonoester the ethoxylated with 1 to 6 moles of ethylene oxide chain or branched C _7-21 alcohols, such as 2-methyl-branched C _9-11 alcohols containing on average 3.5 mol ethylene oxide (EO) or _C12 - ₁₈ - Fatty alcohols with 1 to 4 EO are suitable. Suitable alkyl ether sulfates are, for example, compounds of the formula R ¹ -O- (AO) _n -SO ₃ ^- X ⁺ . In this formula, R ^{1 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 ¹ are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, the representatives with an even number of C- Atoms are preferred. Particularly preferred radicals R ¹ are derived from C _12-18 fatty alcohols, for example, from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol, or C ₁₀ - ₂₀ -oxo alcohols. AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably for an ethylene oxide group. The index n stands for an integer from 1 to 50, preferably from 1 to 20 and 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, including Na ⁺ or K ⁺ , 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.

mit k = 11 bis 19, n = 2, 3, 4, 5, 6, 7 oder 8. Ganz besonders bevorzugte Vertreter sind Na-C₁₂-₁₄-Fettalkoholethersulfate mit 2 EO (k = 11-13, n = 2). Der angegebenen Ethoxylierungsgrad stellt einen statistischen Mittelwert dar, der für ein spezielles Produkt eine ganze oder eine gebrochene Zahl sein kann. Die angegebenen Alkoxylierungsgrade stellen statistische Mittelwerte dar, die für ein spezielles Produkt eine ganze oder eine gebrochene Zahl sein können. Bevorzugte Alkoxylate/Ethoxylate weisen eine eingeengte Homologenverteilung auf (narrow range ethoxylates, NRE).In various embodiments, the alkyl ether sulfate can be selected from fatty alcohol ether sulfates of the formula

with k = 11 to 19, n = 2, 3, 4, 5, 6, 7 or 8. Very particularly preferred representatives are sodium C _12-14 fatty alcohol ether sulfates with 2 EO (k = 11-13, n = 2) . The stated degree of ethoxylation represents a statistical mean value, which for a specific product can be an integer or a fraction. The stated degrees of alkoxylation represent statistical mean values which, for a specific product, can be an integer or a fraction. Preferred alkoxylates / ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE).

It has proven to be advantageous for cold washing performance if the detergents also contain soap (s). Preferred detergents are therefore characterized in that they contain soap (s). Saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid and behenic acid and, in particular, soap mixtures derived from natural fatty acids, e.g. coconut, palm kernel or tallow fatty acids, are suitable.

Suitable nonionic surfactants are in particular alkyl glycosides and ethoxylation and / or propoxylation products of alkyl glycosides or linear or branched alcohols each with 8 to about 18 carbon atoms in the alkyl part and 3 to 20, preferably 4 to 10, alkyl ether groups. Corresponding ethoxylation and / or propoxylation products of N-alkylamines, vicinal diols, fatty acid esters and fatty acid amides, which correspond to the long-chain alcohol derivatives mentioned in terms of the alkyl part, and of alkylphenols with 5 to 12 carbon atoms in the alkyl radical can also be used.

The nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, in particular primary alcohols with preferably 8 to 18 carbon atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol, in which the alcohol radical can be linear or preferably methyl-branched in the 2-position or may contain linear and methyl-branched radicals in the mixture, as they are usually present in oxo alcohol radicals. In particular, however, alcohol ethoxylates with linear residues of alcohols of native origin with 12 to 18 carbon atoms, for example from coconut, palm, tallow or oleyl alcohol, and average 2 to 8 EO per mole of alcohol are preferred. Preferred ethoxylated alcohols include, for example, C _12-14 alcohols with 3 EO or 4 EO, C _9-11 alcohol with 7 EO, C _13-15 alcohols containing 3 EO, 5 EO, 7 EO or 8 EO, C _12-18 alcohols containing 3 EO, 5 EO or 7 EO and mixtures thereof, such as mixtures of C _12-14 alcohol with 3 EO and C _12-18 alcohol with 5 EO. The stated degrees of ethoxylation represent statistical mean values which, for a specific product, can be an integer or a fraction. Preferred alcohol ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples are tallow fatty alcohol with 14 EO, 25 EO, 30 EO or 40 EO.

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

Another class of nonionic surfactants that can be used advantageously are the alkyl polyglycosides (APG). Usable alkyl polyglycosides satisfy the general formula RO (G) z, in which R stands for a linear or branched, in particular in the 2-position methyl branched, saturated or unsaturated, aliphatic radical with 8 to 22, preferably 12 to 18 carbon atoms and G denotes Is a symbol that stands for a glycose unit with 5 or 6 carbon atoms, preferably for glucose. The degree of glycosidation z is between 1.0 and 4.0, preferably between 1.0 and 2.0 and in particular between 1.1 and 1.4. Linear alkyl polyglycosides, that is to say alkyl polyglycosides in which the polyglycosyl radical is a glucose radical and the alkyl radical is an n-alkyl radical, are preferably used.

Nonionic surfactants of the amine oxide type, for example N-cocoalkyl-N, N-dimethylamine oxide and N-tallowalkyl-N, N-dihydroxyethylamine oxide, and the fatty acid alkanolamides can also be suitable.

The amount of these nonionic surfactants is preferably not more than that of the ethoxylated fatty alcohols, in particular not more than half that.

Further nonionic surfactants that can be used in the detergents according to the invention have the formula R ¹ -CH (OH) CH ₂ O- (AO) _w - (A'O) _x - (A "O) _y - (A"'O) _z -R ^2, where R ¹ is a straight-chain or branched, saturated or mono- or polyunsaturated C _6-24 alkyl or alkenyl radical; R ^{2 represents} a linear or branched hydrocarbon radical having 2 to 26 carbon atoms; A, A ', A''andA''' independently of one another for a radical from the group -CH ₂ CH ₂ , -CH ₂ CH ₂ -CH ₂ , - CH ₂ -CH (CH ₃ ), -CH ₂ - CH ₂ -CH ₂ -CH ₂ , -CH ₂ -CH (CH ₃ ) -CH ₂ -, -CH ₂ -CH (CH ₂ -CH ₃ ); w, x, y and z stand for values between 0.5 and 120, where x, y and / or z can also be 0, are preferred.

By adding the aforementioned nonionic surfactants of the formula R ¹ -CH (OH) CH ₂ O- (AO) _w - (A'O) _x - (A "O) _y - (A"'O) _z -R ² , hereinafter also referred to as “hydroxy mixed ethers”, the cleaning performance of enzyme-containing preparations according to the invention can be significantly improved, both in comparison to surfactant-free systems and in comparison to systems that contain alternative nonionic surfactants, eg from the group of polyalkoxylated fatty alcohols.

By using these nonionic surfactants with one or more free hydroxyl group (s) on one or both terminal alkyl radicals, the stability of the enzymes contained in the detergent preparations according to the invention can be significantly improved.

Particularly preferred are those end-capped poly (oxyalkylated) nonionic surfactants which, according to the formula R ¹ O [CH ₂ CH ₂ O] _x CH ₂ CH (OH) R ² , in addition to a radical R ¹ , which stands for linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals with 2 to 30 carbon atoms, preferably with 4 to 22 carbon atoms, furthermore a linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radical R ² with 1 to 30 carbon atoms, where x for values between 1 and 90, preferably for values between 30 and 80 and in particular for values between 30 and 60.

Surfactants of the formula R ¹ O [CH ₂ CH (CH ₃ ) O] _x [CH ₂ CH ₂ O] _y CH ₂ CH (OH) R ² , in which R ^{1 represents} a linear or branched aliphatic hydrocarbon radical with 4, are particularly preferred up to 18 carbon atoms or mixtures thereof, R ² denotes a linear or branched hydrocarbon radical having 2 to 26 carbon atoms or mixtures thereof, and x for values between 0.5 and 1.5 and y for a value of at least 15 stands. The group of these non-ionic surfactants include, for example, the C _2-26 fatty alcohol (PO) ₁ - (EO) _15-40 2-hydroxyalkyl ethers, in particular the C _8-10 fatty alcohol (PO) ₁ - (EO) ₂₂ -2 hydroxydecyl ether.

Also particularly preferred are those end group-capped poly (oxyalkylated) nonionic surfactants of the formula R ¹ O [CH ₂ CH ₂ O] _x [CH ₂ CH (R ³ ) O] _y CH ₂ CH (OH) R ² , in which R ¹ and R ^{2 2} independently of one another represents a linear or branched, saturated or mono- or polyunsaturated hydrocarbon radical having 2 to 26 carbon atoms, R ^{3 is} independently selected from -CH ₃ , -CH ₂ CH ₃ , -CH ₂ CH ₂ -CH ₃ , -CH (CH ₃ ) ₂ , but preferably represents -CH ₃ , and x and y independently of one another represent values between 1 and 32, nonionic surfactants with R ³ = —CH ₃ and values for x from 15 to 32 and y of 0.5 and 1.5 are particularly preferred.

Further nonionic surfactants that can be used with preference are the end group-capped poly (oxyalkylated) nonionic surfactants of the formula R ¹ O [CH ₂ CH (R ³ ) O] _x [CH ₂ ] _k [CH (OH) [CH ₂ ] _j OR ² , in which R ¹ and R ² stand for linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals with 1 to 30 carbon atoms, R ^{3 stands} for H or a methyl, ethyl, n-propyl, iso-propyl, n-butyl, 2 -Butyl or 2-methyl-2-butyl radical, x stands for values between 1 and 30, k and j for values between 1 and 12, preferably between 1 and 5. If the value x ≥ 2, each R ³ in the above formula R ¹ O [CH ₂ CH (R ³ ) O] _x [CH ₂ ] _k CH (OH) [CH ₂ ] _j OR ² can be different. R ¹ and R ² are preferably linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 6 to 22 carbon atoms, radicals having 8 to 18 carbon atoms being particularly preferred. For the radical R ³ , H, —CH ₃ or —CH ₂ CH _{3 are} particularly preferred. Particularly preferred values for x are in the range from 1 to 20, in particular from 6 to 15.

As described above, each R ³ in the above formula may be different if x 2. This allows the alkylene oxide unit in the square brackets to be varied. If x is, for example, 3, the radical R ³ can be selected to form ethylene oxide (R ³ = H) or propylene oxide (R ³ = CH ₃ ) units, which can be joined together in any order, e.g. (EO) ( PO) (EO), (EO) (EO) (PO), (EO) (EO) (EO), (PO) (EO) (PO), (PO) (PO) (EO) and (PO) ( PO) (PO). The value 3 for x has been chosen as an example and can be larger, the range of variation increasing with increasing x values and including, for example, a large number of (EO) groups combined with a small number of (PO) groups, or vice versa .

Particularly preferred end-capped poly (oxyalkylated) alcohols of the above formula have values of k = 1 and j = 1, so that the above formula becomes R ¹ O [CH ₂ CH (R ³ ) O] _x CH ₂ CH (OH ) CH ₂ OR ² simplified. In the last-mentioned formula, R ¹ , R ² and R ^{3 are} as defined above and x stands for numbers from 1 to 30, preferably from 1 to 20 and in particular from 6 to 18. Surfactants in which the radicals R ¹ and R ^{2 have} 9 to 14 carbon atoms, R ^{3 represents} H and x assumes values of 6 to 15.

Finally, the nonionic surfactants of the formula R ¹ -CH (OH) CH ₂ O- (AO) _w -R ² , in which R ^{1 stands} for a straight-chain or branched, saturated or mono- or polyunsaturated C, have proven to be particularly effective _6-24 alkyl or alkenyl radical; R ^{2 represents} a linear or branched hydrocarbon radical having 2 to 26 carbon atoms; A represents a radical from the group CH ₂ CH ₂ , —CH ₂ CH ₂ —CH ₂ , —CH ₂ —CH (CH ₃ ), and w represents values between 1 and 120, preferably 10 to 80, in particular 20 to 40 stands. The group of these non-ionic surfactants include, for example, the C _4-22 fatty alcohol (EO) _10-80 2-hydroxyalkyl ethers, in particular the C _8-12 fatty alcohol (EO) ₂₂ -2-hydroxydecylether and the C _4-22 fatty alcohol (EO) ₄₀ - ₈₀ 2-hydroxyalkyl ether.

Preferred detergents are characterized in that the detergent contains at least one nonionic surfactant, preferably a nonionic surfactant from the group of hydroxy mixed ethers, the proportion by weight of the nonionic surfactant in the total weight of the detergent preferably 0.2 to 10% by weight, preferably 0. 4 to 7.0 wt%, and more preferably 0.6 to 6.0 wt%.

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 with 8 to 25, preferably 10 to 21 carbon atoms, optionally interrupted by heteroatoms or heteroatom groups R ^iv and R ^v are identical or different alkyl radicals having 1 to 3 carbon atoms, in particular C ₁₀ -C ₁₈ alkyl and C dimethylcarboxymethylbetain _11-17 -Alkylamidopropyl-dimethylcarboxymethylbetain.

Suitable cationic surfactants include the quaternary ammonium compounds of the formula (R ^vi ) (R ^vii ) (R ^viii ) (R ^ix ) N ⁺ X ^- , in which Rvi to R ^{ix represent} four identical or different types, in particular two long and two short-chain, alkyl radicals and X ^- stand for an anion, in particular a halide ion, for example didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride 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. By using quaternary surface-active compounds with an antimicrobial effect, the agent can be designed with an antimicrobial effect or its antimicrobial effect, which may already be present due to other ingredients, can be improved.

Another preferred component of detergents according to the invention are complexing agents. Particularly preferred complexing agents are the phosphonates, provided that their use is permitted by regulations. In addition to 1-hydroxyethane-1,1-diphosphonic acid, the complex-forming phosphonates include a number of different compounds such as diethylenetriaminepenta (methylenephosphonic acid) (DTPMP). Hydroxyalkane or aminoalkane phosphonates are particularly preferred in this application. Among the hydroxyalkanephosphonates, 1-hydroxyethane-1,1-diphosphonate (HEDP) is of particular importance as a cobuilder. It is preferably used as the sodium salt, the disodium salt reacting neutrally and the tetrasodium salt reacting alkaline (pH 9). Ethylenediamine tetramethylene phosphonate (EDTMP), diethylenetriamine pentamethylene phosphonate (DTPMP) and their higher homologues are preferred as aminoalkanephosphonates. They are preferably used in the form of the neutrally reacting sodium salts, e.g. as the hexasodium salt of EDTMP or as the hepta- and octasodium salt of DTPMP. From the class of the phosphonates, HEDP is preferably used as the builder. The aminoalkanephosphonates also have a pronounced ability to bind heavy metals. Accordingly, especially if the agents also contain bleach, it can be preferred to use aminoalkanephosphonates, in particular DTPMP, or mixtures of the phosphonates mentioned.

A detergent preferred in the context of this application contains one or more phosphonate (s) from the aminotrimethylene phosphonic acid (ATMP) group and / or their salts; Ethylenediaminetetra (methylenephosphonic acid) (EDTMP) and / or salts thereof; Diethylenetriaminepenta (methylenephosphonic acid) (DTPMP) and / or salts thereof; 1-hydroxyethane-1,1-diphosphonic acid (HEDP) and / or its salts; 2-phosphonobutane-1,2,4-tricarboxylic acid (PBTC) and / or its salts; Hexamethylenediaminetetra (methylenephosphonic acid) (HDTMP) and / or salts thereof; Nitrilotri (methylenephosphonic acid) (NTMP) and / or their salts.

Detergents which contain 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or diethylenetriaminepenta (methylenephosphonic acid) (DTPMP) as phosphonates are particularly preferred. The detergents according to the invention can of course contain two or more different phosphonates. Preferred detergents according to the invention are characterized in that the detergent contains at least one complexing agent from the group of phosphonates, preferably 1-hydroxyethane-1,1-diphosphonate, the proportion by weight of phosphonate in the total weight of the detergent preferably 0.1 and 8.0 wt .-%, preferably 0.2 and 5.0% by weight and more preferably 0.5 and 3.0% by weight.

The detergents according to the invention also preferably contain builder, preferably at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The builders include in particular the silicates, carbonates and organic cobuilders.

Organic cobuilders that may be mentioned are, in particular, polycarboxylates / polycarboxylic acids, polymeric polycarboxylates, aspartic acid, polyacetals, dextrins, other organic cobuilders and phosphonates. These substance classes are described below. Organic cobuilders can, if desired, be present in amounts of up to 40% by weight, in particular up to 25% by weight and preferably from 1 to 8% by weight.

Organic builder substances which can be used are, for example, the polycarboxylic acids which can be used in the form of the free acid and / or its sodium salts, polycarboxylic acids being understood as meaning those carboxylic acids which carry more than one acid function. For example, these are citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids and carboxymethylinulins, monomeric and polymeric aminopolycarboxylic acids, in particular glycinediacetic acid, methylglycinediacetic acid, glutaminediacetic acid, iminodiacetic-diacetic acid, glutaminediacetic acid, nitrilotriacetic acid, nitrilotisiacetic acid, such as nitilotiso-di-acetic acid (nitrilotriacetic acid) and Hydroxyiminodisuccinate, ethylenediaminetetraacetic acid and polyaspartic acid, polyphosphonic acids, in particular aminotris (methylenephosphonic acid), ethylenediamine tetrakis (methylenephosphonic acid), lysine tetra (methylenephosphonic acid) and 1-hydroxyethane-1,1-diphosphonic acids, such as oxyethane-1,1-diphosphonic acids, such as poly (tri-xyrenic) carboxylic acids, such as hydroxylic acid, in particular hydroxylic acid, such as hydroxyethane-1,1-diphosphonic acids, such as hydroxyethane-1,1-diphosphonic acids, such as poly (tri-xyrenic) carboxylic acids Polysaccharides or dextrins accessible polycarboxylates, and / or polymeric acrylic acids, methacrylic acids, Maleic acids and copolymers of these, which can also contain small amounts of polymerizable substances without carboxylic acid functionality in polymerized form. Such organic builder substances can, if desired, be present in amounts of up to 50% by weight, in particular up to 25% by weight and preferably from 10 to 20% by weight.

In addition to their builder effect, the free acids typically also have the property of an acidifying component and thus also serve to set a lower and milder pH value for detergents. Citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid and any mixtures of these should be mentioned in particular. Citric acid or salts of citric acid are used with particular preference as the structural substance. Further particularly preferred builder substances are selected from methylglycinediessidic acid (MGDA), glutamic acid diacetate (GLDA), aspartic acid diacetate (ASDA), hydroxyethyliminodiacetate (HEIDA), iminodisuccinate (IDS) and ethylenediamine disuccinate (EDDS), carboxymethyl inulin and polyaspartate inulin.

In preferred embodiments, citric acid and / or citrate is used as the water-soluble, organic builder. The use of 5 to 25% by weight, preferably 7.5 to 12.5% by weight of citric acid and / or 5 to 25% by weight, preferably 7.5 to 12.5% by weight, is particularly preferred Citrate, preferably alkali citrate, more preferably sodium citrate. Citric acid / citrate can each be used in the form of their hydrates, e.g. citric acid can be used in the form of the monohydrate and citrate in the form of the trisodium citrate dihydrate.

Polymeric polycarboxylates are also suitable as builders, for example the alkali metal salts of polyacrylic acid or polymethacrylic acid, for example those with a relative molecular weight of 500 to 70,000 g / mol. For the purposes of this application, the molar masses specified for polymeric polycarboxylates are weight-average molar masses M _{w of} the respective acid form, which were determined in principle by means of gel permeation chromatography (GPC) using a UV detector. The measurement was carried out against an external polyacrylic acid standard, which, due to its structural similarity to the polymers under investigation, provides realistic molecular weight values. This information deviates significantly from the molecular weight information in which polystyrene sulfonic acids are used as the standard. The molar masses measured against polystyrene sulfonic acids are generally significantly higher than the molar masses given in this application.

Suitable polymers are in particular polyacrylates, which preferably have a molecular weight of 2,000 to 20,000 g / mol. Because of their superior solubility, the short-chain polyacrylates from this group, which have molecular weights from 2,000 to 10,000 g / mol, and particularly preferably from 3,000 to 5,000 g / mol, can be preferred.

Also suitable are copolymeric polycarboxylates, in particular those of acrylic acid with methacrylic acid and acrylic acid or methacrylic acid with maleic acid. Copolymers of acrylic acid with maleic acid which contain 50 to 90% by weight of acrylic acid and 50 to 10% by weight of maleic acid have proven particularly suitable. Their relative molecular weight, based on free acids, is generally 2,000 to 70,000 g / mol, preferably 20,000 to 50,000 g / mol and in particular 30,000 to 40,000 g / mol.

A solid agent according to the invention preferably contains at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The organic builder substances mentioned above belong to the water-soluble organic builder substances.

In addition to the abovementioned water-soluble organic builders, the compositions of the invention can furthermore also contain inorganic water-soluble builders. Particularly suitable water-soluble inorganic builder materials are alkali silicates, alkali carbonates, alkali hydrogen carbonates, alkali phosphates and / or sesquicarbonates, which can be in the form of their alkaline, neutral or acidic sodium or potassium salts. If necessary, solid laundry detergents can also contain small amounts of calcium carbonates. For example, water-soluble crystalline and / or amorphous alkali silicates are suitable. The alkali silicates which can be used as builders in the agents according to the invention preferably have a molar ratio of alkali oxide to SiO ₂ below 0.95, in particular from 1: 1.1 to 1:12, and can be amorphous or crystalline. Preferred alkali silicates are the sodium silicates, in particular the amorphous sodium silicates, with a molar ratio Na ₂ O: SiO ₂ of 1: 2 to 1: 2.8. The crystalline silicates used alone or in a mixture with amorphous silicates are preferably crystalline sheet silicates of the general formula Na ₂ Si _x O _{2x + 1} y H ₂ O, in which x, the so-called module, is a number of 1.9 to 22, in particular 1.9 to 4 and y is a number from 0 to 33 and preferred values for x are 2, 3 or 4. Preferred crystalline sheet silicates are those in which x in the general formula mentioned assumes the values 2 or 3. Both ß- and δ-sodium disilicates (Na ₂ Si ₂ O ₅ · y H ₂ O) are particularly preferred. Virtually anhydrous crystalline alkali silicates of the above general formula, in which x is a number from 1.9 to 2.1, which are produced from amorphous alkali metal silicates, can also be used in agents according to the invention. In a further embodiment of agents according to the invention, a crystalline layered sodium silicate with a module of 2 to 3 is used, 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 embodiment of agents according to the invention. In agents which contain both amorphous and crystalline alkali silicates, the weight ratio of amorphous alkali silicate to crystalline alkali silicate is preferably 1: 2 to 2: 1 and in particular 1: 1 to 2: 1. Crystalline layered silicates of the formula (I) given above are sold by Clariant GmbH under the trade name Na-SKS, e.g. Na-SKS-1 (Na ₂ Si ₂₂ O ₄₅ · xH ₂ O, Kenyaite), Na-SKS- 2 (Na ₂ Si ₁₄ O ₂₉ · xH ₂ O, magadiite), Na-SKS-3 (Na ₂ Si ₈ O ₁₇ · xH ₂ O) or Na-SKS-4 (Na ₂ Si ₄ O ₉ · xH ₂ O , Makatite). Of these, Na-SKS-5 (α-Na ₂ Si ₂ O ₅ ), Na-SKS-7 (ß-Na ₂ Si ₂ O ₅ , Natrosilit), Na-SKS-9 (NaHSi ₂ O ₅ 3H ₂ O), Na-SKS-10 (NaHSi ₂ O ₅ · 3H ₂ O, Kanemite), Na-SKS-11 (t-Na ₂ Si ₂ O ₅ ) and Na-SKS-13 (NaHSi ₂ O ₅ ) , but especially Na-SKS-6 (δ-Na ₂ Si ₂ O ₅ ). In one embodiment of the agents according to the invention, a granular compound of crystalline sheet silicate and citrate, of crystalline sheet silicate and the above-mentioned (co) polymeric polycarboxylic acid, or of alkali silicate and alkali carbonate, such as is commercially available under the name Nabion® 15, is used. Such water-soluble inorganic builder materials are contained in the agents according to the invention preferably in amounts of 1 to 20% by weight, in particular 5 to 15% by weight.

Furthermore, the carbonates (and hydrogen carbonates), in particular sodium carbonate, and the phosphonic acids / phosphonates are also of importance as water-soluble inorganic builder substances. Phosphonic acids are also understood to mean optionally substituted alkylphosphonic acids, which can also have several phosphonic acid groups (so-called polyphosphonic acids). They are preferably selected from the hydroxy and / or aminoalkylphosphonic acids and / or their alkali salts, such as dimethylaminomethanediphosphonic acid, 3-aminopropane-1-hydroxy-1,1-diphosphonic acid, 1-amino-1-phenyl-methanediphosphonic acid, 1-hydroxyethane 1,1-diphosphonic acid (HEDP), aminotris (methylenephosphonic acid), N, N, N ', N'-ethylenediamine tetrakis (methylenephosphonic acid), diethylenetriaminepenta (methylenephosphonic acid) (DTPMP) and acylated derivatives of phosphorous acid, which can also be used in any mixtures can.

1. a) 0 bis 10 Gew.-%, vorzugsweise 1 bis 5 Gew.-% Citronensäure;
2. b) 0 bis 10 Gew.-%, vorzugsweise 1 bis 5 Gew.-% Citrat, vorzugsweise Alkalicitrat;
3. c) 0 bis 40 Gew.-%, vorzugsweise 0 bis 15 Gew.-% Alkalicarbonat, welches auch zumindest anteilig durch Alkalihydrogencarbonat ersetzt sein kann, insbesondere Natriumcarbonat;
4. d) 0 bis 20 Gew.-%, vorzugsweise 3 bis 10 Gew.-% Alkalisilikat;
5. e) 0,005 bis 10 Gew.-%, vorzugsweise 0,02 bis 2 Gew.-% Phosphonsäure und/oder Alkaliphosphonat, insbesondere HEDP und/oder DTPMP; und
6. f) 0 bis 10 Gew.-%, vorzugsweise 0,5 bis 3 Gew.-% polymeres Polycarboxylat, insbesondere Polyacrylat.

In various embodiments, the builder system is preferably composed of the components, each based on the total mass of the agent:

1. a) 0 to 10% by weight, preferably 1 to 5% by weight of citric acid;
2. b) 0 to 10 wt .-%, preferably 1 to 5 wt .-% citrate, preferably alkali citrate;
3. c) 0 to 40% by weight, preferably 0 to 15% by weight, alkali metal carbonate, which can also be at least partly replaced by alkali metal hydrogen carbonate, in particular sodium carbonate;
4. d) 0 to 20% by weight, preferably 3 to 10% by weight, alkali metal silicate;
5. e) 0.005 to 10% by weight, preferably 0.02 to 2% by weight of phosphonic acid and / or alkali metal phosphonate, in particular HEDP and / or DTPMP; and
6. f) 0 to 10% by weight, preferably 0.5 to 3% by weight, polymeric polycarboxylate, in particular polyacrylate.

With regard to component f), e.g. the alkali metal salts of polyacrylic acid or polymethacrylic acid, e.g. those with a relative molecular weight of 500 to 70,000 g / mol, are suitable. This class of substances has already been described in detail above. The (co) polymeric polycarboxylates can be used either as a powder or as an aqueous solution.

The agents according to the invention are preferably free from phosphate builder, i.e. contain less than 1% by weight, preferably no deliberately added phosphate builder.

The agents can also contain water-insoluble builder substances. As water-insoluble inorganic builder materials, in particular crystalline or amorphous water-dispersible alkali alumosilicates, in amounts of up to 50% by weight, preferably not more than 40% by weight, in particular from 3 to 20% by weight and particularly preferably from 1 to 15% by weight, are used. -%, used. Among these are the crystalline sodium aluminosilicates in detergent quality, in particular zeolite A, zeolite P, zeolite MAP and optionally zeolite X, alone or in mixtures, e.g. in the form of a co-crystallizate of the zeolites A and X (Vegobond® AX, a commercial product from Condea Augusta SpA) is preferred. Quantities close to the upper limit mentioned are preferably used in solid, particulate compositions. Suitable aluminosilicates in particular have no particles with a particle size greater than 30 μm and preferably consist of at least 80% by weight of particles with a size less than 10 μm. Your calcium binding capacity, according to DE2412837 can be determined is usually in the range of 100 to 200 mg CaO per gram.

In addition to the builders described above, the detergent can contain active cleaning polymers. The proportion by weight of active cleaning polymers in the total weight of detergents according to the invention is preferably 0.1 to 20% by weight, preferably 1.0 to 15% by weight and more preferably 2.0 to 12% by weight.

Polymers containing sulfonic acid groups, in particular from the group of copolymeric polysulfonates, are preferably used as cleaning-active polymers. In addition to monomer (s) containing sulfonic acid groups, these copolymeric polysulfonates contain at least one monomer from the group of unsaturated carboxylic acids.

The unsaturated carboxylic acid (s) used is / are with particular preference unsaturated carboxylic acids of the formula R ¹ (R ² ) C =C (R ³ ) COOH, in which R ¹ to R ³ independently of one another represent -H, -CH ₃ , a straight-chain or branched saturated alkyl radical with 2 to 12 carbon atoms, a straight-chain or branched, mono- or polyunsaturated alkenyl radical with 2 to 12 carbon atoms, alkyl or alkenyl radicals substituted with -NH ₂ , -OH or -COOH as defined above or for -COOH or -COOR ⁴ , where R ^{4 is} a saturated or unsaturated, straight-chain or branched hydrocarbon radical having 1 to 12 carbon atoms. Particularly preferred unsaturated carboxylic acids are acrylic acid, methacrylic acid, ethacrylic acid, α-chloroacrylic acid, α-cyanoacrylic acid, crotonic acid, α-phenyl acrylic acid, maleic acid, maleic anhydride, fumaric acid, itaconic acid, citraconic acid, methylenemalonic acid, sorbic acid, cinnamic acid or mixtures thereof. The unsaturated dicarboxylic acids can of course also be used.

In the case of monomers containing sulfonic acid groups, preference is given to those of the formula R ⁵ (R ⁶ ) C =C (R ⁷ ) -X-SO ₃ H, in which R ⁵ to R ^7, independently of one another, represent -H, -CH ₃ , a straight-chain or branched, saturated alkyl radical with 2 to 12 carbon atoms, a straight-chain or branched, mono- or polyunsaturated alkenyl radical with 2 to 12 carbon atoms, alkyl or alkenyl radicals substituted with -NH ₂ , -OH or -COOH or for -COOH or -COOR ⁴ R ^{4 is} a saturated or unsaturated, straight-chain or branched hydrocarbon radical having 1 to 12 carbon atoms, and X is an optionally present spacer group which is selected from - (CH ₂ ) _n - with n = 0 to 4, -COO - (CH ₂ ) _k - with k = 1 to 6, -C (O) -NH-C (CH ₃ ) ₂ -, -C (O) -NH-C (CH ₃ ) ₂ -CH ₂ - and - C (O) -NH-CH (CH ₂ CH ₃₎ -.

Preferred among these monomers are those of the formulas H ₂ C = CH-X-SO ₃ H, H ₂ C = C (CH ₃ ) -X-SO ₃ H and HO ₃ SX- (R ⁶ ) C = C (R ⁷ ) -X-SO ₃ H, in which R ⁶ and R ^{7 are} independently selected from -H, -CH ₃ , -CH ₂ CH ₃ , -CH ₂ CH ₂ CH ₃ , -CH (CH ₃ ) ₂ and X stands for an optionally present spacer group which is selected from - (CH ₂ ) _n - with n = 0 to 4, -COO- (CH ₂ ) _k - with k = 1 to 6, -C (O) -NH-C (CH ₃ ) ₂ -, - C (O) -NH-C (CH ₃ ) ₂ -CH ₂ - and -C (O) -NH-CH (CH ₂ CH ₃ ) -.

Particularly preferred monomers containing sulfonic acid groups are 1-acrylamido-1-propanesulfonic acid, 2-acrylamido-2-propanesulfonic acid, 2-acrylamido-2-methyl-1-propanesulfonic acid, 2-methacrylamido-2-methyl-1-propanesulfonic acid, 3- Methacrylamido-2-hydroxy-propanesulphonic acid, allylsulphonic acid, methallylsulphonic acid, allyloxybenzenesulphonic acid, methallyloxybenzenesulphonic acid, 2-hydroxy-3- (2-propenyloxy) propanesulphonic acid, 2-methyl-2-propen1-sulphonic acid, 3-sulphate , Sulfomethacrylamide, sulfomethyl methacrylamide and mixtures of the acids mentioned or their water-soluble salts.

In the polymers, the sulfonic acid groups can be wholly or partly in neutralized form. The use of partially or fully neutralized copolymers containing sulfonic acid groups is preferred according to the invention. The molar mass of the sulfo-copolymers preferably used according to the invention can be varied in order to adapt the properties of the polymers to the desired application.

The nonionic monomers used are preferably monomers of the formula R ¹ (R ² ) C =C (R ³ ) -XR ⁴ , in which R ¹ to R ³ independently of one another represent -H, -CH ₃ or -C ₂ H ₅ , X stands for an optionally present spacer group which is selected from -CH ₂ -, -C (O) O- and -C (O) -NH-, and R ^{4 stands} for a straight-chain or branched saturated alkyl radical having 2 to 22 carbon atoms or represents an unsaturated, preferably aromatic radical having 6 to 22 carbon atoms.

Particularly preferred nonionic monomers are butene, isobutene, pentene, 3-methylbutene, 2-methylbutene, cyclopentene, hexene, hexene-1, 2-methylpentene-1, 3-methylpentene-1, cyclohexene, methylcyclopentene, cycloheptene, methylcyclohexene, 2,4 , 4-trimethylpentene-1, 2,4,4-trimethylpentene-2, 2,3-dimethylhexene-1, 2,4-dimethylhexene-1, 2,5-dimethylhexene-1, 3,5-dimethylhexene-1, 4 , 4-dimethylhexane-1, ethylcyclohexyn, 1-octene, α-olefins with 10 or more carbon atoms such as 1-decene, 1-dodecene, 1-hexadecene, 1-octadecene and C ₂₂ -α-olefin, 2-styrene, α-methylstyrene, 3-methylstyrene, 4-propylstyrene, 4-cyclohexylstyrene, 4-dodecylstyrene, 2-ethyl-4-benzylstyrene, 1-vinylnaphthalene, 2-vinylnaphthalene, methyl acrylate, ethyl acrylate, propyl acrylate, methyl acrylate, pentyl acrylate, acrylate N- (methyl) acrylamide, 2-ethylhexyl acrylate, 2-ethylhexyl methacrylate, N- (2-ethylhexyl) acrylamide, octyl acrylate, octyl methacrylate Iester, N- (octyl) acrylamide, acrylic acid lauryl ester, methacrylic acid lauryl ester, N- (lauryl) acrylamide, acrylic acid stearyl ester, methacrylic acid stearyl ester, N- (stearyl) acrylamide, acrylic acid behenyl ester, methacrylic acid behenyl ester and N- (behenyl) acrylamide or mixtures thereof.

The weight proportion of the copolymers containing sulfonic acid groups in the total weight of detergents according to the invention is preferably 0.1 to 15% by weight, preferably 1.0 to 12% by weight and more preferably 2.0 to 10% by weight.

• - 5 bis 70 Gew.-%, insbesondere 5 bis 30 Gew.-% Tenside und/oder
• - 10 bis 65 Gew.-%, insbesondere 12 bis 60 Gew.-% wasserlösliches oder wasserdispergierbares anorganisches Buildermaterial und/oder
• - 0,5 bis 10 Gew.-%, insbesondere 1 bis 8 Gew.-%, wasserlösliche organische Buildersubstanzen und/oder
• - 0,01 bis 15 Gew.-% feste anorganische und/oder organische Säuren bzw. saure Salze und/oder
• - 0,01 bis 5 Gew.-% Komplexbildner für Schwermetalle und/oder
• - 0,01 bis 5 Gew.-% Vergrauungsinhibitor und/oder
• - 0,01 bis 5 Gew.-% Farbübertragungsinhibitor und/oder
• - 0,01 bis 5 Gew.-% Schauminhibitor.

In one embodiment, a detergent comprises

• - 5 to 70 wt .-%, in particular 5 to 30 wt .-% surfactants and / or
• 10 to 65% by weight, in particular 12 to 60% by weight, of water-soluble or water-dispersible inorganic builder material and / or
• - 0.5 to 10% by weight, in particular 1 to 8% by weight, of water-soluble organic builder substances and / or
• - 0.01 to 15 wt .-% solid inorganic and / or organic acids or acidic salts and / or
• - 0.01 to 5 wt .-% complexing agent for heavy metals and / or
• - 0.01 to 5 wt .-% graying inhibitor and / or
• - 0.01 to 5 wt .-% dye transfer inhibitor and / or
• - 0.01 to 5 wt .-% foam inhibitor.

Optionally, the agent can further comprise optical brighteners, preferably from 0.01 to 5% by weight.

Suitable graying inhibitors or soil-release active ingredients are cellulose ethers, such as carboxymethyl cellulose, methyl cellulose, hydroxyalkyl celluloses and mixed cellulose ethers, such as methyl hydroxyethyl cellulose, methylhydroxypropyl cellulose and methyl carboxymethyl cellulose. Sodium carboxymethyl cellulose, hydroxyporpylmethyl cellulose and their mixtures and, if appropriate, their mixtures with methyl cellulose are preferably used. The soil release active ingredients usually used include copolyesters which contain dicarboxylic acid units, alkylene glycol units and polyalkylene glycol units. The proportion of graying inhibitors and / or soil release active ingredients in agents according to the invention is generally not more than 2% by weight and is preferably 0.5 to 1.5% by weight.

For example, derivatives of diaminostilbene disulfonic acid or its alkali metal salts can be contained as optical brighteners for textiles made of cellulose fibers (e.g. cotton). For example, salts of 4,4'-bis (2-anilino-4-morpholino-1,3,5-triazin-6-yl-amino) -stilbene-2,2'-disulfonic acid or similarly structured compounds which instead of of the morpholino group carry a diethanolamino group, a methylamino group or a 2-methoxyethylamino group. Furthermore, brighteners of the substituted 4,4'-distyryl-diphenyl type can be present, for example 4,4'-bis- (4-chloro-3-sulfostyryl) -diphenyl. Mixtures of brighteners can also be used. For polyamide fibers, brighteners of the 1,3-diaryl-2-pyrazoline type, e.g. 1- (p-sulfoamoylphenyl) -3- (p-chlorophenyl) -2-pyrazoline, and similarly structured compounds are particularly suitable. The content of optical brighteners or brightener mixtures in the agent is generally not more than 1% by weight, preferably 0.05 to 0.5% by weight. In a preferred embodiment of the invention, the agent is free from such active ingredients.

The customary foam regulators which can be used in the agents according to the invention include, for example, polysiloxane-silica mixtures, the finely divided silica contained therein preferably being silanized or otherwise hydrophobized. The polysiloxanes can be made from both linear compounds cross-linked polysiloxane resins and their mixtures. Further defoamers are paraffinic hydrocarbons, especially microparaffins and paraffin waxes whose melting point is above 40 ° C, saturated fatty acids or soaps with in particular 20 to 22 carbon atoms, for example sodium behenate, and alkali salts of phosphoric acid mono- and / or dialkyl esters, in which the alkyl chains each have 12 to 22 carbon atoms. ₁₈ alkyl groups used - among these is preferred Natriummonoalkylphosphat and / or with -dialkylphosphat to C _16. The proportion of foam regulators can preferably be 0.2 to 2% by weight.

To set the desired pH, the agents according to the invention can contain acids that are compatible with the system and the environment, in particular citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid and / or adipic acid, but also mineral acids, in particular sulfuric acid or alkali hydrogen sulfates, or bases, in particular ammonium or alkali hydroxides. Such pH regulators are contained in the agents according to the invention preferably not more than 10% by weight, in particular from 0.5 to 6% by weight.

Peroxygen compounds suitable for use in agents according to the invention are, in particular, organic peracids or peracid salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and, under the washing conditions, inorganic salts which release hydrogen peroxide, including perborate, percarbonate, persilicate and / or persulfate such as caroate, as well as hydrogen peroxide inclusion compounds such as H ₂ O ₂ -urea adducts, into consideration. Hydrogen peroxide can also be generated with the aid of an enzymatic system, ie an oxidase and its substrate. If solid peroxygen compounds are to be used, these can be used in the form of powders or granules, which can also be coated in a manner known in principle. The peroxygen compounds can be added to the washing liquor as such or in the form of agents containing them, which in principle can contain all customary detergent, cleaning agent or disinfectant constituents. Alkali percarbonate or alkali perborate monohydrate is particularly preferably used. If an agent according to the invention contains peroxygen compounds, these are present in amounts of preferably up to 50% by weight, in particular from 5 to 30% by weight, more preferably from 0.1 to 20% by weight.

Compounds which, under perhydrolysis conditions, give aliphatic peroxycarboxylic acids with preferably 1 to 10 carbon atoms, in particular 2 to 4 carbon atoms, and / or optionally substituted perbenzoic acid can be used as bleach activators in the compositions. Substances which carry O- and / or N-acyl groups with the stated number of carbon atoms and / or optionally substituted benzoyl groups are suitable. Polyacylated alkylenediamines, especially tetraacetylethylenediamine (TAED), acylated triazine derivatives, especially 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, especially tetraacetylglycoluril (TAGU), N- are preferred Acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenol sulfonates or carboxylates or the sulfonic or carboxylic acids of these, in particular nonanoyl or isononanoyloxybenzenesulfonate or laroyloxybenzenesulfonate (NOBS or iso-NOBS or LOBSoxycarbony), 4- (2xy-NOBSloxy-decony-carbony) ) benzene sulfonate (DECOBS) or decanoyloxybenzoate (DOBA), carboxylic acid anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate, 2,5-diacetoxy-2,5-dihydrofuran and enol esters, as well as acetylated sorbitol and mannitol or the mixtures thereof described SORMAN), acylated sugar derivatives, in particular pentaacetyl glucose (PAG), pentaacetyl fructose, tetraacetylxylose and octaacetyllact ose, acetylated, optionally N-alkylated glucamine and gluconolactone, N-acylated lactams, e.g. N-benzoylcaprolactam, nitriles from which perimidic acids are formed, in particular aminoacetonitrile derivatives with a quaternized nitrogen atom, and / or oxygen-transferring sulfonimines and / or acylhydrazones. The hydrophilically substituted acyl acetals and the acyl lactams are also used with preference. Combinations of conventional bleach activators can also be used. Such bleach activators can, in particular when the abovementioned hydrogen peroxide-supplying bleaches are present, be present in the usual quantity range, preferably in quantities of 0.5 to 10% by weight, in particular 1 to 8% by weight, based on the total agent Use of percarboxylic acid as the sole bleaching agent, however, is preferably completely.

• - 5 bis 20 Gew.-% Natriumpercarbonat,
• - 1 bis 5 Gew.-% Tetraacetylethylendiamin (TAED),
• - 10 bis 24 Gew.-% anionsiche Tenside (LAS),
• - 1 bis 3 Gew.-% nichtionische Tenside.

In preferred embodiments, a detergent according to the invention comprises

• - 5 to 20% by weight sodium percarbonate,
• - 1 to 5 wt .-% tetraacetylethylenediamine (TAED),
• - 10 to 24% by weight of anionic surfactants (LAS),
• - 1 to 3% by weight of nonionic surfactants.

In addition to the conventional bleach activators or instead of them, solid agents can also contain sulfonimines and / or bleach-enhancing transition metal salts or transition metal complexes as so-called bleach catalysts.

The detergents according to the invention can contain an organic solvent as a further component. The addition of organic solvents has a beneficial effect on the enzyme stability and the cleaning performance of these agents. Preferred organic solvents come from the group consisting of monohydric or polyhydric alcohols, alkanolamines or glycol ethers. The solvents are preferably selected from ethanol, n- or i-propanol, butanol, glycol, propane or butanediol, glycerine, diglycol, propyl or butyl diglycol, hexylene glycol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-butyl ether, diethylene glycol mono-butyl ether, diethylene glycol mono-butyl ether, ethylene glycol mono-butyl ether , Propylene glycol methyl, ethyl or propyl ether, dipropylene glycol methyl or ethyl ether, methoxy, ethoxy or butoxy triglycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether and Mixtures of these solvents. The proportion by weight of these organic solvents in the total weight of detergents according to the invention is preferably 0.1 to 10% by weight, more preferably 0.2 to 8.0% by weight and more preferably 0.5 to 5.0% by weight. A particularly preferred organic solvent that is particularly effective in terms of stabilizing the detergents is glycerol and 1,2 propylene glycol. Liquid detergents preferably comprise at least one polyol, preferably from the group glycerol and 1,2-propylene glycol, based on the total weight of the detergent, preferably 0.1 to 10% by weight, preferably 0.2 to 8.0% by weight. % and more preferably 0.5 to 5.0% by weight.

Further preferred organic solvents are the organic amines and alkanolamines. The detergents according to the invention preferably contain these amines in amounts of 0.1 to 10% by weight, preferably 0.2 to 8.0% by weight and more preferably 0.5 to 5.0% by weight, each based on their total weight. A particularly preferred alkanolamine is ethanolamine.

Another preferred component of the detergents according to the invention is a sugar alcohol (alditol). The group of alditols includes non-cyclic polyols of the formula HOCH _{2 [} CH (OH)] _n CH ₂ OH- The alditols include, for example, mannitol (mannitol), isomalt, lactitol, sorbitol (sorbitol) and xylitol (xylitol), threit, erythritol and Arabitol. Sorbitol has proven to be particularly advantageous in terms of enzyme stability. The proportion by weight of sugar alcohol in the total weight of the detergent is preferably 1.0 to 10% by weight, more preferably 2.0 to 8.0% by weight and more preferably 3.0 to 6.0% by weight.

An agent according to the invention advantageously contains the protease in an amount of 2 μg to 20 mg, preferably 5 μg to 17.5 mg, particularly preferably 20 μg to 15 mg and very particularly preferably 50 μg to 10 mg per g of the agent. Furthermore, the protease contained in the agent and / or other ingredients of the agent can be coated with a substance which is impermeable to the enzyme at room temperature or in the absence of water and which becomes permeable to the enzyme under conditions of use of the agent. Such an embodiment of the invention is thus characterized in that the protease is coated with a substance which is impermeable to the protease at room temperature or in the absence of water. Furthermore, the detergent itself can also be packaged in a container, preferably an air-permeable container, from which it is released shortly before use or during the washing process.

The protease and / or possibly other enzymes of the same or a different type contained in the detergent can / can be adsorbed on carrier substances and / or embedded in coating substances in order to protect them against premature inactivation. In the washing liquor, i.e. under application conditions, the enzyme is then released and can develop its catalytic effect. Preferred packaging forms have 0.05 to 15% by weight and in particular up to 10% by weight of active protein of the protease mentioned. A detergent according to the invention contains the protease increasingly preferably in an amount of 1 × 10 ^-8 to 5% by weight, from 0.0001 to 1% by weight, from 0.0005 to 0.5% by weight, from 0.001 up to 0.1% by weight, each based on active protein.

In the agents described herein, the enzymes to be used can also be packaged together with accompanying substances, for example from fermentation. In liquid formulations, the enzymes are preferably used as liquid enzyme formulation (s).

As a rule, the enzymes are not made available in the form of the pure protein, but rather in the form of stabilized, storable and transportable preparations. These pre-packaged preparations include, for example, the solid preparations obtained by granulation, extrusion or lyophilization or especially in the case of liquid or gel-form agents, solutions of the enzymes, advantageously as concentrated as possible, with little water and / or with stabilizers or other auxiliaries added.

Alternatively, the enzymes can be encapsulated both for the solid and for the liquid dosage form, 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 in a solidified gel or those of the core-shell type, in which an enzyme-containing core is coated with a protective layer impermeable to water, air and / or chemicals. Additional active ingredients, e.g. stabilizers, emulsifiers, pigments, bleaches or dyes can also be applied in superimposed layers. Such capsules are applied by methods known per se, e.g. by shaking or rolling granulation or in fluid-bed processes. Such granules are advantageously low in dust, e.g. due to the application of polymeric film formers, and due to the coating are stable in storage.

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

Detergents according to the invention can exclusively contain a Bacillus gibsonii protease, as defined herein. Alternatively, they can also contain other enzymes in a concentration appropriate for the effectiveness of the agent. A further embodiment of the invention thus represent agents which also comprise one or more further enzymes. Other enzymes which can preferably be used are all enzymes which can develop a catalytic activity in the agent according to the invention, in particular a lipase, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, xyloglucanase, β-glucosidase, pectinase, carrageenase, perhydrolase, Oxidase, oxidoreductase or other protease - distinguishable from the protease according to the invention, and mixtures thereof. Further enzymes are advantageously contained in the agent in an amount of 1 × 10 ⁻⁸ to 5% by weight, based on active protein. Each further enzyme is increasingly preferred in an amount of 1 × 10 ^-7 to 3% by weight, from 0.00001 to 1% by weight, from 0.00005 to 0.5% by weight, from 0.0001 up to 0.1% by weight and particularly preferably from 0.0001 to 0.05% by weight in agents according to the invention, based on active protein. The enzymes particularly preferably show synergistic cleaning performance with respect to specific soiling or stains, ie the enzymes contained in the agent composition mutually support one another in their cleaning performance. Such a synergism is particularly preferably present between the protease contained according to the invention and a further enzyme of an agent according to the invention, including in particular between said protease and an amylase and / or a lipase and / or a mannanase and / or a cellulase and / or a pectinase . 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. Solid laundry detergents preferred according to the invention therefore have at least one protease and at least one amylase. In a further preferred embodiment of the invention, solid laundry detergents have at least one protease and at least one cellulase. In a further preferred embodiment, solid laundry detergents have at least one protease and at least one lipase. Solid laundry detergents which have 3 to 10 different enzymes are particularly preferred, and solid laundry detergents which have 3 to 10 different types of enzymes can be particularly preferred with regard to cleaning performance over a very large spectrum of stains.

Examples of proteases are the subtilisins BPN 'from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, the protease PB92, the subtilisins 147 and 309, the protease from Bacillus lentus, subtilisin DY and the subtilases, but no longer attributable to the subtilisins in the narrower sense Thermitase, Proteinase K and the proteases TW3 and TW7. Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from the Novozymes company. The subtilisins 147 and 309 are sold under the trade names Esperase® and Savinase® by the company Novozymes. The protease variants under the name BLAP® are derived from the protease from Bacillus lentus DSM 5483. Further usable proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase® and Ovozyme® from the Novozymes company, which are sold under the trade names, Purafect®, Purafect® OxP, Purafect® Prime, Excellase® and Properase® by the company Danisco / Genencor, which is sold under the trade name Protosol® by the company Advanced Biochemicals Ltd., which is sold under the trade name Wuxi® by the company Wuxi Snyder Bioproducts Ltd., which is sold under the trade name Proleather® and Protease P ® from Amano Pharmaceuticals Ltd., and under the name Proteinase K-16 from Kao Corp. available enzymes. The proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in the international patent applications, are also used with particular preference WO2008086916 and WO2007131656 . Further proteases which can be used advantageously are disclosed in the patent applications WO9102792 , WO2008007319 , WO9318140 , WO0144452 , GB1243784 , WO9634946 , WO2002029024 and WO2003057246 . Further proteases that can be used are those which are naturally present in the microorganisms Stenotrophomonas maltophilia, in particular Stenotrophomonas maltophilia K279a, Bacillus intermedius and Bacillus sphaericus.

Examples of amylases are the α-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens or Bacillus stearothermophilus and, in particular, their improved further developments for use in detergents or cleaning agents. The enzyme from Bacillus licheniformis is available from the Novozymes company under the name Termamyl® and from the Danisco / Genencor company under the name Purastar® ST. Further development products of this α-amylase are available from Novozymes under the trade names Duramyl® and Termamyl® ultra, from Danisco / Genencor under the name Purastar® OxAm and from Daiwa Seiko Inc. as Keistase®. The α-amylase from Bacillus amyloliquefaciens is sold by the Novozymes company under the name BAN®, and variants derived from the α-amylase from Bacillus stearothermophilus under the names BSG® and Novamyl®, also by the Novozymes company. Furthermore, the α-amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) should be emphasized. The amylolytic enzymes described in the international patent applications can also be used WO2003002711 , WO2003054177 and WO2007079938 are disclosed, to the disclosure of which is therefore expressly referred to or whose disclosure content in this regard is therefore expressly included in the present patent application. Fusion products of all mentioned molecules can also be used. In addition, the further developments of the α-amylase from Aspergillus niger and A. oryzae, available from the Novozymes company under the trade names Fungamyl®, are suitable. Further commercial products that can be used advantageously are, for example, Amylase-LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus® and Amplify ™ 12L or Amplify Prime ™ 100L, the latter also from Novozymes. Variants of these enzymes obtainable by point mutations can also be used according to the invention.

Examples of cellulases (endoglucanases, EG) is the fungal, endoglucanase (EG) -rich cellulase preparation or its further developments, which is offered by the Novozymes company under the trade name Celluzyme®. The products Endolase® and Carezyme®, which are also available from Novozymes, are based on the 50 kD EG and the 43 kD EG from Humicola insolens DSM 1800. Other commercial products from this company are Cellusoft®, Renozyme® and Celluclean®. Cellulases, for example, which are available from the company AB Enzymes under the trade names Ecostone® and Biotouch®, and which are at least partly based on the 20 kD EG from Melanocarpus, can also be used. Other cellulases from AB Enzymes are Econase® and Ecopulp®. Further suitable cellulases are from Bacillus sp. CBS 670.93 and CBS 669.93, the ones from Bacillus sp. CBS 670.93 is available from Danisco / Genencor under the trade name Puradax®. Other commercial products from Danisco / Genencor that can be used are “Genencor detergent cellulase L” and IndiAge®Neutra.

Other enzymes that can be used are e.g. lipases or cutinases, in particular because of their triglyceride-cleaving activities, but also to generate peracids in situ from suitable precursors. These include, for example, the lipases originally obtained from Humicola lanuginosa (Thermomyces lanuginosus) or further developed therefrom, in particular those with one or more of the following amino acid exchanges starting from the lipase mentioned in positions D96L, T213R and / or N233R, particularly preferably T213R and N233R. Lipases are sold, for example, by the Novozymes company under the trade names Lipolase®, Lipolase® Ultra, LipoPrime®, Lipozyme® and Lipex®. Another lipase that can be used advantageously is available under the trade name Lipoclean® from Novozymes. Furthermore, e.g. the cutinases that were originally isolated from Fusarium solani pisi and Humicola insolens can be used. Lipases which can also be used are available from Amano under the names Lipase CE®, Lipase P®, Lipase B®, or Lipase CES®, Lipase AKG®, Bacillus sp. Lipase®, Lipase AP®, Lipase M-AP® and Lipase AML® available. For example, the lipases or cutinases from the Danisco / Genencor company can be used whose starting enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii. Other important commercial products are the preparations M1 Lipase® and Lipomax® originally sold by the company Gist-Brocades (now Danisco / Genencor) and those from the company Meito Sangyo KK under the names Lipase MY-30®, Lipase OF® and Lipase PL ® should be mentioned, as well as the product Lumafast® from Danisco / Genencor.

To increase the bleaching effect, according to the invention, oxidoreductases, for example oxidases, oxygenases, catalases, peroxidases, such as halo-, chloro-, bromo-, lignin, glucose or manganese peroxidases, Dioxygenases or laccases (phenol oxidases, polyphenol oxidases) are used. Advantageously, preferably organic, particularly preferably aromatic, compounds interacting with the enzymes are added in order to increase the activity of the oxidoreductases concerned (enhancers) or to ensure the flow of electrons (mediators) in the event of greatly differing redox potentials between the oxidizing enzymes and the soiling.

The enzymes to be used in the context of the present invention can originate, for example, originally from microorganisms, for example of the genera Bacillus, Streptomyces, Humicola or Pseudomonas, and / or be produced by suitable microorganisms according to known biotechnological processes, for example by transgenic expression hosts, for example of the genera Escherichia , Bacillus or filamentous fungi. It is emphasized that it can in particular also be technical enzyme preparations of the respective enzyme, i.e. accompanying substances can be present. The enzymes can therefore be packaged and used together with accompanying substances, for example from fermentation or with other stabilizers.

The embodiments of the present invention include all solid, powdery, granular, tablet-like, liquid, gel-like or pasty dosage forms of agents according to the invention, which can optionally also consist of several phases and can be in compressed or uncompressed form. The agent can be in the form of a free-flowing powder, in particular with a bulk density of 300 to 1200 g / l, in particular 500 to 900 g / l or 600 to 850 g / l. The solid dosage forms of the agent also include extrudates, granules, tablets or pouches containing solid agents, which can be present both in large containers and in portions. Alternatively, the agent can also be liquid, gel-like or pasty, e.g. in the form of a non-aqueous agent or a non-aqueous paste or in the form of an aqueous agent or a water-containing paste. Furthermore, the agent can be in the form of a one-component system. Such means consist of a phase. Alternatively, a product can also consist of several phases (multi-component system). Such an agent is therefore divided into several components, e.g. two liquid, two solid or one liquid and one solid phase. The liquid forms based on water and / or organic solvents can be thickened or in the form of gels.

According to the definition of the invention, a substance, e.g. a composition or an agent, is solid if it is in the solid state of aggregation at 25 ° C and 1,013 mbar.

According to the definition of the invention, a substance, e.g. a composition or an agent, is liquid if it is in the liquid state of aggregation at 25 ° C and 1,013 mbar. Liquid also includes gel-like.

When the detergents according to the invention are in liquid form, they preferably contain more than 40% by weight, preferably 50 to 90% by weight and particularly preferably 60 to 80% by weight of water, based on their total weight.

A further subject matter of the invention is a method for cleaning textiles, a textile detergent according to the invention, in particular a solid textile detergent, being used in at least one process step. This includes both manual and machine processes, with machine processes being preferred due to their more precise controllability, for example with regard to the quantities used and exposure times. Processes for cleaning textiles are generally characterized in that, in one or more process steps, various active cleaning substances are applied to the items to be cleaned and washed off after the exposure time, or that the items to be cleaned are treated in some other way with a detergent or a solution of this agent. In various embodiments, the method is characterized in that the protease is used at a temperature of 0 to 100 ° C., preferably 10 to 70 ° C., more preferably 30 to 50 ° C. and most preferably 20 to 40 ° C. In particular, in processes which are carried out at a temperature between 10 and 60 ° C, preferably between 15 and 50 ° C and more preferably between 20 and 40 ° C, the advantages of using the textile detergents according to the invention compared to textile detergents with conventionally used proteases for the Consumer visible. All facts, subjects and embodiments that are described for textile detergents according to the invention are also applicable to this subject matter of the invention. Therefore, reference is expressly made at this point to the disclosure at the appropriate point with the note that this disclosure also applies to the above methods according to the invention.

Alternative embodiments of this subject matter of the invention also represent processes for treating raw textile materials or for textile care, in which a protease according to the invention becomes active in at least one process step. Among these, processes for textile raw materials, fibers or textiles with natural components are preferred, and very particularly for those with wool or silk.

The proteases used in the agents according to the invention can advantageously be used in accordance with the above statements in textile detergents and methods for washing textiles. They can therefore be used advantageously to provide proteolytic activity in appropriate agents and processes.

• - eine Verwendung eines erfindungsgemäßen Mittels zur Reinigung von Textilien, und/oder
• - eine Verwendung einer Protease, die mindestens 70% Sequenzidentität mit der in SEQ ID NO:1 angegebenen Aminosäuresequenz über deren Gesamtlänge aufweist und die eine Aminosäuresubstitution an mindestens einer der Positionen, die den Positionen 12, 43, 122, 127, 154, 156, 160, 211, 212 und 222, jeweils bezogen auf die Nummerierung gemäß SEQ ID NO:1, entsprechen, aufweist, zur Entfernung von proteasesensitiven Anschmutzungen von Textilien;

insbesondere derart, dass die Protease jeweils in einer Menge von 40 µg bis 4 g, vorzugsweise von 50 µg bis 3 g, besonders bevorzugt von 100 µg bis 2 g und ganz besonders bevorzugt von 200 µg bis 1 g eingesetzt wird. Besonders bevorzugte Ausführungsformen stellen dabei z.B. die Handwäsche, die manuelle Entfernung von Flecken von Textilien oder die Verwendung im Zusammenhang mit einem maschinellen Verfahren dar. Alle Sachverhalte, Gegenstände und Ausführungsformen, die für erfindungsgemäße Proteasen und sie enthaltende Mittel beschrieben sind, sind auch auf diesen Erfindungsgegenstand anwendbar. Daher wird an dieser Stelle ausdrücklich auf die Offenbarung an entsprechender Stelle verwiesen mit dem Hinweis, dass diese Offenbarung auch für die vorstehende erfindungsgemäße Verwendung gilt.Further subjects of the invention are therefore

• - Use of an agent according to the invention for cleaning textiles, and / or
• a use of a protease which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length and which has an amino acid substitution in at least one of the positions corresponding to positions 12, 43, 122, 127, 154, 156, 160, 211, 212 and 222, each based on the numbering according to SEQ ID NO: 1, corresponds to, for removing protease-sensitive soiling from textiles;

in particular such that the protease is used in an amount of 40 μg to 4 g, preferably 50 μg to 3 g, particularly preferably 100 μg to 2 g and very particularly preferably 200 μg to 1 g. Particularly preferred embodiments are, for example, hand washing, manual removal of stains from textiles or use in connection with a machine process. All facts, objects and embodiments that are described for proteases according to the invention and agents containing them are also applicable to this subject matter of the invention applicable. For this reason, reference is expressly made at this point to the disclosure at the appropriate point with the note that this disclosure also applies to the above use according to the invention.

Examples

Example 1: Cleaning performance of protease in solid detergent

A commercially available solid detergent with the following composition was used: raw material % AM in Formula Surfactant 5-20 Bleach 4-16 Bleach activator 1-5 Builder 15-50 Cobuilder 3-8 Enzymes (other than protease) 0.1-2 Optical brighteners 0.05-0.3 Fillers 5-60 Dosage: 65 g pH value: 10.5

• The proteases were incorporated into the above-mentioned detergent matrix with an active enzyme content of 0.0012%. The proteases used were:
  • E1: protease according to WO2002088340
  • E2: Protease according to SEQ ID NO: 5 from WO2017215925

The washing test was carried out according to A.I.S.E. Laundry Detergent Testing Guidelines carried out in a Miele W1935 (standard washing program, 53 min main wash, 17 L water, 16 ° dH, 3.5 kg ballast laundry). The cleaning performance was measured on six protease-sensitive soils. Five repetitions were performed in each case and the results averaged. The cleaning performance was determined as the lightening performance of the soiling on the textiles. The modified Y-value was determined for all soiling in accordance with the IEC standard 59D / 165 / CDV procedure. The various types of soiling were measured with a Mach 5 / Speactraflash 500, 600 (Co. Datacolor) (large area view = 30mm, barrier filter 420nm) or with an X-Rite SP62 (large area view = 14mm) with ColorScout XY table (1 measuring point ) measured.

Results: Soiling E1 E2 CFT CS-01 Blood (aged) CO 45.3 46.4 TEST -111 Blood CO 70.6 71.6 CFT C-05 Blood, milk, ink CO 31.3 33.9 CFT C-03 Chocolate milk with carbon black CO 66.1 68.6 CFT CS-02 Cocoa CO 59.9 61.7 WFK 10Z Chocolate CO 68.7 69.7

Protease E2 shows an improved cleaning performance on chocolate and blood stains.

QUOTES INCLUDED IN THE DESCRIPTION

This list of the documents listed by the applicant was generated automatically and is included solely for the better information of the reader. The list is not part of the German patent or utility model application. The DPMA assumes no liability for any errors or omissions.

Patent literature cited

• DE 2412837 [0094]
• WO 2008086916 [0125]
• WO 2007131656 [0125]
• WO 9102792 [0125]
• WO 2008007319 [0125]
• WO 9318140 [0125]
• WO 0144452 [0125]
• GB 1243784 [0125]
• WO 9634946 [0125]
• WO 2002029024 [0125]
• WO 2003057246 [0125]
• WO 2003002711 [0126]
• WO 2003054177 [0126]
• WO 2007079938 [0126]

Non-patent literature cited

• Altschul et al. (1990) "Basic local alignment search tool", J. Mol. Biol. 215: 403-410 [0025]
• Altschul et al. (1997) "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs", Nucleic Acids Res., 25: 3389-3402 [0025]
• Chenna et al. (2003) "Multiple sequence alignment with the cluster series of programs", Nucleic Acid Res. 31: 3497-3500 [0025]
• Notredame et al. (2000) "T-Coffee: A novel method for multiple sequence alignments", J. Mol. Biol. 302: 205-217 [0025]
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Claims (10)

Textile detergent, in particular solid laundry detergent, comprising at least one protease which comprises an amino acid sequence which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length and which has an amino acid substitution in at least one of the positions corresponding to positions 12, 43, 122, 127, 154, 156, 160, 211, 212 or 222, each based on the numbering according to SEQ ID NO: 1. Detergent according to Claim 1 , wherein the at least one amino acid substitution is selected from the group consisting of Q12L, I43V, M122L, D127P, N154S, T156A, G160S, M211N, M211L, P212D, P212H or A222S, each based on the numbering according to SEQ ID NO: 1. Detergent according to Claim 1 and 2 , wherein the protease has one of the following amino acid substitution variants, in each case based on the numbering according to SEQ ID NO: 1: (i) 143V; (ii) M122L, N154S, and T156A; (iii) M211N and P212D; (iv) M211L and P212D; (v) G160S; (vi) D127P, M211L and P212D; (vii) P212H; or (viii) Q12L, M122L and A222S. Detergent according to Claim 1 to 3 , wherein the protease in an amount of 1 × 10 ^-8 to 5 wt .-% and increasingly preferably from 0.0001 to 1 wt .-%, from 0.0005 to 0.5 wt .-%, from 0.001 to 0 , 1 wt .-%, based on the total weight of the detergent is contained in this. Detergent according to one of the Claims 1 to 4th , wherein it comprises at least one further enzyme selected from the group consisting of amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, xyloglucanases, β-glucosidases, pectinases, carrageenases, perhydrolases, oxidases, oxidoreductases, lipase and combinations thereof is, preferably at least one amylase. Detergent according to one of the Claims 1 to 5 , where it - 2 to 30 wt .-%, in particular 5 to 25 and more preferably 10 to 20 wt .-% bleach, in particular an inorganic or organic peroxide source, preferably selected from peracids or peracid salts of organic acids such as phthalimidopercaproic acid, perbenzoic acid or Diperdodecanedioic acid, inorganic salts such as perborate, percarbonate, particularly preferably alkali percarbonate or alkali perborate, and / or - 1 to 10% by weight, in particular 1.5 to 7.5% by weight and more preferably 2 to 5% by weight bleach activator , especially selected from acylated alkylenediamines, especially tetraacetylethylenediamine (TAED), acylated triazine derivatives, especially 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, especially tetraacetylglycoluril (TAGU), N Acylimides, in particular N-nonanoyl succinimide (NOSI), acylated phenol sulfonates or carboxylates or the sulfonic or carboxylic acids of these, especially nonanoyl or isononanoyloxybenzenesulfonate or laroyloxybenzenesulfonate (NOBS or iso-NOBS or LOBS), 4- (2-decanoyloxyethoxycarbonyloxy) -benzenesulfonate (DECOBS) or decanoyloxybenzoate (DOBA), carboxylic anhydrides, in particular phthalic anhydride, in particular triacylated polyhydric alcohols, 2,5 Diacetoxy-2,5-dihydrofuran and enol esters as well as acetylated sorbitol and mannitol or their mixtures (SORMAN), acylated sugar derivatives, in particular pentaacetyl glucose (PAG), pentaacetyl fructose, tetraacetylxylose and octaacetyl lactose, acetylated, optionally N-alkylated glucamine and glucone acylated lactams, nitriles, in particular aminoacetonitrile derivatives with a quaternized nitrogen atom, and / or oxygen-transferring sulfonimines and / or acylhydrazones. Detergent according to one of the Claims 1 to 6 in a 1% strength by weight solution in deionized water at 20 ° C. having a pH in a range from 7 to 12, in particular 8 to 12, preferably 9 to 11 and particularly preferably 10 to 11. Process for cleaning textiles, characterized in that in at least one process step an agent according to one of the Claims 1 to 7th is applied. Use of a detergent according to one of the Claims 1 to 7th for removing peptide or protein-containing soiling from textiles. Use of a protease which comprises an amino acid sequence which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length and which has an amino acid substitution in at least one of the positions corresponding to positions 12, 43, 122, 127, 154 , 156, 160, 211, 212 or 222, each based on the numbering according to SEQ ID NO: 1, for removing protein-containing soiling from textiles.