DE102007036756A1 - New proteases and detergents and cleaners containing these new proteases - Google Patents

Abstract

The present invention relates to novel subtilisin-type proteases and to sufficiently related proteins and their derivatives. It also relates to detergents and cleaners with these novel subtilisin-type proteases, sufficiently related proteins and their derivatives, corresponding washing and cleaning processes and their use in detergents and cleaners, and other technical uses.

Description

The present application relates to a novel proteases whose DNA Soil samples were obtained, all sufficiently similar Proteases and nucleic acids as well as technical applications for these proteases, especially their use in washing and detergents.

Proteases are among the most technically important enzymes of all. Of these, in turn, proteases of the subtilisin type (subtilases, subtilopeptidases, EC 3.4.21.62) are particularly important, which are attributed to the serine proteases due to the catalytically active amino acids. They act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are internal to peptides or proteins. Their pH optimum is usually in the clearly alkaline range. An overview of this family offers for example 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 naturally produced by microorganisms; Of these, in particular, the subtilisins formed and secreted by Bacillus species are to be mentioned as the most important group within the subtilases.

proteases In addition to other enzymes, active ingredients of washing and detergents. They cause the breakdown proteinaceous Stains on the items to be cleaned. Conveniently result synergies between the enzymes and the rest Components of the funds concerned. Among the detergent and cleaner proteases take subtilases because of their favorable enzymatic Properties such as stability or pH optimum are outstanding Position. They are also suitable for a variety other technical uses, for example as components of cosmetics or in organic-chemical Synthesis.

Examples for those preferably used in detergents and cleaners Subtilisin-type proteases are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, subtilisin DY and those subtilases, not but more to the subtilisins in the narrower sense attributable enzymes Thermitase, proteinase K and the proteases TW3 and TW7.

The subtilisin BPN ', which is derived from Bacillus amyloliquefaciens, or B. subtilis, is from the work of Vasantha et al. (1984) in J. Bacteriol., Volume 159, pp. 811-819 and from JA Wells et al. (1983) in Nucleic Acids Research, Volume 11, pp. 7911-7925 known. Subtilisin BPN 'serves as a reference enzyme of the subtilisins, in particular with regard to the numbering of the positions.

Subtilisin Carlsberg in a developed form under the trade names Alcalase ^® from Novozymes A / S, Bagsvaerd, Denmark. It is published in the publications of EL Smith et al. (1968) in J. Biol. Chem., Volume 243, pp. 2184-2191 , and from Jacobs et al. (1985) in Nucl. Acids Res., Vol. 13, pp. 8913-8926 and is naturally produced by Bacillus licheniformis.

The protease PB92 is naturally derived from the alkaliphilic bacterium Bacillus nov. spec. 92 and Gist-Brocades, Delft, The Netherlands, available under the trade name was Maxacal ^® by the company.. In its original sequence, it is in the patent application EP 283075 A2 described.

The subtilisins 147 and 309 are sold under the trade names Esperase ^®, or Savinase ^® from Novozymes. They are originally from Bacillus strains with the application GB 1243784 A be revealed.

From the protease from Bacillus lentus DSM 5483 ( WO 91/02792 A1 ) derive from the name under the name BLAP ^® variants, which in particular in WO 92/21760 A1 . WO 95/23221 A1 . WO 02/088340 A2 and WO 03/038082 A2 to be discribed. Other useful proteases from various Bacillus sp. and B. gibsonii go out of the patent applications WO 03/054185 A1 . WO 03/056017 A2 . WO 03/055974 A2 and WO 03/054184 A1 out.

The subtilisin DY is originally from Nedkov et al. 1985 in Biol. Chem Hoppe-Seyler, volume 366, pp. 421-430 been described.

Other usable proteases are, for example, under the trade names Durazym ^®, relase ^®, Everlase® ^®, Nafizym, Natalase ^®, Kannase® ^® and Ovozyme ^® from Novozymes, the ^® under the trade names Purafect ^®, Purafect ^® OxP, Purafect Prime and Properase.RTM ^® from Genencor, that under the trade name Protosol® ^® from Advanced Biochemicals Ltd., Thane, India, under the Han registered names Wuxi ^® from Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® ^® and Protease P ^® from Amano Pharmaceuticals Ltd., Nagoya, Japan, and sold under the name Proteinase K-16 from Kao Corp. ., Tokyo, Japan.

Further usable variants of proteases of type TY145 are described in US Pat US Patent Application US 2004/0209343, for example according to SEQ ID NO. 1 of said US application.

The Proteases used in agents according to the invention are either originally from microorganisms, for example from microorganisms of the genera Bacillus, Streptomyces, Humicola, or Pseudomonas, and / or are used according to known biotechnological Process produced by suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or by filamentous fungi.

The classical procedure for the production of new enzymes consists of microorganism-containing To take samples from natural habitats and under the conditions considered suitable - for example in alkaline medium - to cultivate. In this way one obtains enrichment cultures of microorganisms that with a certain probability also enzymes, including Alkaline Contain proteases which are active under the conditions in question are. This will then, for example, over Ausplattieren on protein-containing agar plates and measuring the lysis court formed the microorganisms selected with the most powerful enzymes and purified or cloned the genes in question.

Such a procedure is for example in the Textbook "Alkalophilic Microorganisms. A new microbial world "by K. Horikoshi and T. Akiba (1982), Japan Scientific Societies Press, Springer-Verlag, New York, Heidelberg, Berlin, ISBN 0-387-10924-2, Chapter 2, pages 9-26 described. For example, too WO 00/24882 A1 discloses a method for producing a gene bank obtained by culturing and thus enriching microorganism-containing samples from any habitat, for example, the rumen, under the conditions of interest, and isolating and cloning nucleic acids of interest thereto.

Thus, naturally, preferably microbially formed alkaline proteases are used in detergents and cleaners. For example, after logging in WO 93/07276 A1 those from Bacillus spec. 164-A1 Protease 164-A1 available from Chemgen Corp., Gaithersburg, MD, USA, and Vista Chemical Company, Austin, TX, USA, for use in detergents and cleaners. Other examples are the alkaline protease from Bacillus sp. PD138, NCIMB 40338 from Novozymes A / S, Bagsværd, Denmark, ( WO 93/18140 A1 ) derived from Bacillus sp. ferm. BP-3376-derived proteinase K-16 from Kao Corp., Tokyo, Japan, ( U.S. Patent 5,344,770 ) and according to WO 96/25489 A1 (Procter & Gamble, Cincinnati, OH, USA) the protease from the psychrophilic organism Flavobacterium balustinum.

Other alkaline proteases, which are formed by microorganisms which are isolatable from natural habitats, go for example from the applications WO 03/054185 A1 (from Bacillus gibsonii (DSM 14391)), WO 03/056017 A2 (from Bacillus sp. (DSM 14390)), WO 03/055974 A2 (from Bacillus sp. (DSM 14392)) and WO 03/054184 A1 (from Bacillus gibsonii (DSM 14393)). All of these applications also disclose corresponding detergents and cleaners containing these novel alkaline proteases.

Regarding the use of proteases in detergents and cleaners known that proteases improve the washing or Cleaning performance together with other enzymes, for example Amylases, cellulases, hemicellulases, mannanases, β-glucosidases, Oxidases, oxidoreductases or lipases can be used. Likewise, the use of proteases in detergents in combination with other active ingredients such as bleaches or soil release agents known to the skilled person.

It It is also known that some for use in detergents established proteases also for cosmetic purposes or for the organic-chemical synthesis are suitable.

The exemplified here, various technical applications require proteases with different properties, for example the reaction conditions, stability or substrate specificity As. Conversely, the technical capabilities are dependent proteases, for example in the context of a detergent or cleaning agent formulation, of other factors such as stability of the enzyme high temperatures, against oxidizing agents, whose Denaturation by surfactants, folding effects or desired Synergies with other ingredients.

Consequently There is still a high demand for technically usable Proteases, due to the variety of their uses in their Entire a wide range of properties to very much cover subtle differences in performance.

The Basis for this is extended by new proteases, which For its part, it is purposefully further developed with regard to special fields of application can be.

Of the The present invention was therefore based on the object, more, yet to find unknown proteases. The respective wild-type enzyme should preferably be characterized in that it is in use in an appropriate manner established for this purpose At least comes close to enzymes. Here was in particular the contribution for the performance of a detergent or cleaning agent of interest.

Further Objects of the present invention can be seen therein to provide proteases, in particular of the subtilisin type, which compared to the prior art, an improved stability against temperature influences, pH fluctuations, denaturing or oxidizing agents, proteolytic degradation, high temperatures, acidic or alkaline conditions or opposite have a change in the redox ratios. Other tasks may result in decreased immunogenicity or reduced allergenic effects.

A Another particular object of the present invention was proteases to locate at temperatures of 20 to 60 ° C. a good washing performance, preferably an improved washing performance in the Comparison to the proteases disclosed in the prior art, in particular those of the subtilisin type.

A Another particular object of the present invention was proteases to locate those known in the art homologous proteases have improved washing performance at least one soiling, preferably in relation to several soils, exhibit.

Further Partial tasks consisted of nucleic acids which code for such proteases and vectors, To provide host cells and manufacturing processes, which can be used to obtain such proteases. Furthermore, appropriate means, in particular washing and cleaning agents, appropriate washing and cleaning procedures and corresponding Uses for such proteases to provide. Finally, should technical applications for the found Proteases are defined.

• a) Aminosäuresequenz, die zu der in SEQ ID NO. 3 angegebenen Aminosäuresequenz zu mindestens zu 94,2% identisch ist.
• b) Aminosäuresequenz, die zu der in SEQ ID NO. 2 angegebenen Aminosäuresequenz zu mindestens 59% identisch ist.

The object is achieved according to the teaching of claim 1. An object of the invention thus forms a protease comprising an amino acid sequence which is selected from the group consisting of

• a) Amino acid sequence corresponding to that shown in SEQ ID NO. 3 amino acid sequence is identical to at least 94.2% identical.
• b) Amino acid sequence corresponding to that shown in SEQ ID NO. 2 amino acid sequence is identical to at least 59% identical.

Herewith are as further subject of the invention the associated Nucleic acids, corresponding natural cells, appropriate methods for their identification, in particular the Nucleic acid-based molecular biology method and process elements and agents, detergents and cleaning agents, Washing and cleaning procedures and the concerned Proteases identified uses connected.

Already the in SEQ ID NO. 3 indicated enzyme has a proteolytic activity so that the proteases can be used for their application in washing and detergents are considered suitable. Due to the Provided DNA is an additional Optimization of this enzyme, for example via further point mutations possible. Furthermore, this DNA can be used in shuffling approaches introduced and thus to produce completely new proteases be used.

Under For the purposes of the present application, an enzyme is a protein to understand that has a certain biocatalytic function. Protease in the sense of the present application is an enzyme which catalyzes the hydrolysis of peptide bonds and thereby be able to cleave peptides or proteins.

One Protein is one of the natural within the meaning of the present application Amino acids composed, largely linearly structured, to perform its function mostly three-dimensional structure accepting polymer, d. H. a polypeptide to understand. A peptide In the present application, the proteinogenic, naturally occurring L-amino acids with the internationally commonly used 1- and 3-letter codes. numerous Proteins are called preproteins, ie together formed with a signal peptide. Below that is the N-terminal Part of the protein whose function is mostly to the discharge of the formed protein from the producing cell into the periplasm or the surrounding medium and / or its correct one To ensure folding. Subsequently, the Signal peptide under natural conditions by a signal peptidase split off from the remaining protein, so this is its actual catalytic activity without the initial ones Exerts N-terminal amino acids. Proproteins are inactive precursors of proteins. Their forerunner with signal sequence are referred to as pre-pro-proteins. For technical applications are due to their enzymatic Activity the valves, d. H. mature peptides, d. H. the After their preparation, enzymes were processed in relation to the Preproteins preferred. The proteins can be from the cells producing them after the production of the polypeptide chain be modified, for example, by attaching Sugar molecules, formylations, aminations, etc. Such Modifications are referred to as post-translational modifications. These post translational modifications may need however, do not exert any influence on the function of the protein.

in the For the purposes of the present invention, all enzymes, proteins, fragments and derivatives, unless explicitly addressed as such to be summarized under the generic term proteins.

By Comparison with known enzymes, for example, in general accessible databases From the amino acid or nucleotide sequence the enzymatic Activity of a considered enzyme infer. This can through other areas of the protein that are not at the actual Reaction involved, qualitatively or quantitatively modified become. This could be, for example, the enzyme stability, the activity, the reaction conditions or the substrate specificity affect.

Such a comparison is accomplished by associating similar sequences in the nucleotide or amino acid sequences of the proteins of interest. This is called homologization. A tabular assignment of the respective positions is referred to as alignment. In the analysis of nucleotide sequences, in turn, both complementary strands and all three possible reading frames are to be taken into account; as well as the degeneracy of the genetic code and the organism-specific use of codons (codon usage). Meanwhile, alignments are created using computer programs, such as the algorithms FASTA or BLAST; This procedure is for example by DJ Lipman and WR Pearson (1985) in Science, Vol. 227, pp. 1435-1441 described.

A Compilation of all matching in the compared sequences Positions is called a consensus sequence.

Such a comparison also allows a statement about the similarity or homology of the compared sequences to each other. This one will in percent identity, that is the proportion of identical nucleotides or amino acid residues on the same or in an alignment corresponding positions reproduced. One more broad homology term refers to the conserved Amino acid substitutions in this value. It is then from percent similarity the speech. Such statements can over entire proteins or genes or only over individual areas to be hit.

homologous Areas of different proteins are by matches defined in the amino acid sequence. these can also be characterized by identical function. She goes up to complete identities in the smallest areas, so-called boxes, which comprise only a few amino acids and mostly essential for overall activity Exercise functions. Among the functions of homologues Areas are the smallest subfunctions of the whole protein To understand function, such as the training of individual Hydrogen bonds for complexation of a substrate or transitional complex.

The amino acid sequences according to the invention are as described in the examples for the present application, derived from nucleic acids derived from a proteolytic active bacterium have been isolated from a soil sample.

A Nucleic acid sequence according to the invention is under SEQ ID NO. 1 indicated. This nucleic acid encodes for a polypeptide which is one for subtilisins typical classification into signal peptide, propeptide and mature Protease has. The full-length protein is under SEQ ID NO. 2 and the mature protease under SEQ ID NO. 3 indicated. By this is meant the actually active mature protein, because this exercises the technically relevant function. Especially therefore, the amino acid sequence of the mature, active protease is preferred.

As shown in Example 3, this protease was added to the non-redundant gene bank ( Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs "; Nucleic Acids Res., 25, pp. 3389-3402 .) Homology comparison performed with the previously known proteases.

The next-described enzyme described was the protease identified as SEQ ID NO. 1 is disclosed in US patent application US 2004/0209343. Like all subsequent homology values via the computer program Vector NTI ^® Suite 7.0, available from InforMax, Inc., Bethesda, USA, determined with the specified default parameters identity at the amino acid level is 94.1% (cf. 1 ), based on the sequence of the mature enzyme according to SEQ ID NO. 3, which includes 307 amino acids. Thus, the protease found is a new enzyme. Thus, all proteases which are at least 94.2% identical to SEQ ID NO. 3 are. To the established B. lentus alkaline protease ( WO 97/21760 A1 ) gives an identity of 36.5% over the length of this alkaline protease at the amino acid level, again based on the mature enzyme. Based on the total length protein according to SEQ ID NO. 2, the BLAST query described above resulted in the next similar database entry as the protease according to database entry AA693489.1 ("toxin degrading protease") .The determined identity at the amino acid level is 58% based on the sequence of the total protein according to SEQ ID NO All proteases which are at least 59% identical to SEQ ID NO. 2 are included in the scope of protection.

• a) Aminosäuresequenz, die zu der in SEQ ID NO. 3 angegebenen Aminosäuresequenz zunehmend bevorzugt zu mindestens 94,5%, 95%, 95,5%, 96%, 96,5%, 97%, 97,5%, 98%, 98,5%, 99%, 99,5% und ganz besonders bevorzugt zu 100% identisch ist
• b) Aminosäuresequenz, die zu der in SEQ ID NO. 2 angegebenen Aminosäuresequenz zu mindestens 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 94,5%, 95%, 95,5%, 96%, 96,5%, 97%, 97,5%, 98%, 98,5%, 99%, 99,5% und ganz besonders bevorzugt zu 100% identisch ist.

In a preferred embodiment of the invention, the protease is characterized by comprising an amino acid sequence selected from the group consisting of

• a) Amino acid sequence corresponding to that shown in SEQ ID NO. 3, more preferably at least 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5 % and most preferably 100% identical
• b) Amino acid sequence corresponding to that shown in SEQ ID NO. 2 at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 94.5%, 95%, 95.5% , 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5%, and most preferably 100% identical.

proteins can also talk about the reaction with an antiserum or a particular antibody to groups immunologically related proteins are summarized. The members A group is characterized by being the same, by one Antibodies recognized to have antigenic determinant.

a Another subject of the invention therefore proteases, characterized are that they have at least one and increasingly two, three or four matching antigenic determinants with one having protease of the invention.

In Another embodiment of the invention is an inventive Protease naturally present in an organism, which can be isolated from a natural habitat.

These Embodiment is therefore particularly advantageous because then the associated organism itself taken into culture can be. Advantageously, can then be from its cell extracts or culture supernatants of the invention Isolate and produce proteases.

this includes those alkaline proteases are preferred, wherein the said organism is a microorganism, preferably a fungus, a Gram-negative or a Gram-positive bacterium, and among these more preferably one of the genus Bacillus.

Because especially for these organisms are in the state of the art Cultivation methods known and established. This is especially true for Bacilli, which in the technical enzyme production a play a prominent role. In a further embodiment the invention is a protease according to the invention characterized in that they are in the bacterial strain Bacillus sp. DSM ID 01-189 is naturally present.

Proteases or enzymes in general can be prepared by various methods, e.g. For example, targeted genetic modification by mutagenesis, further developed and for certain applications or specific properties, such as catalytic activity, stability, etc., to be optimized. Changes in the nucleotide sequence, as can be brought about, for example, by molecular biological methods known per se, are accordingly termed mutations. Depending on the nature of the change, for example, deletion, insertion or substitution mutations or those in which different genes or parts of genes are shuffled together; these are gene mutations. The associated organisms are called mutants. The proteins derived from mutant nucleic acids are called variants. Thus, for example, deletion, insertion, substitution mutations or fusions lead to deletion, insertion, substitution mutated or fusion genes and at the protein level to corresponding deletion, insertion or substitution variants or fusion proteins. The strategy of introducing targeted point mutations into the known molecules, for example to improve the washing performance of proteases, for example subtilisins, is also referred to as rational protein design. A similar performance improvement strategy is to change the surface charges and / or the isoelectric point of the molecules and, above that, their interactions with the substrate. Thus, for example, the net charge of the subtilisins can be changed via point mutations in order to influence the substrate binding, in particular for use in detergents and cleaners. Another, and in particular complementary, strategy is to increase the stability of the proteases in question and thereby increase their effectiveness. Stabilization via coupling to a polymer is for proteases for cosmetics, for example, in the patent US 5230891 described; it is associated with a better skin tolerance. In contrast, stabilizers by point mutations are more common, especially for detergents and cleaners.

A modern direction of enzyme development is to combine elements from known, related proteins via statistical methods into new enzymes with previously unattainable properties. Such methods are also summarized under the generic term Directed Evolution. These include, for example, the following methods: the StEP method ( Zhao et al. (1998), Nat. Biotechnol., Vol. 16, pp. 258-261 ), Random priming recombination ( Shao et al., (1998), Nucleic Acids Res., Vol. 26, pp. 681-683 ), DNA shuffling ( Stemmer, WPC (1994), Nature, Vol. 370, pp. 389-391 ) or RACHITT ( Coco, WM et al. (2001), Nat. Biotechnol., Vol. 19, pp. 354-359 ). Another shuffling method called recombining ligation reaction (RLR) is described in US Pat WO 00/09679 A1 described.

For the description of point mutations that exactly one amino acid position affect (amino acid exchanges), the following convention applied: first, the natural existing amino acid in the form of the internationally used Denotes one-letter codes, then follows the associated sequence position and finally the inserted amino acid. Several exchanges within the same polypeptide chain are performed Slashes separated.

It It is also well known in the art that advantageous properties of individual mutations, eg. B. individual Point mutations, can complement. One regarding certain properties already optimized protease, for example in terms of their stability to surfactants or other components, according to the invention additionally be further developed.

Under Fragments are understood to mean all proteins or peptides that are smaller are as natural proteins and, for example, also synthetic can be obtained. Due to their amino acid sequences can they are assigned to the relevant complete proteins become. For example, you can assume the same structures or proteolytic activities or partial activities exercise, such as the complexation of a substrate. Fragments and deletion variants of starting proteins are in principle similar; while fragments are rather smaller fragments lacking deletion mutants tend to lack only short regions, and thus only individual subfunctions.

Under chimeric or hybrid proteins are within the meaning of the present invention To understand such proteins whose sequence sequences the sequences or partial sequences of at least two parent proteins. The source proteins may look like this different or from the same organism. chimera or hybrid proteins, for example, by recombination mutagenesis to be obtained. The purpose of such recombination can be, for example It consists of using the fused protein part of a induce or induce certain enzymatic function modify. It is immaterial in the context of the present invention, whether such a chimeric protein from a single polypeptide chain or several subunits, to which differ Distribute functions.

Under proteins obtained by insertion mutation are such variants to understand that by inserting a protein fragment were obtained in the starting sequences. They are their principal similarity because of the chimeric proteins. They differ of them only in the size ratio of unchanged protein part to size of the entire protein. In such insertionsmutierten proteins the proportion of foreign protein is lower than in chimeric Proteins.

Inversion, So a partial sequence reversal, as a special form both the deletion, as well as the insertion. The same thing applies to one of the original amino acid sequence differing regrouping of different parts of the molecule. It can be used both as deletion variant, as insertion variant, as also as a shuffling variant of the original protein be considered.

Under Derivatives are for the purposes of the present application, such proteins understood, the pure amino acid chain chemically modified has been. Such derivatizations can be, for example biological in the context of protein biosynthesis by the Host cell done. For this purpose, molecular biological Methods are used. You can also do it chemically be carried out, for example by the chemical transformation a side chain of an amino acid or by covalent Binding of another compound to the protein. With such a Compound can also be, for example, other proteins, for example, bifunctional chemical compounds be bound to proteins of the invention. Such modifications may include, for example, substrate specificity or affect the bond strength to the substrate or a temporary block of enzymatic activity cause, if it is at the coupled substance is an inhibitor. This can be for example the period of storage be useful. Likewise, under derivatization covalent attachment to a macromolecular carrier as well as a noncovalent inclusion in suitable macromolecular cage structures.

a Another object of the invention thus represents a protease, which is characterized in that it consists of a Protease is obtainable as a parent molecule by fragmentation, deletion, Insertion or substitution mutagenesis and an amino acid sequence which covers a length of at least 300 and more preferably at least 290, 280, 270, 260, 250, 240, 230, 220, 210, 200, 190, 180, 170, 160, 150, 140, 130, 120, 110, 100, 90, 80, 70, 60 and 50 contiguous amino acid positions matches the parent molecule.

Thus, for example, it is possible to delete individual amino acids at the termini or in the loops of the enzyme without thereby losing the proteolytic activity. Such mutations are for example in WO 99/49057 A1 described. WO 01/07575 A2 teaches that such deletions lower the allergenicity of proteases involved, and thus their overall usefulness can be improved. Fragmentation benefits the insertion or substitution mutagenesis aspect outlined below and / or possible fusion with other enzymes. With regard to the intended use of these enzymes, it is particularly preferred if they also have a proteolytic activity after fragmentation or deletion mutagenesis.

Numerous prior art documents disclose beneficial effects of insertions and substitutions in subtilases; including the publications WO 99/49057 A1 and WO 01/07575 A2 , In principle, this also includes single substitutions of amino acids, but it can also be several contiguous amino acids exchanged for others. This also includes recombinations of larger enzyme sections, such as the above-mentioned fragments, with other proteases or proteins of a different function. For example, it is based on WO 99/57254 A1 it is possible to provide a protein of the invention or parts thereof via peptidic linkers or directly as a fusion protein with binding domains of other proteins, such as the cellulose-binding domain, thereby making the hydrolysis of the substrate more effective. Likewise, proteins according to the invention can also be linked with amylases or cellulases, for example, in order to perform a dual function.

A further subject of the invention is a protease, which is characterized in that it is obtainable from a protease according to the invention as the starting molecule and has one or more amino acid substitutions in positions which correspond to the positions 3, 4, 36, 42, 47, 56, 61 , 69, 87, 96, 99, 101, 102, 104, 114, 118, 120, 130, 139, 141, 142, 154, 157, 188, 193, 199, 205, 211, 224, 229, 236, 237 , 242, 243, 255 and 268 of the Bacillus lentus alkaline protease according to SEQ ID NO. 4 are assigned in an alignment. The amino acid positions are determined here by an alignment of the amino acid sequence of a protease according to the invention with the amino acid sequence of the alkaline protease from Bacillus lentus, as described in SEQ ID NO. 4 is assigned. In this way, so-called homologous positions certainly. An example of such an alignment is in 1 specified.

A final confirmation in the assignment of homologous positions, ie in particular their functional correspondence, can ultimately only provide comparative experiments, according to which the two positions assigned to each other on the basis of an alignment in both compared proteases are point mutated in the same way and observed whether in both the enzymatic activity is changed in the same way. For example, when an amino acid substitution in a particular position of the B. lentus alkaline protease (BLAP) is accompanied by an increase in K _M or other enzymatic parameter, the same shift in K _M value tends to be observed in a protease variant of the invention. whose amino acid exchange has been achieved by the same amino acid introduced, the confirmation of this aspect of the invention is to be seen herein.

In the said positions are in the wild-type molecule of the For example, lentus alkaline protease has the following amino acid residues: S3, V4, S36, N42, A47, T56, G61, T69, E87, A96, R99, A101, I102, S104, N114, H118, A120, S130, S139, T141, S142, S154, S157, A188, V193, V199, G205, L211, A224, K229, S236, N237, N242, H243, N255 or T268.

There in addition to the alkaline protease from Bacillus licheniformis the B. lentus alkaline protease in the art is an important reference molecule to describe new proteases and point mutations and the new proteases described herein, and thus their sequence hitherto unknown, it seems advantageous in the assignment of the point mutations on the count of the alkaline protease Bacillus lentus reference. Furthermore, the count depends generally after the mature (mature) protein. Advantageous positions for sequence changes, for example by Point mutations, the alkaline protease from Bacillus lentus, that transmit to homologous positions of the proteases of the invention are of importance and the protease advantageous functional Lend properties are given below.

From the registration WO 92/21760 A1 single and multiple variants of the subtilisin from Bacillus lentus DSM 5483 are evident in the following positions: 3, 4, 36, 42, 47, 56, 69, 87, 96, 101, 102, 104, 114, 118, 120, 130, 139 , 141, 142, 157, 188, 193, 199, 205, 224, 229, 236, 237, 242, 243, 255 and 268. The application WO 95/23221 A1 additionally discloses exchanges of this molecule in positions 99, 154 and 211, in particular R99G, R99A, R99S, S154D, S154E, L211D and 1211E. Such variants are suitable for registration WO 95/07770 A1 especially for use in cosmetics. In addition to other exchange is in the registration WO 02/088340 A2 also described the replacement L211G, and in WO 03/038082 A2 the exchange G61A. Of these, accordingly preferred are those in which the further amino acid substitutions in one or more of the positions 3, 4, 61, 188, 193, 199 and 211 are present. Among these, according to what has been stated above, those which are one or more of the amino acid substitutions 3T, 4I, 61A, 188P, 193M, 199I and 211D or 211G are again preferred, provided that the corresponding homologous positions are not already naturally of one of these preferred amino acids be taken.

The exchanges S3T and V4I lead, in particular in WO 02/088340 A2 is likely to have a stabilizing effect on the molecule to improve its contribution to the washing performance of a detergent or cleaning agent.

One Another object of the invention is a protease described above, which is additionally stabilized, in particular by coupling to a polymer.

For an increase in the stability during storage and / or during use, for example during the washing process means that their activity lasts longer and is thus enhanced in the effect. Possible stabilization options are all strategies described in the prior art and suitable strategies, for example according to FIG US 5230891 the covalent coupling to a polymer.

Alternatively, those stabilizations are also suitable which are possible by means of point mutagenesis of the molecule itself (and because of the sequence differences already fall under the embodiments described above). Because these stabilizations require after the protein recovery no further steps. Some point mutations suitable for this purpose are known per se from the prior art. So can according to US 6087315 and US 6110884 Proteases are stabilized by replacing certain tyrosine residues with others.

• – Veränderung der Bindung von Metallionen, insbesondere der Calcium-Bindungsstellen, beispielsweise gemäß der Lehre der Anmeldungen WO 88/08028 A1 und WO 88/08033 A1 ; gemäß der ersten dieser Schriften müßten eine oder mehrere der an der Calcium-Bindung beteiligten Aminosäure-Reste gegen negativ geladene Aminosäuren ausgetauscht werden; gemäß der Lehre der Anmeldung WO 88/08033 müßten zur Stabilisierung über die Calcium-Bindung gleichzeitig in mindestens einer der Folgen der beiden Reste Arginin/Glycin Punktmutationen eingeführt werden;
• – Gemäß dem Patent US 5453372 können Proteine durch bestimmte Mutationen auf der Oberfläche gegen den Einfluß von denaturierenden Agentien wie Tensiden geschützt werden.

Other options include:

• - Modification of the binding of metal ions, in particular the calcium binding sites, for example according to the teaching of the applications WO 88/08028 A1 and WO 88/08033 A1 ; according to the first of these documents, one or more of the amino acid residues involved in the calcium binding would have to be exchanged for negatively charged amino acids; according to the teaching of the application WO 88/08033 For stabilization via the calcium binding, point mutations would have to be introduced simultaneously in at least one of the sequences of the two residues arginine / glycine;
• - According to the patent US 5453372 For example, proteins may be protected against the influence of denaturing agents such as surfactants by certain surface mutations.

Another way to stabilize against elevated temperature and the action of surfactants would be in application of the teaching WO 92/21760 A1 . WO 02/088340 A2 and WO 03/038082 A2 the stabilization through the exchange of amino acids that are close to the N-terminus, against those that presumably come into contact with the rest of the molecule via non-covalent interactions and thus contribute to the maintenance of the globular structure.

Preferred embodiments are those in which the molecule is stabilized in several ways. For example, after WO 89/09819 A1 It can be assumed that several stabilizing mutations have an additive or synergistic effect.

a Another object of the invention provides a protease as above described, which is characterized in that they at least has a chemical modification. A protease with such a Change is also called derivative, i. H. the Protease is derivatized.

Under Derivatives are therefore understood as meaning those proteins which are replaced by a additional modification from the executed Proteins are obtained. This is preferably a chemical modification of the invention Proteins. Such modifications may be, for example stability, substrate specificity or binding strength to the substrate or the enzymatic activity. They can also serve to increase the allergenicity and / or to reduce immunogenicity of the protein and for example, to increase its skin tolerance.

Such Derivatizations, in particular chemical modifications, can for example, by biological means, such as in context with protein biosynthesis by the producing host organism. Here are couplings of low molecular weight compounds such as lipids or oligosaccharides.

However, derivatizations can also be carried out chemically, for example by the chemical transformation of a side chain or by covalent bonding of another, for example macromolecular, compound to the protein. Such a chemical modification is for example in the application DE 4013142 A1 described. For example, the coupling of amines to carboxyl groups of an enzyme to change the isoelectric point goes out WO 95/26398 A1 out. For example, macromolecules such as proteins, for example via bifunctional chemical compounds, can be bound to proteins according to the invention. So it is for example in application of the doctrine of WO 99/57154 A1 it is possible to provide a protein according to the invention also with a specific binding domain via a nonprotein linker. Such derivatives are particularly suitable for use in detergents or cleaners. Analogous WO 00/01831 A2 Protease inhibitors can also be linked to the proteins according to the invention via linkers, in particular amino acid linkers. Couplings with other macromolecular compounds such as polyethylene glycol improve the molecule in terms of other properties such as stability or skin compatibility as already explained above.

Derivatives of proteins according to the invention can in the broadest sense also be understood to mean preparations of these enzymes. Depending on the extraction, processing or preparation, a protein may be associated with various other substances, for example from the culture of the producing microorganisms. A protein may also have been deliberately added to certain other substances, for example to increase its storage stability. Therefore, all preparations of a protein according to the invention are also according to the invention. This is also independent of whether or not it actually exhibits this enzymatic activity in a particular preparation. Because it may be desired that it has no or only low activity during storage, and unfolds its proteolytic function only at the time of use. This can be controlled, for example, via appropriate accompanying substances. In particular, the joint preparation of proteases with protease inhibitors is advantageous and known from the prior art ( WHERE 00/01826 A2 ).

The Solution of a subtask and thus an independent task Subject of the invention form nucleic acid molecules, that for a protease according to the invention encode as well as vectors containing such a nucleic acid.

Under Nucleic acids are within the meaning of the present application naturally constructed from nucleotides as information carriers serving for the linear molecules Code amino acid sequence in proteins or enzymes. she can be as a single strand, as one to this single strand complementary single strand or as a double strand. As the naturally more permanent information carrier the nucleic acid DNA for molecular biological Works preferred. In contrast, for the Realization of the invention in natural environment, such as for example, in an expressing cell, an RNA is formed, which is why essential RNA molecules also embodiments of the present invention.

at DNA is the sequence of both complementary strands to be considered in all three possible reading frames. It should also be noted that different codon triplets can code for the same amino acids, so that a certain amino acid sequence of several different and possibly low identity containing nucleotide sequences can be derived, what as Degeneracy of the genetic code is called. Furthermore Different organisms have differences in the use of these codons on. For these reasons, both amino acid sequences must as well as nucleotide sequences in the consideration of the scope be included. Therefore, all nucleotide sequences are included in the invention, one of the above-described Encode oxidases. The skilled person is able to determine these nucleotide sequences beyond doubt, because despite the Degeneracy of the genetic code defined individual codons Amino acids are assigned. Therefore, the skilled artisan starting one of each is just as an example coding for to look at a particular amino acid sequence.

The a protein corresponding information unit is also in the sense referred to as the gene of the present application.

A person skilled in the art can use well-known methods such as chemical synthesis or the polymerase chain reaction (PCR) in combination with molecular biological and / or proteinchemical standard methods, using known DNA and / or amino acid sequences, the corresponding nucleic acids to complete genes manufacture. Such methods are for example Sambrook, J., Fritsch, EF and Maniatis, T. 2001. Molecular cloning: a laboratory manual, 3rd Edition Cold Spring Laboratory Press. known.

amendments the nucleotide sequence, as known for example by per se molecular biological methods can be brought about, are called mutations. Depending on the type of change knows For example, deletion, insertion or substitution mutations or those involving different genes or parts of genes with each other fused or recombined; these are gene mutations. The associated organisms are called mutants. The proteins derived from mutant nucleic acids become referred to as variants. For example, deletion, Insertion substitution mutations or fusions to deletion, insertion-substitution-mutated or fusion genes and at the protein level to corresponding deletion, insertion or substitution variants, or fusion proteins.

• a) Nukleinsäuresequenz, die zu der in SEQ ID NO. 1 angegebenen Nukleinsäuresequenz in einem Teilstück von mindestens 300 zusammenhängenden Nukleotiden mindestens zu 59% identisch ist
• b) Nukleinsäuresequenz, die zu der in SEQ ID NO. 1 angegebenen Nukleinsäuresequenz in den Positionen 343 bis 1269 mindestens zu 59% identisch ist
• c) Nukleinsäuresequenz, die zu der in SEQ ID NO. 1 angegebenen Nukleinsäuresequenz mindestens zu 59% identisch ist.

In a preferred embodiment of the invention, the nucleic acid molecule which codes for a protease according to the invention is characterized in that it comprises a nucleic acid sequence which is selected from the group consisting of

• a) Nucleic acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 nucleic acid sequence in a portion of at least 300 contiguous nucleotides is at least 59% identical
• b) Nucleic acid sequence corresponding to the amino acid sequence shown in SEQ ID NO. 1 at positions 343 to 1269 is at least 59% identical
• c) Nucleic acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 nucleic acid sequence is at least 59% identical.

In further embodiments of the invention, the nucleic acid molecule is characterized in that it comprises a nucleic acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated nucleic acid sequence in a portion of increasingly preferably 400, 500, 600, 700, 800, 900, 1000, 1100 contiguous nucleic acid residues is at least 59% identical.

In In another embodiment of the invention, the nucleic acid molecule is that for a protease according to the invention encoded, characterized in that it is a nucleic acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated nucleic acid sequence in a section of at least 300 contiguous Nucleotides increasingly preferably at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5%, and most preferably is 100% identical.

In Further embodiments of the invention is the nucleic acid molecule, that for a protease according to the invention encoded, characterized in that it is a nucleic acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated nucleic acid sequence in a portion of increasingly preferred 400, 500, 600, 700, 800, 900, 1000, 1100 contiguous nucleic acid residues increasingly preferably at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% and most preferably 100% identical is.

In a preferred embodiment of the invention is that Nucleic acid molecule, which is responsible for a Protease encoded, characterized in that it is a nucleic acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated nucleic acid sequence in positions 343 to 1269, increasingly preferably at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% and especially preferably 100% identical. With these positions is as above explained the area meant for the mature (mature), that is also for the active protein coded. Also the stop codon is included, because its existence makes sure that not a bigger, possibly no longer functional, unwanted fusion protein is formed. Thus, when cloning is to pay attention that at this point there is also a stop codon, if not specifically induced via the C-terminus, a protein fusion shall be. Should later turn out that the Mature protein is formed only from part of this sequence is, the scope of protection applies accordingly for this Part.

In Another embodiment of the invention is the nucleic acid molecule characterized in that it is a nucleic acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated nucleic acid sequence increasingly preferably at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% and most preferably 100% identical is.

Prefers are such nucleic acids that are mature for mature Encode proteins, and increasingly preferred are those for increasingly active variants of the invention Encode proteins.

Farther preferred are those nucleic acids of which one or preferably several codons have been replaced by synonymous codons are.

This Aspect refers to the heterologous expression of the subject Proteases. So every organism, especially every production strain, has over a certain codon usage. This can lead to bottlenecks come in protein biosynthesis when acting on the transgenic nucleic acid lying codons in the host cell of a comparatively small Face number of loaded tRNAs. Synonyms Codons encode, however, for the same amino acids and can be better translated depending on the host. This possibly necessary rewriting thus depends of the choice of the expression system.

Especially for samples from unknown, possibly non-cultivable organisms an appropriate adjustment may be necessary.

The present invention involves the production of recombinant proteins. According to the invention, these are to be understood as meaning all genetic engineering or microbiological processes which are based on the genes for the proteins of interest being introduced into a suitable host cell for the production and being transcribed and translated by it. Suitably, the introduction of the relevant genes via vectors, in particular expression vectors; but also those that cause the gene of interest in the host cell to be inserted into an already existing genetic element, such as the chromosome or other vectors. The functional unit of gene and promoter and any other genetic elements is referred to as expression cassette according to the invention. But she does not have to necessarily also exist as a physical entity.

Under For the purposes of the present invention, vectors are made from nucleic acids existing elements understood as the characteristic nucleic acid region contain a gene of interest. You can do this in one species or cell line over several generations or to establish cell divisions as a stable genetic element. Vectors, especially when used in bacteria, are special plasmids, so circular genetic elements. There is a difference in genetic engineering on the one hand between such vectors, the storage and thus to a certain extent also serve the genetic engineering work, the so-called cloning vectors, and on the other hand those which the Function, the gene of interest in the host cell to realize, that is, the expression of the relevant Enable protein. These vectors are called expression vectors designated.

in the The present invention relates to the nucleic acid suitably cloned into a vector. The molecular biological Dimension of the invention thus consists in vectors with the genes for the corresponding proteins. This can, for example those that are different from bacterial plasmids, from viruses or derived from bacteriophages, or predominantly synthetic Vectors or plasmids with elements of various origins. With the other genetic elements that are available Vectors, in the respective host cells over several Generations as stable units. It is thereby irrelevant in the context of the invention, whether they are extrachromosomal establish as own units or integrate into a chromosome. Which of the numerous known from the prior art systems is chosen, depends on the individual case. decisive For example, the achievable copy number used for Available selection systems, including above all Antibiotic resistance, or the cultivability of the for admission the vectors are capable host cells.

The Vectors form suitable starting points for molecular biology and biochemical studies of the gene or its associated Proteins and for further developments of the invention and ultimately for amplification and production according to the invention Proteins. They represent insofar embodiments of the present Invention, as the sequences of the invention contained Nucleic acid regions each within the above closer designated homology regions are.

a Another object of the invention thus represent vectors that contain at least one nucleic acid molecule, which for a protease according to the invention encodes, in particular a nucleic acid molecule, as described above. In a further embodiment invention, the vector is characterized in that the vector a cloning vector or an expression vector. cloning vectors are in addition to storage, biological amplification or Selection of the gene of interest for characterization of the gene in question, such as the creation of a restriction map or the sequencing. Cloning vectors are also preferred Embodiments of the present invention because they a transportable and storable form of the claimed Represent DNA. They are also preferred starting points for molecular biology techniques that are not bound to cells, such as for example, the polymerase chain reaction.

expression vectors are chemically similar to cloning vectors but in those subsequences that enable them in the host cells optimized for the production of proteins or To replicate host organisms and there the gene for expression bring to. Preferred embodiments are expression vectors, which themselves carry the genetic elements necessary for expression. The expression is influenced, for example, by promoters, which regulate the transcription of the gene. So the expression by the natural, originally before this Gene localized promoter done, but also after genetic engineering Fusion by both provided on the expression vector Promoter of the host cell as well as by a modified or a completely different promoter of another organism or another host cell.

preferred Embodiments are those expression vectors that undergo changes the culture conditions or addition of certain compounds, such as for example cell density or special factors, regulatable are. Expression vectors allow the associated Protein heterologous, so in another cell or host cell as the one from which it is naturally derived can, is produced. The cells can be quite belonging to different organisms or of different ones Come from organisms. Also a homologous protein recovery from a the gene naturally expressing host cell an appropriate vector is within the scope of the present invention Invention.

These may have the advantage of being natural, with translation related modification reactions on the resulting Protein can be carried out the same way as it naturally would expire.

A further embodiment represent expression systems, in which additional genes, such as those that be provided on other vectors that Influence production of proteins according to the invention. These may be modifying gene products or to those with the protein of the invention be cleaned together, about its enzymatic function to influence. These may be, for example, other proteins or enzymes to inhibitors or to act on such elements influence the interaction with different substrates.

alternative Embodiments of the present invention may be also be cell-free expression systems involving protein biosynthesis understood in vitro. Such expression systems are available the technique also established.

One Another object of the invention is a non-human host cell, a protease of the invention or a fragment of the same or which are encouraged to produce them can, preferably using an expression vector. The in vivo synthesis an enzyme according to the invention, ie by living cells, requires the transfer of the associated Gene into a host cell, their so-called transformation. As host cells In principle, all cells are suitable, that is prokaryotic or eukaryotic cells. Preferred are such host cells, the be genetically advantageous to handle what, for example the transformation with the expression vector and its stable Establishment, for example, unicellular fungi or bacteria. In addition, preferred host cells are characterized by a good microbiological and biotechnological manageability. That concerns for example easy cultivability, high growth rates, low requirements on fermentation media and good production and secretion rates for foreign proteins. Often need to out The abundance of different according to the state of the art available standing systems the optimal expression systems for determine the individual case experimentally. Each invention Protein can in this way from a multiplicity of host cells be won. Also, such host cells are preferred by the that after transformation with one of them have been obtained as described above. It can For example, be cloning vectors for storage and / or modification, for example in any bacterial strain or another host cell according to the invention introduced have been. Such steps are in storage and further development genetic elements. Because of these Host cells transfer the relevant genetic elements into subsequent, immediately transferred to the expression of suitable host cells can be, are the same with the previous ones Transformation products to realizations of the subject invention.

preferred Embodiments illustrate such host cells that are due to genetic regulatory elements, for example, on the expression vector be made available, but also from the outset may be present in these cells, in their activity are adjustable. For example, by controlled addition of chemical compounds that serve as activators, by amendment the cultivation conditions or when a certain Cell density, these can be excited for expression. This allows a very economical production of proteins of interest.

preferred Host cells are prokaryotic or bacterial cells. bacteria are usually distinguished from eukaryotes shorter generation times and lower demands to the cultivation conditions. This can be cost effective Method for obtaining proteins according to the invention established become. In Gram-negative bacteria, such as Escherichia coli (E. coli), are a variety of proteins in the periplasmic Space secreted, so in the compartment between the two Cells enclosing membranes. This can be for special applications be beneficial. Gram-positive bacteria, such as Bacilli or Actinomycetes or other representatives the Actinomycetales, in contrast, have no external Membrane so that secreted proteins readily enter the cells surrounding nutrient medium are released from which according to a further preferred embodiment, the expressed purify proteins according to the invention directly to let.

preferred dimensions the host cell is therefore characterized by being the protein of the invention or a fragment or derivative thereof secreted into the surrounding medium. A further subject of the invention thus provide host cells which are characterized in that they are the protease or a Fragment of the same secrete into the host cell surrounding medium.

In Another preferred embodiment is the invention Host cell characterized in that it is a bacterium, in particular one which is selected from the group of genera of Escherichia, Klebsiella, Bacillus, Staphylococcus, Corynebacterium, Arthrobacter, Streptomyces, Stenotrophomonas and Pseudomonas.

Especially Preferably, the host cell is a bacterium which is selected from the group of Escherichia coli, Klebsiella planticola, Bacillus licheniformis, Bacillus lentus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus alcalophilus, Bacillus globigii gibsonii, Bacillus pumilus, Staphylococcus carnosus, Corynebacterium glutamicum, Arthrobacter oxidans, Streptomyces lividans, Streptomyces coelicolor and Stenotrophomonas maltophilia.

The Host cells can meet their requirements the cultural conditions have changed, others or additional Have selection markers or other or additional Express proteins. It may in particular be such host cells acting in addition to the protein produced according to the invention even more, especially economically interesting proteins express.

The However, the host cell can also be a eukaryotic cell that is characterized characterized in that it has a nucleus. Another one The invention therefore provides a host cell which is characterized characterized in that it has a nucleus.

In contrast to prokaryotic cells, eukaryotic cells are capable of post-translationally modifying the protein formed. Examples thereof are fungi such as Actinomycetes or yeasts such as Saccharomyces or Kluyveromyces. This may be particularly advantageous, for example, if the proteins are to undergo specific modifications in the context of their synthesis that enable such systems. Modifications that eukaryotic systems perform, especially in connection with protein synthesis, include, for example, the binding of low molecular weight compounds such as membrane anchors or oligosaccharides. Such oligosaccharide modifications may be desirable, for example, to reduce allergenicity. Also, coexpression with the enzymes naturally produced by such cells, such as cellulases, may be advantageous. Thermophilic fungal expression systems are described, for example, in WO 96/02653 A1 presented. Such are particularly suitable for the expression of temperature-resistant variants.

The Host cells according to the invention are in themselves cultivated and fermented in a known manner, for example in discontinuous or continuous systems. In the first case will be a suitable one Nutrient medium inoculated with the host cells and the product after an experimentally determined period of time from the medium harvested. Continuous fermentations are characterized by reaching a steady state in which over a relatively long-term cells partly die off but regrow and simultaneously remove product from the medium can be.

fermentation process are known per se from the prior art and represent the actual large-scale technical Production step, usually followed by a suitable one Purification method of the product produced, for example of the recombinant protein. All fermentation methods based on one of the above-mentioned processes for the preparation of based recombinant proteins, make corresponding preferred Embodiments of this subject invention is.

in this connection must be used for the manufacturing processes used, for the host cells and / or the proteins to be produced each optimal conditions based on the previously optimized culture conditions of the strains concerned, according to the knowledge of the person skilled in the art, for example, fermentation volume, media composition, Oxygen supply or stirrer speed experimental be determined.

Fermentation process, which are characterized in that the fermentation over An inflow strategy is also implemented into consideration. Here are the media components, by the continuous cultivation are consumed, fed; One also speaks of a feeding strategy. hereby can bring significant increases in both the Cell density, as well as in the dry biomass and / or especially the Activity of the protein of interest can be achieved.

Analogous In addition, the fermentation can also be designed so that unwanted Metabolites filtered out or by adding buffer or each appropriate counterions are neutralized.

The produced protein can be harvested subsequently from the fermentation medium. This Fermentation process is preferred over dry matter product processing, but requires the provision of suitable secretion markers and transport systems. Without secretion u. U. the purification of the protein from the cell mass required, and various methods are known as precipitation z. B by ammonium sulfate or ethanol, or the chromatographic purification, if necessary to homogeneity. However, the majority of the described technical methods should manage with an enriched, stabilized preparation.

All Already executed above elements can be used to process be combined to proteins of the invention manufacture. It is for each invention Protein a variety of possible combinations Process steps conceivable. The optimal procedure must be for be determined experimentally for each specific case.

By Expression or cloning can be the invention Proteases in the required for technical use Amount to be made available.

a independent subject of the invention thus also provide Process for the preparation of an inventive Protease

To Every method that comes to making a top belongs described protease invention suitable or that is the receipt of an inventive Protease allows. These include, for example also chemical synthesis methods.

In contrast, however, all of those known in the art are preferred above in some aspects already mentioned molecular biological, microbiological or biotechnological production processes, the invention referred to above Build up proteins or nucleic acids. Therefor can according to the above, for example, in the sequence listing under SEQ ID NO. 1 specified nucleic acid or from this obtained mutants or partial sequences are used.

Preferably these are procedures that are made using a previously designated nucleic acid, preferably using a as described above, and more preferably using a previously designated, advantageously genetically modified host cell done. Because this is the corresponding preferred genetic information in microbiologically utilizable Form provided.

embodiments The present invention can be described on the basis of associated nucleic acid sequences also cell-free Expression systems in which protein biosynthesis in vitro is traced. All elements already listed above can also be combined to new methods to inventive Produce proteins. It is for each invention Protein a variety of possible combinations Process steps conceivable, so that optimal process for must be determined experimentally for each specific case.

Corresponding the above, such methods are still among the methods mentioned preferred in which the nucleotide sequence in one, preferably several codons have been adapted to the codon usage of the host strain is.

a own subject of the invention represents a means by that characterized in that it is at least one inventive Protease as described above contains.

This includes all types of compositions, especially mixtures, formulations, solutions, etc., the utility of which is improved by addition of a protein of the invention described above, within the scope of the present invention. Depending on the field of application, these may be, for example, solid mixtures, for example powders with freeze-dried or encapsulated proteins, or gel or liquid agents. Preferred formulations contain, for example, buffer substances, stabilizers, reaction partners and / or cofactors of the proteases and / or other ingredients synergistic with the proteases. In particular, this appropriation is to be understood as the areas of application set out below. Further fields of application emerge from the prior art and are described, for example, in US Pat Handbook "Industrial Encyclopedia and their Applications" by H. Uhlig, Wiley-Verlag, New York, 1998 shown.

In preferred embodiments of the invention is an inventive Agent characterized in that it contains a detergent, hand detergent, Dishwashing liquid, hand dishwashing detergent, dishwasher detergent, Cleaning agents, denture or contact lens care products, Rinsing agent, disinfectant, cosmetic, pharmaceutical agent or a means of treating filter media, Textiles, furs, paper, skins or leather, is.

this Subject of the invention are as preferred embodiment Attributed to funds that are detergents or cleaners is.

Because as in the embodiments of the present application was shown, could use for detergents and cleaners a preferred protease according to the invention a Performance increase over a protease-free agent be noted and a very good cleaning performance in terms on protease-sensitive stains can be achieved.

To this invention includes all conceivable types of detergents, both concentrates and undiluted agents, for use on a commercial scale, in the washing machine or at the hand laundry or cleaning. This includes For example, detergents for textiles, carpets, or Natural fibers for which according to the present invention Label detergent is used. These include, for example also dishwashing detergents for dishwashers or manual dishwashing detergent or cleaner for hard surfaces such as metal, glass, porcelain, ceramics, Tiles, stone, painted surfaces, plastics, wood or leather; for such is according to the present invention the term used cleaning agent.

One Means according to the invention can be both an agent for bulk consumers or technical users as also be a product for the private consumer, whereby all types of detergents and cleaning agents established in the prior art also embodiments of the present invention represent. These include, for example, concentrates and undiluted agent for use in commercial Scale, in the washing machine or in the hand wash or cleaning. Likewise, for example, include detergents for textiles, carpets, or natural fibers, for the term detergent according to the present invention is used. Furthermore, this includes, for example Dishwashing liquid for dishwashers or manual dishwashing detergent or cleaner for hard surfaces such as metal, glass, porcelain, ceramics, Tiles, stone, painted surfaces, plastics, wood or leather; for such is according to the present invention the term used cleaning agent.

embodiments The present invention includes all established and / or all appropriate dosage forms. These include For example, solid, powdered, liquid, gelatinous or pasty agents, if necessary can also consist of several phases as well as in compressed or uncompressed form. Another one The subject of the invention therefore represents means which are characterized are that they are present as a one-component system. Such means preferably consist of one phase. Of course However, agents according to the invention can also consist of several phases. Another subject of the invention form therefore means characterized by being in several Components are split. To the invention Dosage forms also include extrudates, granules, Tablets or pouches, both in bulk containers as may also be packaged in portions. Prefers an agent according to the invention is characterized that it contains the protease in an amount of 2 μg to 20 mg, preferably from 5 μg to 17.5 mg, more preferably from 20 μg to 15 mg and most preferably from 50 μg to 10 mg per g of the agent.

invention Agents may be in solid form. Another one The invention therefore relates to agents which are characterized are that they are in solid form. In a preferred embodiment the agent is a free-flowing powder with a bulk density from 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l, before.

alternative agents according to the invention can also be liquid or be pasty. Another object of the invention the agent is therefore characterized in that it is pasty or liquid form, in particular in the form of a non-aqueous liquid detergent or a non-aqueous paste or in the form of a aqueous liquid detergent or a hydrous paste.

The agent according to the invention, in particular washing or cleaning agent, can be packaged in a container, preferably an air-permeable container, from which it is released shortly before use or during the washing process; in particular, the protease and / or further ingredients of the co coated with a substance impermeable to the enzyme at room temperature or in the absence of water, which becomes permeable to the enzyme under conditions of use of the agent. The agent 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.

Compositions according to the invention may contain only one protease. Alternatively, they may also contain other proteases or other enzymes in a concentration effective for the effectiveness of the agent. A further subject of the invention thus represents agents which further comprise one or more further enzymes, wherein in principle all enzymes established in the prior art for these purposes can be used. Other enzymes which can be used as further enzymes are all enzymes which can display catalytic activity in the agent according to the invention, in particular proteases, amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, .beta.-glucosidases, carrageenases, oxidases, oxidoreductases or lipases, and preferably their mixtures. These enzymes are basically of natural origin; Starting from the natural molecules, improved variants are available for use in detergents and cleaners, which are preferably used accordingly. ^{Compositions according} to the invention preferably contain enzymes in total amounts of 1 × 10 ^-8 to 5 percent by weight based on active protein. Preferably, the enzymes are from 0.001 to 5% by weight, more preferably from 0.01 to 5% by weight, even more preferably from 0.05 to 4% by weight and most preferably from 0.075 to 3.5% by weight. % contained in agents according to the invention, wherein each enzyme contained can be present in the stated proportions.

The protein concentration can be determined by known methods, for example the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method ( Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 ). The further enzymes particularly preferably support the effect of the agent, for example the cleaning performance of a washing or cleaning agent, with regard to certain stains or stains. Particularly preferably, the enzymes show synergistic effects with respect to their action against certain stains or stains, ie the enzymes contained in the middle composition mutually support each other in their cleaning performance. Synergistic effects can occur not only between different enzymes, but also between one or more enzymes and other ingredients of the composition according to the invention. In a further preferred embodiment of the invention, the agent according to the invention is therefore characterized in that it contains at least one further enzyme which comprises a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, β-glucosidase, carrageenase, oxidase, oxidoreductase or a lipase.

The enzymes used in agents according to the invention are either originally from microorganisms, about genera Bacillus, Streptomyces, Humicola, or Pseudomonas, and / or are used according to known biotechnological processes produced by suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or by filamentous Fungi.

In agents according to the invention is the inventive Protease, for example, with one or more of the following Ingredients combined: nonionic, anionic and / or cationic Surfactants, (optionally further) bleaching agents, bleach activators, Bleach catalysts, builders and / or cobuilders, acids, alkaline Substances, hydrotropes, solvents, thickeners, sequestering agents, Electrolytes, optical brighteners, grayness inhibitors, corrosion inhibitors, in particular silver protectants (silver corrosion inhibitors), soil release agents, Color transfer (or transfer) inhibitors, foam inhibitors, Abrasives, dyes, fragrances, perfumes, antimicrobial Active ingredients, UV protectants or absorbents, antistatic agents, pearlescing agents and skin protection agents, enzymes such as protease, amylase, Cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, β-glucosidase, Carrageenase, oxidase, oxidoreductase or a lipase, stabilizers, in particular enzyme stabilizers, and other components made up known in the art. In a further embodiment The invention is an agent according to the invention thus characterized in that it is at least one further component contains, selected from the group consisting of Surfactants, builders, acids, alkaline substances, hydrotropes, Solvents, thickeners, bleaches, dyes, Perfumes, corrosion inhibitors, sequestering agents, electrolytes, optical brighteners, grayness inhibitors, silver corrosion inhibitors, Color transfer inhibitors, foam inhibitors, abrasives, UV absorbers, solvents, antistatic agents, pearlescing agents and skin protection products.

The ingredients to be selected as well as the conditions under which the agent is used, such as temperature, pH, ionic strength, redox ratios or mechanical influences, should be used for the respective cleaning problem be optimized. For example, normal temperatures for detergents and cleaners range from 10 ° C for manual agents above 40 ° C and 60 ° C up to 95 ° for mechanical or technical applications. Since the temperature is usually infinitely adjustable in modern washing machines and dishwashers, all intermediate stages of the temperature are included. Preferably, the ingredients of the respective agents are coordinated. Synergies in terms of cleaning performance are preferred. Particularly preferred in this regard are synergies which are present in a temperature range between 20.degree. C. and 60.degree. C., since the protease contained in the agents according to the invention is catalytically active in this temperature range.

• – 5 Gew.-% bis 70 Gew.-%, insbesondere 5 Gew.-% bis 30 Gew.-% Tenside und/oder
• – 10 Gew.-% bis 65 Gew.-%, insbesondere 12 Gew.-% bis 60 Gew.-% wasserlösliches oder wasserdispergierbares anorganisches Buildermaterial und/oder
• – 0,5 Gew.-% bis 10 Gew.-%, insbesondere 1 Gew.-% bis 8 Gew.-%, wasserlösliche organische Buildersubstanzen und/oder
• – 0,01 bis 15 Gew.-% feste anorganische und/oder organische Säuren beziehungsweise 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 a further preferred embodiment, an agent according to the invention, in particular a washing or cleaning agent, furthermore comprises

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

optional the agent may further comprise optical brighteners. The optical Brighteners are preferably used from 0.01 to 5% by weight.

The protease activity in such agents may be as described in U.S. Pat Surfactants, Vol. 7 (1970), pp. 125-132 method described. It is accordingly stated in PE (protease units).

at comparing the performance of two detergent enzymes, such as in the examples of the present application, must between distinguished from the same and the same activity become. Especially when genetically engineered, largely free of side activity Preparations the same protein use is appropriate. Because that is a statement about whether it is possible the same amount of protein - as a measure of the yield of fermentative production - comparable Results. Gap the respective conditions from active substance to total protein (the values of the specific activity) apart, so is an activity-same comparison too recommend because this is the respective enzymatic properties be compared. Generally speaking, a low specific Activity by adding a larger one Protein amount can be compensated. This is ultimately for an economic consideration.

a own subject invention represents the use of an above-described agent according to the invention for the removal of protease-sensitive Soiling on textiles or hard surfaces, d. H. for cleaning textiles or hard surfaces, represents.

Because Agents according to the invention can, in particular according to the properties described above, used for this purpose be proteinaceous of textiles or hard surfaces Eliminate impurities. Provide embodiments for example, hand washing, manual removal of patches of textiles or of hard surfaces or the use in connection with a machine process represents.

In a preferred embodiment of this use the relevant agents according to the invention, preferably Washing or cleaning agent, according to one of the above Embodiment provided.

a another own subject of the invention provide methods for cleaning textiles or hard surfaces in which at least in one of the method steps an inventive Medium is used. The procedure for cleaning textiles or hard surfaces is thus characterized that in at least one method step, an inventive Medium is applied.

These include both manual and mechanical processes, with mechanical processes being more precise as regards, for example, the quantities and exposure times used, are preferred.

method for the cleaning of textiles are generally characterized from that in several process steps different cleaning active Substances applied to the items to be cleaned and after the exposure time be washed off, or that the items to be cleaned in any other way with a detergent or a solution of this agent is treated. The same applies to procedures for cleaning of all materials other than textiles, which are covered by the term hard surfaces are summarized. All conceivable Washing or cleaning methods can be used in at least one the process steps to an inventive Means are enriched, and then provide embodiments of the present invention.

In Another preferred embodiment of such methods become the respective enzymes of the invention in the context of one of the above recipes for Composition according to the invention, preferably according to the invention Detergents or cleaning agents provided.

There preferred enzymes of the invention naturally already have a protein-dissolving activity and they also unfold in media, which otherwise no cleaning power own, such as in bare buffer, can single sub-step of such a method for machine Cleaning of textiles is that, if desired in addition to stabilizing compounds, salts or buffer substances as only cleaning-active component an inventive Enzyme is applied. This constitutes a particularly preferred embodiment of the present invention.

In Another embodiment of the invention is the method for cleaning textiles or hard surfaces therefore characterized in that in at least one method step a protease according to any one of claims 1 to 11 proteolytically is active. The protease is preferably used in an amount of 40 μg to 4 g, preferably from 50 μg to 3 g, more preferably from 100 μg to 2 g, and most preferably from 200 μg used up to 1 g per application.

preferred Embodiments of this subject invention provide Process for the treatment of textile raw materials or for textile care in which in at least one of the method steps an inventive Alkaline protease becomes active.

this includes are processes for textile raw materials, fibers or textiles preferred with natural ingredients, and especially for those with wool or silk.

It This may be, for example, processes in which materials prepared for processing in textiles, such as anti-fungal finishing, or, for example, methods which carried the cleaning Enrich textiles with a nourishing component. Because of the above described effect of proteases on natural, protein-containing Raw materials are in preferred embodiments to processes for the treatment of textile raw materials, fibers or textiles with natural ingredients, especially with wool or Silk.

invention Enzymes are as described above advantageous in agents according to the invention, in particular Detergents and cleaners, and processes, in particular washing and cleaning Cleaning method, can be used. You can use this be proteinaceous of textiles or hard surfaces Eliminate impurities. Provide embodiments for example, hand washing, manual removal of patches of textiles or of hard surfaces or the use in connection with a machine process represents.

a Another object of the invention is therefore the use of a protease according to the invention, as described above has been described for cleaning textiles or hard surfaces. Preferably, the protease is added in an amount of 40 μg 4 g, preferably from 50 μg to 3 g, more preferably from 100 μg to 2 g, and most preferably from 200 μg used up to 1 g per application.

In a preferred embodiment of this use the respective inventive alkaline Proteases in the context of one of the above formulations for agents according to the invention, preferably Detergents or cleaning agents provided.

A further embodiment of this subject invention provides the use of an alkaline according to the invention Protease for activating or deactivating ingredients of Detergents or cleaners.

As is known, protein components of detergents or cleaners can be inactivated by the action of a protease. To use this otherwise rather unwanted effect targeted, is an object of the present invention. Likewise, it is possible, as described above, that proteolysis activates another component, for example, if it is a hybrid protein of the actual enzyme and the corresponding inhibitor, as described, for example, in the application WO 00/01831 A2 has been disclosed. Another example of such regulation is that in which an active component for protection or control of its activity is encapsulated in a material which is attacked by proteolysis. Proteins of the invention can thus be used for inactivation, activation or release reactions, in particular in multiphase agents.

• – Die Verwendung einer erfindungsgemäßen Alkalischen Protease zur Gewinnung oder Behandlung von Rohmaterialien oder Zwischenprodukten in der Textilherstellung, insbesondere zum Entfernen von Schutzschichten auf Geweben;
• – die Verwendung einer erfindungsgemäßen Alkalischen Protease zur Behandlung von Textilrohstoffen oder zur Textilpflege und hierunter bevorzugt
• – die entsprechende Verwendung für Textilrohstoffe, Fasern oder Textilien mit natürlichen Bestandteilen und ganz besonders für solche mit Wolle oder Seide.

In accordance with the above, the following uses are embodiments of the present invention:

• The use of an alkaline protease according to the invention for the recovery or treatment of raw materials or intermediates in textile production, in particular for the removal of protective layers on fabrics;
• The use of an alkaline protease according to the invention for the treatment of textile raw materials or for textile care and among these are preferred
• - the corresponding use for textile raw materials, fibers or textiles with natural components and especially for those with wool or silk.

The The present invention is also in the form of such an inventive Alkaline protease-containing agents realized in which it is cosmetics. Below are all types of cleansing and nourishing agents for human skin or hair, especially cleansers.

Because proteases also play a crucial role in the cell renewal process of human skin (desquamation) ( T. Egelrud et al., Acta Derm. Venerol., Vol. 71 (1991), pp. 471-474 ). Accordingly, proteases are also used as bioactive components in skin care agents to aid in the breakdown of desmosome structures that are increased in dry skin. The use of subtilisin proteases with amino acid substitutions in the positions R99G / A / S, S154D / E and / or L211D / E for cosmetic purposes is described, for example, in US Pat WO 97/07770 A1 described. As explained in detail above, proteases according to the invention can be further developed via the corresponding point mutations. Thus, proteases according to the invention, in particular those which are controlled in their activity, for example after mutagenesis or by addition of corresponding substances interacting with them, are also suitable as active components in skin or hair cleansing or care preparations. Particular preference is given to those preparations of these enzymes which, as described above, for example by coupling to macromolecular carriers (cf. US 5230891 ) are stabilized and / or derivatized by point mutations at highly allergenic positions, so that they have a higher skin compatibility for humans.

Accordingly also appropriate cosmetic cleaning and care procedures and the use of such proteolytic enzymes in cosmetic Purposes included in this subject of the invention, in particular in appropriate means, such as shampoos, soaps or washing lotions, or in care products, for example, in the form of creams offered become. Also use in a peeling drug, or for its production is included in this claim.

• – die Verwendung einer erfindungsgemäßen Alkalischen Proteasen zur biochemischen Analyse oder zur Synthese von niedermolekularen Verbindungen oder von Proteinen;
• – darunter bevorzugt die Verwendung zur Endgruppenbestimmung im Rahmen einer Peptid-Sequenzanalyse;
• – die Verwendung einer erfindungsgemäßen Alkalischen Proteasen zur Präparation, Reinigung oder Synthese von Naturstoffen oder biologischen Wertstoffen, vorzugsweise im Rahmen entsprechender Mittel oder Verfahren;
• – die Verwendung einer erfindungsgemäßen Alkalischen Proteasen zur Synthese von Proteinen oder anderen niedermolekularen chemischen Verbindungen;
• – die Verwendung einer erfindungsgemäßen Alkalischen Proteasen zur Behandlung von natürlichen Rohstoffen, insbesondere zur Oberflächenbehandlung, ganz besonders in einem Verfahren zur Behandlung von Leder, vorzugsweise im Rahmen entsprechender Mittel oder Verfahren;
• – die Verwendung einer erfindungsgemäßen Alkalischen Proteasen zur Behandlung von photographischen Filmen, insbesondere zur Entfernung von gelatinhaltigen oder ähnlichen Schutzschichten; und
• – die Verwendung einer erfindungsgemäßen Alkalischen Proteasen zur Herstellung von Lebensmitteln oder von Futtermitteln.

In addition to the use in detergents and cleaners and cosmetics numerous applications of proteases, in particular subtilases are established in the prior art. An overview over this offers for example the Handbook "Industrial Encyclopedia and their Applications" by H. Uhlig, Wiley-Verlag, New York, 1998 , All of these techniques can be enriched according to the invention alkaline proteases. Should it turn out that they can be further developed by the use of proteases according to the invention, they are included in the scope of protection of the present invention. These include in particular the following fields of application:

• The use of an alkaline protease according to the invention for the biochemical analysis or for the synthesis of low molecular weight compounds or of proteins;
• - including preferred use for end-group determination in a peptide sequence analysis;
• The use of an alkaline protease according to the invention for the preparation, purification or synthesis of natural substances or biological valuable substances, preferably in the context of appropriate agents or processes;
• The use of an alkaline protease according to the invention for the synthesis of proteins or other low-molecular-weight chemical compounds;
• The use of an alkaline protease according to the invention for the treatment of natural raw materials, in particular for surface treatment, more particularly in a process for the treatment of leather, preferably in the context of appropriate agents or processes;
• The use of an alkaline protease according to the invention for the treatment of photographic films, in particular for the removal of gelatin-containing or similar protective layers; and
• The use of an alkaline protease according to the invention for the production of food or feed.

in principle becomes the use of alkaline according to the invention Proteases in all other technical fields in the protection area included in the present application for which it is turns out to be suitable.

The previously described inventive agent or those according to the invention described above Process prepared means may contain further Ingredients such as other enzymes, enzyme stabilizers, surfactants, z. Nonionic, anionic and / or amphoteric surfactants, and / or bleaches, and / or builder, and optionally further customary Ingredients, which are listed below.

builders

To the builders include in particular the zeolites, Silicates, carbonates, organic cobuilders and - where no ecological Prejudices against their use exist - even the phosphates.

The finely crystalline, synthetic and bound water-containing zeolite used is preferably zeolite A and / or P. As zeolite P, zeolite ^MAP® (commercial product from Crosfield) is particularly preferred. Also suitable, however, are zeolite X and mixtures of A, X and / or P. Commercially available and preferably usable in the context of the present invention is, for example, a cocrystal of zeolite X and zeolite A (about 80% by weight of zeolite X) ), by the formula n Na ₂ O • (1 - n) K ₂ O • Al ₂ O ₃ • (2 - 2.5) SiO ₂ • (3.5-5.5) H ₂ O can be described. The zeolite can be used both as a builder in a granular compound and for a kind of "powdering" of a granular mixture, preferably a mixture to be compressed, whereby usually both ways of incorporating the zeolite into the premix are used an average particle size of less than 10 microns (volume distribution, measuring method: Coulter Counter) and preferably contain 18 to 22 wt .-%, in particular 20 to 22 wt .-% of bound water.

Preference is given to using crystalline layer-form silicates of the general formula NaMSi _x O _{2x + 1} .yH ₂ O, where M is sodium or hydrogen, x is a number from 1.9 to 22, preferably from 1.9 to 4, with particularly preferred Values for x are 2, 3 or 4, and y is a number from 0 to 33, preferably from 0 to 20. The crystalline layer-form silicates of the formula NaMSi _x O _{2x + 1} .yH ₂ O are sold, for example, by the company Clariant GmbH (Germany) under the trade name Na-SKS. Examples of these silicates are 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 ₅ O ₁₇ .xH ₂ O) or Na-SKS-4 (Na ₂ Si ₄ O ₉ .xH ₂ O, Makatite).

Particularly suitable for the purposes of the present invention are crystalline phyllosilicates of the formula NaMSi _x O _{2x + 1} .yH ₂ O, in which x is 2. In particular, both β- and δ-sodium disilicates are Na ₂ Si ₂ O ₅ .yH ₂ O and also, above all, Na-SKS-5 (α-Na ₂ Si ₂ O ₅ ), Na-SKS-7 (β-Na ₂ Si ₂ O _5, natrosilite), Na-SKS-9 (NaHSi ₂ O ₅ · H ₂ O), Na-SKS-10 (NaHSi ₂ O ₅ · 3 H 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 ).

Detergents or cleaning agents preferably contain a weight fraction of the crystalline layered silicate of the formula NaMSi _x O _{2x + 1} .yH ₂ O of from 0.1 to 20% by weight, preferably from 0.2 to 15% by weight and in particular of 0.4 to 10 wt .-%, each based on the total weight of these agents.

It is also possible to use amorphous sodium silicates with a Na ₂ O: SiO ₂ modulus of from 1: 2 to 1: 3.3, preferably from 1: 2 to 1: 2.8 and in particular from 1: 2 to 1: 2.6, which preferably delayed release and Se have kundärwaschigenschaften. The dissolution delay compared with conventional amorphous sodium silicates may have been caused in various ways, for example by surface treatment, compounding, compaction / densification or by overdrying. In the context of this invention, the term "amorphous" is understood to mean that the silicates do not yield sharp X-ray reflections typical of crystalline substances in X-ray diffraction experiments, but at most one or more maxima of the scattered X-rays having a width of several degrees of diffraction angle , cause.

alternative or in combination with the aforementioned amorphous sodium silicates X-ray amorphous silicates are used whose silicate particles fuzzy or even sharp in electron diffraction experiments Provide diffraction maxima. This is to be interpreted as meaning that Products microcrystalline size ten up to several hundred nm, with values up to max. 50 nm and especially up to max. 20 nm are preferred. Such X-ray amorphous Silicates, also have a dissolution delay compared to conventional water glasses on. Particularly preferred are compacted / compacted amorphous Silicates, compounded amorphous silicates and overdried X-ray amorphous silicates.

in the Within the scope of the present invention, it is preferred that this (s) Silicate (s), preferably alkali metal silicates, particularly preferably crystalline or amorphous alkali disilicates, in detergents or cleaners in amounts of from 3 to 60% by weight, preferably from 8 to 50% by weight and in particular from 20 to 40 wt .-%, each based on the weight of the washing or cleaning agent are included.

Of course it is also possible to use the generally known phosphates as builders, if such use is not for environmental reasons should be avoided. Among the variety of commercially available Phosphates have the alkali metal phosphates, with particular preference of Pentasodium or pentakalium triphosphate (sodium or potassium tripolyphosphate) the largest in the detergents and cleaners industry Importance.

Alkali metal phosphates is the summary term for the alkali metal (especially sodium and potassium) salts of various phosphoric acids, in which one can distinguish metaphosphoric acids (HPO ₃ ) _n and orthophosphoric H ₃ PO _{4 in} addition to higher molecular weight representatives. The phosphates combine several advantages: they act as alkali carriers, prevent lime deposits on machine parts or lime incrustations in fabrics and also contribute to the cleaning performance.

Technically particularly important phosphates are the pentasodium triphosphate, Na ₅ P ₃ O ₁₀ (sodium tripolyphosphate) and the corresponding potassium salt pentapotassium triphosphate, K ₅ P ₃ O ₁₀ (potassium tripolyphosphate). The sodium potassium tripolyphosphates are also preferably used according to the invention.

Become in the context of the present application phosphates as washing or cleaning active Substances used in detergents or cleaners, so included preferred agents are said phosphate (s), preferably alkali metal phosphate (s), particularly preferably pentasodium or pentapotassium triphosphate (sodium or potassium tripolyphosphate), in amounts of 5 to 80 wt .-%, preferably from 15 to 75% by weight, in particular, from 20 to 70% by weight, respectively based on the weight of the washing or cleaning agent.

Further Builders are the alkali carriers. As alkali carrier For example, alkali metal hydroxides, alkali metal carbonates, Alkali metal bicarbonates, alkali metal sesquicarbonates, the mentioned alkali metal silicates, alkali metal silicates, and mixtures of aforementioned substances, wherein for the purposes of this invention preferably the Alkali carbonates, especially sodium carbonate, sodium bicarbonate or sodium sesquicarbonate. Especially preferred is a builder system containing a mixture of tripolyphosphate and Sodium. Because of their compared with other builders low chemical compatibility with the rest Ingredients of detergents or cleaners, the alkali metal hydroxides are preferred only in small amounts, preferably in amounts below 10% by weight, preferably below 6% by weight, more preferably below 4% by weight and in particular below 2 wt .-%, each based on the total weight of the washing or cleaning agent used. Especially preferred are means which, in relation to their total weight, are less than Contain 0.5 wt .-% and in particular no alkali metal hydroxides.

Particularly preferred is the use of carbonate (s) and / or bicarbonate (s), preferably alkali metal carbonate (s), more preferably sodium carbonate, in amounts of 2 to 50 wt .-%, preferably from 5 to 40 wt .-% and in particular from 7.5 to 30 wt .-%, each based on the weight of the washing or cleaning agent. Particularly preferred are agents which, based on the weight of the washing or Detergent less than 20 wt .-%, preferably less than 17 wt .-%, preferably less than 13 wt .-% and in particular less than 9 wt .-% of carbonate (s) and / or bicarbonate (s), preferably alkali metal carbonate ( e), particularly preferably sodium carbonate.

When Organic co-builders are in particular polycarboxylates / polycarboxylic acids, polymeric polycarboxylates, aspartic acid, polyacetals, Dextrins, other organic cobuilders (see below) and phosphonates to call. These classes of substances are described below.

useful Organic builders are, for example, those in Usable form of the free acid and / or its sodium salts Polycarboxylic acids, wherein among polycarboxylic acids Such carboxylic acids are understood to be more than one Wear acidity. For example, these are citric acid, Adipic acid, succinic acid, glutaric acid, malic acid, Tartaric acid, maleic acid, fumaric acid, sugar acids, Aminocarboxylic acids, nitrilotriacetic acid (NTA), provided such use for environmental reasons not to complain about, as well as mixtures of these. The free Acids typically also have, in addition to their builder effect the property of an acidifying component and thus serve also for setting a lower and milder pH of Detergents or cleaners. In particular, here are citric acid, Succinic acid, glutaric acid, adipic acid, Gluconic acid and any mixtures of these.

When Builders are further suitable polymeric polycarboxylates, These are, for example, the alkali metal salts of polyacrylic acid or polymethacrylic acid, for example those with a molecular weight of 500 to 70000 g / mol.

For the purposes of this document, the molecular weights stated for polymeric polycarboxylates are weight-average molar masses M _{w of} the particular acid form, which were determined in principle by means of gel permeation chromatography (GPC), a UV detector being used. The measurement was carried out against an external polyacrylic acid standard, which provides realistic molecular weight values due to its structural relationship with the polymers investigated. These data differ significantly from the molecular weight data, in which polystyrene sulfonic acids are used as standard. The molar masses measured against polystyrenesulfonic acids are generally significantly higher than the molecular weights specified in this document.

suitable Polymers are in particular polyacrylates, which preferably have a molecular weight from 2000 to 20,000 g / mol. Because of their superior Solubility can turn out of this group the short-chain polyacrylates, the molecular weights of 2,000 to 10,000 g / mol, and more preferably from 3000 to 5000 g / mol, be preferred.

Suitable are furthermore copolymeric polycarboxylates, especially those of Acrylic acid with methacrylic acid and acrylic acid or methacrylic acid with maleic acid. As special suitable copolymers of acrylic acid with maleic acid proven, the 50 to 90 wt .-% acrylic acid and 50 to 10 Wt .-% maleic acid. Your molecular weight, based on free acids, is generally 2000 to 70000 g / mol, preferably 20,000 to 50,000 g / mol and in particular 30,000 to 40,000 g / mol.

The (co) polymeric polycarboxylates can be used either as a powder or used as an aqueous solution. The content of detergents or cleaning agents on (co) polymeric polycarboxylates is preferably 0.5 to 20 wt .-%, in particular 3 to 10% by weight.

to The water solubility can be improved Polymers also allylsulfonic acids such as allyloxybenzenesulfonic acid and methallylsulfonic acid, as a monomer.

Especially Biodegradable polymers of more than two are also preferred various monomer units, for example, those as monomers Salts of acrylic acid and maleic acid and vinyl alcohol or vinyl alcohol derivatives or the salts of acrylic acid as monomers and the 2-alkylallylsulfonic acid and sugar derivatives.

Further preferred copolymers are those which are used as monomers acrolein and Acrylic acid / acrylic acid salts or acrolein and vinyl acetate exhibit.

As well as further preferred builder substances are polymeric aminodicarboxylic acids, to mention their salts or their precursors. Especially Polyaspartic acids or their salts are preferred.

Further Suitable builders are polyacetals, which by reaction of dialdehydes with polyolcarboxylic acids, which are 5 to 7 C atoms and at least 3 hydroxyl groups can be obtained. Preferred polyacetals are selected from dialdehydes such as glyoxal, glutaraldehyde, Terephthalaldehyde and mixtures thereof and from Polyolcarbonsäuren such as gluconic acid and / or glucoheptonic acid.

Further suitable organic builders are dextrins, for example Oligomers or polymers of carbohydrates by partial Hydrolysis of starches can be obtained. The hydrolysis can be carried out by customary, for example acidic or enzyme-catalyzed processes. Preferably, they are hydrolysis products with middle Molar masses in the range of 400 to 500,000 g / mol. This is a polysaccharide with a dextrose equivalent (DE) in the range of 0.5 to 40, in particular from 2 to 30 preferred, DE being a common Measure of the reducing effect of a polysaccharide compared to dextrose, which has a DE of 100. Useful are both maltodextrins with a DE between 3 and 20 and dry glucose syrups with a DE between 20 and 37 as well as so-called yellow dextrins and white dextrins with higher molecular weights in the range from 2000 to 30,000 g / mol.

at the oxidized derivatives of such dextrins are their reaction products with oxidants, which are able are at least one alcohol function of the saccharide ring to the carboxylic acid function to oxidize.

Also Oxydisuccinates and other derivatives of disuccinates, preferably Ethylenediamine disuccinate are other suitable cobuilders. there ethylenediamine-N, N'-disuccinate (EDDS) is preferably used in the form of its sodium or magnesium salts used. Further preferred are in this Also related glycerol disuccinates and glycerol trisuccinates. Suitable amounts are zeolithhaltigen and / or silicate-containing Formulations at 3 to 15 wt .-%.

Further useful organic cobuilders are, for example, acetylated Hydroxycarboxylic acids or their salts, which optionally may also be present in Lactonform and which at least 4 carbon atoms and at least one hydroxy group and maximum contain two acid groups.

About that In addition, all connections that are able to To form complexes with alkaline earth ions, as builders be used.

to Group of surfactants are the nonionic, the anionic, the cationic and the amphoteric surfactants counted.

As nonionic surfactants, it is possible to use all nonionic surfactants known to the person skilled in the art. Suitable nonionic surfactants are, for example, alkyl glycosides of the general formula RO (G) _x in which R is a primary straight-chain or methyl-branched, in particular 2-methyl-branched aliphatic radical having 8 to 22, preferably 12 to 18 carbon atoms and G is the symbol which is a glycose unit having 5 or 6 C atoms, preferably glucose. The degree of oligomerization x, which indicates the distribution of monoglycosides and oligoglycosides, is any number between 1 and 10; preferably x is 1.2 to 1.4.

A another class of preferred nonionic surfactants, the 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 having 1 to 4 carbon atoms in the alkyl chain.

Also nonionic surfactants of the amine oxide type, for example N-cocoalkyl-N, N-dimethylamine oxide and N-tallow alkyl-N, N-dihydroxyethylamine oxide, and the fatty acid alkanolamide may be suitable. The amount of these nonionic surfactants is preferably not more than that of the ethoxylated Fatty alcohols, especially not more than half of them.

in der R für einen aliphatischen Acylrest mit 6 bis 22 Kohlenstoffatomen, R¹ für Wasserstoff, einen Alkyl- oder Hydroxyalkylrest mit 1 bis 4 Kohlenstoffatomen und [Z] für einen linearen oder verzweigten Polyhydroxyalkylrest mit 3 bis 10 Kohlenstoffatomen und 3 bis 10 Hydroxylgruppen steht. Bei den Polyhydroxyfettsäureamiden handelt es sich um bekannte Stoffe, die üblicherweise durch reduktive Aminierung eines reduzierenden Zuckers mit Ammoniak, einem Alkylamin oder einem Alkanolamin und nachfolgende Acylierung mit einer Fettsäure, einem Fettsäurealkylester oder einem Fettsäurechlorid erhalten werden können.Further suitable surfactants are polyhydroxy fatty acid amides of the formula

wherein R is an aliphatic acyl radical having 6 to 22 carbon atoms, R ^{1 is} hydrogen, an alkyl or hydroxyalkyl radical having 1 to 4 carbon atoms and [Z] is a linear or branched polyhydroxyalkyl radical having 3 to 10 carbon atoms and 3 to 10 hydroxyl groups. In the polyhydroxy fatty acid amides These are known substances which can usually be obtained by reductive amination of a reducing sugar with ammonia, an alkylamine or an alkanolamine and subsequent acylation with a fatty acid, a fatty acid alkyl ester or a fatty acid chloride.

in der R für einen linearen oder verzweigten Alkyl- oder Alkenylrest mit 7 bis 12 Kohlenstoffatomen, R¹ für einen linearen, verzweigten oder zyklischen Alkylrest oder einen Arylrest mit 2 bis 8 Kohlenstoffatomen und R² für einen linearen, verzweigten oder zyklischen Alkylrest oder einen Arylrest oder einen Oxy-Alkylrest mit 1 bis 8 Kohlenstoffatomen steht, wobei C_1-4-Alkyl- oder Phenylreste bevorzugt sind und [Z] für einen linearen Polyhydroxyalkylrest steht, dessen Alkylkette mit mindestens zwei Hydroxylgruppen substituiert ist, oder alkoxylierte, vorzugsweise ethoxylierte oder propxylierte Derivate dieses Restes.The group of polyhydroxy fatty acid amides also includes compounds of the formula

R is a linear or branched alkyl or alkenyl radical having 7 to 12 carbon atoms, R ^{1 is} a linear, branched or cyclic alkyl radical or an aryl radical having 2 to 8 carbon atoms and R ^{2 is} a linear, branched or cyclic alkyl radical or an aryl radical or an oxyalkyl radical having 1 to 8 carbon atoms, with C _1-4 alkyl or phenyl radicals being preferred and [Z] being a linear polyhydroxyalkyl radical whose alkyl chain is substituted by at least two hydroxyl groups, or alkoxylated, preferably ethoxylated or propoxylated Derivatives of this residue.

[Z] is preferably by reductive amination of a reduced sugar obtained, for example, glucose, fructose, maltose, lactose, galactose, Mannose or xylose. The N-alkoxy or N-aryloxy-substituted Compounds can be prepared by reaction with fatty acid methyl esters in the presence of an alkoxide as a catalyst in the desired Polyhydroxyfatty acid amides are transferred.

Low-foaming nonionic surfactants are used as preferred surfactants. With particular preference, washing or cleaning agents, in particular automatic dishwashing detergents, contain nonionic surfactants from the group of the alkoxylated alcohols. The nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, in particular primary, alcohols having preferably 8 to 18 carbon atoms and on average 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 linear and methyl-branched radicals in the mixture can contain, as they are usually present in Oxoalkoholresten. In particular, however, alcohol ethoxylates with linear radicals of alcohols of native origin having 12 to 18 carbon atoms, for. From coconut, palm, tallow or oleyl alcohol, and on average from 2 to 8 moles of EO per mole of alcohol. The preferred ethoxylated alcohols include, for example, C _12-14 alcohols with 3 EO or 4 EO, C _9-11 alcohols with 7 EO, C _13-15 alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C _12-18 alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, 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 averages, which may correspond to a particular product of an integer or a fractional number. 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 include tallow fatty alcohol with 14 EO, 25 EO, 30 EO or 40 EO.

Particular preference is therefore given to ethoxylated nonionic surfactants consisting of C _6-20 monohydroxyalkanols or C _6-20 alkylphenols or C _16-20 fatty alcohols and more than 12 mol, preferably more than 15 mol and in particular more than 20 mol of ethylene oxide per mol Alcohol was used. A particularly preferred nonionic surfactant is obtained from a straight-chain fatty alcohol having 16 to 20 carbon atoms (C _16-20 alcohol), preferably a C ₁₈ -alcohol and at least 12 mol, preferably at least 15 mol and especially at least 20 mol of ethylene oxide. Of these, the so-called "narrow range ethoxylates" are particularly preferred.

With Particular preference continues to be combinations of one or several tallow fatty alcohols with 20 to 30 EO and silicone defoamers used.

Especially preferred are nonionic surfactants which have a melting point above Have room temperature. Nonionic surfactant (s) having a melting point above 20 ° C, preferably above 25 ° C, more preferably between 25 and 60 ° C and in particular between 26.6 and 43.3 ° C, is / are particularly preferred.

Suitable nonionic surfactants which have melting or softening points in the temperature range mentioned are, for example, low-foaming nonionic surfactants which may be solid or highly viscous at room temperature. If nonionic surfactants are used which are highly viscous at room temperature, it is preferred that they have a viscosity above 20 Pa · s, preferably above 35 Pa · s and in particular above 40 Pa · s. Also nonionic surfactants, the waxy consistency at room temperature be are preferred, depending on their intended use.

nonionic surfactants from the group of alkoxylated alcohols, particularly preferably from the group of mixed alkoxylated alcohols and in particular from the group of EO-AO-EO-Niotenside, are also with special Preference used.

The nonionic surfactant solid at room temperature preferably has propylene oxide units in the molecule. Preferably, such PO units make up at 25% by weight, more preferably up to 20% by weight and in particular up to 15% by weight of the total molecular weight of the nonionic surfactant out. Particularly preferred nonionic surfactants are ethoxylated Monohydroxyalkanols or alkylphenols which additionally contain polyoxyethylene-polyoxypropylene Have block copolymer units. The alcohol or alkylphenol content such nonionic surfactant molecules preferably makes more as 30 wt .-%, more preferably more than 50 wt .-% and in particular more than 70 wt .-% of the total molecular weight of such nonionic surfactants. Preferred agents are characterized by being ethoxylated and propoxylated nonionic surfactants containing the propylene oxide units in the molecule up to 25% by weight, preferably up to 20% by weight and in particular up to 15 wt .-% of the total molecular weight of the nonionic Make up surfactants.

Prefers Surfactants to be used come from the groups of the alkoxylated Nonionic surfactants, in particular the ethoxylated primary alcohols and mixtures of these surfactants structurally complicated Surfactants such as polyoxypropylene / polyoxyethylene / polyoxypropylene ((PO / EO / PO) surfactants). Such (PO / EO / PO) nonionic surfactants are also outstanding by good foam control.

Further particularly preferred nonionic surfactants with melting points above room temperature contain from 40 to 70% of a polyoxypropylene / polyoxyethylene / polyoxypropylene block polymer blend, the 75% by weight of a reverse block copolymer of polyoxyethylene and polyoxypropylene with 17 moles of ethylene oxide and 44 moles of propylene oxide and 25% by weight of a block copolymer of polyoxyethylene and polyoxypropylene, initiated with trimethylolpropane and containing 24 moles of ethylene oxide and 99 moles of propylene oxide per mole of trimethylolpropane.

bevorzugt, in der R¹ für einen geradkettigen oder verzweigten, gesättigten oder ein- bzw. mehrfach ungesättigten C_6-24-Alkyl- oder -Alkenylrest steht; jede Gruppe R² bzw. R³ unabhängig voneinander ausgewählt ist aus -CH₃, -CH₂CH₃, -CH₂CH₂-CH₃, CH(CH₃)₂ und die Indizes w, x, y, z unabhängig voneinander für ganze Zahlen von 1 bis 6 stehen.In the context of the present invention, particularly preferred nonionic surfactants have been low foaming nonionic surfactants which have alternating ethylene oxide and alkylene oxide units. Among these, in turn, surfactants with EO-AO-EO-AO blocks are preferred, wherein in each case one to ten EO or AO groups are bonded to each other before a block of the other groups follows. Here are nichionic surfactants of the general formula

in which R ^{1 is} a straight-chain or branched, saturated or mono- or polyunsaturated C _6-24 alkyl or alkenyl radical; each group R ² or R ^{3 is} independently selected from -CH ₃ , -CH ₂ CH ₃ , -CH ₂ CH ₂ -CH ₃ , CH (CH ₃ ) ₂ and the indices w, x, y, z independently stand for integers from 1 to 6.

The preferred nonionic surfactants of the above formula can be prepared by known methods from the corresponding alcohols R ¹ -OH and ethylene or alkylene oxide. The radical R ¹ in the above formula may vary depending on the origin of the alcohol. When native sources are used, the radical R ^{1 has} an even number of carbon atoms and is usually unbranched, the linear radicals being selected from alcohols of native origin having 12 to 18 C atoms, eg. B. from coconut, palm, tallow or oleyl alcohol, are preferred. Alcohols which are accessible from synthetic sources are, for example, the Guerbet alcohols or methyl-branched or linear and methyl-branched radicals in the 2-position, as they are usually present in oxo alcohol radicals. Irrespective of the type of alcohol used to prepare the nonionic surfactants contained in the compositions, preference is given to nonionic surfactants in which R ¹ in the above formula is an alkyl radical having 6 to 24, preferably 8 to 20, particularly preferably 9 to 15 and in particular 9 to 11 Carbon atoms.

As the alkylene oxide unit which is contained in the preferred nonionic surfactants in alternation with the ethylene oxide unit, in particular butylene oxide is considered in addition to propylene oxide. But also other alkylene oxides in which R ² or R ^{3 are} independently selected from -CH ₂ CH ₂ -CH ₃ or CH (CH ₃ ) ₂ are suitable. Preference is given to using nonionic surfactants of the above formula in which R ² or R ^{3 is} a residue -CH ₃ , w and x independently of one another for values of 3 or 4 and y and z independently of one another for values of 1 or 2 stand.

In summary, particularly preferred are nonionic surfactants having a C _9-15 alkyl group having 1 to 4 ethylene oxide units followed by 1 to 4 propylene oxide units followed by 1 to 4 ethylene oxide units followed by 1 to 4 propylene oxide units. These surfactants have the required low viscosity in aqueous solution and can be used according to the invention with particular preference.

Surfactants of the general formula R ¹ -CH (OH) CH ₂ O- (AO) _w - (A'O) _x - (A''O) _y - (A''O) _z -R ² , in which R ¹ and R ² independently of one another represent a straight-chain or branched, saturated or mono- or polyunsaturated C _2-40 -alkyl or -alkenyl radical; A, A ', A''andA''' are independently of one another a radical from the group -CH ₂ CH ₂ , -CH ₂ CH ₂ -CH ₂ , -CH ₂ -CH (CH ₃ ), -CH ₂ - CH _{2 is} -CH ₂ -CH ₂ , -CH ₂ -CH (CH ₃ ) -CH ₂ -, -CH ₂ -CH (CH ₂ -CH ₃ ); and w, x, y and z are values between 0.5 and 90, where x, y and / or z can also be 0 are preferred according to the invention.

Preference is given in particular to those end-capped poly (oxyalkylated) nonionic surfactants which are of 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 is linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 2 to 30 carbon atoms, preferably having 4 to 22 carbon atoms, further having a linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radical R2 Have from 1 to 30 carbon atoms, wherein x stands for values between 1 and 90, preferably for values between 40 and 80 and in particular for values between 40 and 60.

Particularly preferred are 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 is} a linear or branched aliphatic hydrocarbon radical having 4 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 is a value of at least 15.

Particular preference is furthermore given to those end-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 independently of one another are 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 are values between 1 and 32, wherein nonionic surfactants with R ³ = -CH ₃ and values for x of 15 to 32 and y of 0.5 and 1.5 are very particularly preferred.

Other preferred nonionic surfactants are the end-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 are} linear or branched, saturated or unsaturated, aliphatic or aromatic hydrocarbon radicals having 1 to 30 carbon atoms, R ^{3 is} H or a methyl, ethyl, n-propyl, iso-propyl, n- Butyl, 2-butyl or 2-methyl-2-butyl radical, x are values between 1 and 30, k and j are values between 1 and 12, preferably between 1 and 5. When 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 may 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, with radicals having 8 to 18 carbon atoms being particularly preferred. For the Rest R ³ are H, -CH ₃ or -CH ₂ CH ₃ 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. As a result, the alkylene oxide unit in the square bracket can be varied. For example, when x is 3, the radical R ³ can be selected to form ethylene oxide (R ³ = H) or propylene oxide (R ³ = CH ₃ ) units which may be joined in any order, for example (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 selected here by way of example and may well be greater, with the variation width increasing with increasing x values and including, for example, a large number (EO) groups combined with a small number (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 zu R ¹ O [CH ₂ CH (R ³ ) O] _x CH ₂ CH (OH) CH ₂ OR ² simplified. In the latter formula, R ¹ , R ² and R ^{3 are} as defined above and x is from 1 to 30, preferably from 1 to 20 and in particular from 6 to 18. Particularly preferred are surfactants in which the radicals R ¹ and R ^{2 has} 9 to 14 C atoms, R ^{3 is} H and x assumes values of 6 to 15.

The specified C chain lengths and Ethoxylierungsgrade or Alkoxylation of the aforementioned nonionic surfactants provide statistical Mean values that for a particular product a whole or a fractional number. Due to the manufacturing process For the most part, commercial products of the formulas mentioned do not exist an individual representative, but of mixtures, resulting in for both the C chain lengths and for the degrees of ethoxylation or degrees of alkoxylation averages and resulting in fractional numbers.

Of course Not only can the aforementioned nonionic surfactants as individual substances, but also as surfactant mixtures of two, three, four or more surfactants are used. As surfactant mixtures are not mixtures of nonionic surfactants, in their entirety under one of the above general Formulas, but rather such mixtures, the two, three, contain four or more nonionic surfactants, which are different the above general formulas can be described.

As anionic surfactants, for example, those of the sulfonate type and sulfates are used. The surfactants of the sulfonate type are preferably C _9-13 -alkylbenzenesulfonates, olefinsulfonates, ie mixtures of alkene and hydroxyalkanesulfonates and disulfonates, as are obtained, for example, from C _12-18 -monoolefins having terminal or internal double bonds by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acid hydrolysis of the sulfonation products into consideration. Also suitable are alkanesulfonates which are obtained from C _12-18 alkanes, for example by sulfochlorination or sulfoxidation with subsequent hydrolysis or neutralization. Likewise, the esters of α-sulfo fatty acids (ester sulfonates), z. As the α-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids suitable.

Further Suitable anionic surfactants are sulfated fatty acid glycerol esters. Among fatty acid glycerol esters are the mono-, di- and triesters As well as their mixtures to understand, as in the production through Esterification of a monoglycerine with 1 to 3 moles of fatty acid or in the transesterification of triglycerides with 0.3 to 2 moles of glycerol to be obtained. Preferred sulfated fatty acid glycerol esters are the sulfonation of saturated fatty acids with 6 to 22 carbon atoms, for example caproic acid, Caprylic acid, capric acid, myristic acid, Lauric acid, palmitic acid, stearic acid or behenic acid.

Alk (en) ylsulfates are the alkali metal salts and in particular the sodium salts of the sulfuric monoesters of C ₁₂ -C ₁₈ fatty alcohols, for example coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or the C ₁₀ -C ₂₀ oxo alcohols and those half-esters of secondary alcohols of these chain lengths are preferred. Also preferred are alk (en) ylsulfates of said chain length, which contain a synthetic, produced on a petrochemical basis straight-chain alkyl radical, which have an analogous degradation behavior as the adequate compounds based on oleochemical raw materials. Of washing technology interest, the C ₁₂ -C ₁₆ alkyl sulfates and C ₁₂ -C ₁₅ alkyl sulfates and C ₁₄ -C ₁₅ alkyl sulfates are preferred. The 2,3-alkyl sulfates, which as commercial products from Shell Oil Company under the name DAN ^® he are suitable anionic surfactants.

The sulfuric acid monoesters of straight-chain or branched C _7-21 -alcohols ethoxylated with from 1 to 6 mol of ethylene oxide, such as 2-methyl-branched C _9-11- alcohols having on average 3.5 mol of ethylene oxide (EO) or C _12-18 . Fatty alcohols with 1 to 4 EO are suitable. Due to their high foaming behavior, they are only used in detergents in relatively small amounts, for example in amounts of from 1 to 5% by weight.

Further suitable anionic surfactants are also the salts of alkylsulfosuccinic acid, which are also referred to as sulfosuccinates or as sulfosuccinic acid esters and which are monoesters and / or diesters of sulfosuccinic acid with alcohols, preferably fatty alcohols and in particular ethoxylated fatty alcohols. Preferred sulfosuccinates contain C _8-18 fatty alcohol residues or mixtures of these. Particularly preferred sulfosuccinates contain a fatty alcohol residue derived from ethoxylated fatty alcohols, which by themselves are nonionic surfactants. Sulfosuccinates, whose fatty alcohol residues are derived from ethoxylated fatty alcohols with a narrow homolog distribution, are again particularly preferred. Likewise, it is also possible to use alk (en) ylsuccinic acid having preferably 8 to 18 carbon atoms in the alk (en) yl chain or salts thereof.

When other anionic surfactants are especially soaps into consideration. Suitable are 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 from natural fatty acids, z. As coconut, palm kernel or tallow, derived Soap mixtures.

The anionic surfactants including soaps can in the form of their sodium, potassium or ammonium salts and as soluble Salts of organic bases, such as mono-, di- or triethanolamine, are present. The anionic surfactants are preferably in the form of their sodium or potassium salts, especially in the form of the sodium salts.

At Position of said surfactants or in conjunction with them it is also possible to use cationic and / or amphoteric surfactants.

worin jede Gruppe R¹ unabhängig voneinander ausgewählt ist aus C_1-6-Alkyl-, -Alkenyl- oder -Hydroxyalkylgruppen; jede Gruppe R² unabhängig voneinander ausgewählt ist aus C_8-28-Alkyl- oder -Alkenylgruppen; R³ = R¹ oder (CH₂)_n-T-R²; R⁴ = R¹ oder R² oder (CH₂)_n-T-R²; T = -CH₂-, -O-CO- oder -CO-O- und n eine ganze Zahl von 0 bis 5 ist.As cationic active substances, for example, cationic compounds of the following formulas can be used:

wherein each R ^{1 group is} independently selected from C _1-6 alkyl, alkenyl or hydroxyalkyl groups; each R ^{2 group is} independently selected from C _8-28 alkyl or alkenyl groups; R ³ = R ¹ or (CH ₂ ) _n -TR ² ; R ⁴ = R ¹ or R ² or (CH ₂ ) _n -TR ² ; T = -CH ₂ -, -O-CO- or -CO-O- and n is an integer from 0 to 5.

In automatic dishwashing detergents, is the Content of cationic and / or amphoteric surfactants preferably less than 6% by weight, preferably less than 4% by weight, very particularly preferably less than 2% by weight and in particular less than 1% by weight. Machine dishwashing detergents which are not cationic or amphoteric surfactants are particularly preferred.

polymers

to Group of polymers include in particular the washing or cleaning-active polymers, for example the rinse aid polymers and / or as softeners effective polymers. Generally are in detergents or cleaners in addition to nonionic polymers also cationic, anionic and amphoteric polymers can be used.

"Cationic Polymers "in the context of the present invention are polymers which carry a positive charge in the polymer molecule. This can for example, by (alkyl) ammonium groups present in the polymer chain or other positively charged groups. Especially preferred cationic polymers are from the groups of the quaternized Cellulose derivatives containing polysiloxanes with quaternary groups, the cationic guar derivatives, the polymeric dimethyldiallylammonium salts and their copolymers with esters and amides of acrylic acid and methacrylic acid, the copolymers of vinylpyrrolidone with quaternized derivatives of dialkylamino acrylate and methacrylate, the vinylpyrrolidone-methoimidazolinium chloride copolymer, the quaternized Polyvinyl alcohols or under the INCI names Polyquaternium 2, Polyquaternium 17, Polyquaternium 18 and Polyquaternium 27 Polymers.

"Amphoteric Poylmere "within the meaning of the present invention, in addition to a positively charged group in the polymer chain also continues to be negative charged groups or monomer units. In these groups These may be, for example, carboxylic acids, sulfonic acids or phosphonic acids.

Preferred washing or cleaning agents, in particular preferred automatic dishwashing agents, are characterized in that they contain a polymer a) which has monomer units of the formula R ¹ R ² C =CR ³ R ⁴ in which each R ¹ , R ² , R ⁴ radical ³ , R ^{4 is} independently selected from hydrogen, derivatized hydroxy, C _1-30 linear or branched alkyl groups, aryl, aryl substituted C _1-30 linear or branched alkyl groups, polyalkoxylated alkyl groups, heteroatomic organic groups having at least one positive charge without charged nitrogen , at least one quaternized nitrogen atom or at least one amino group having a positive charge in the partial range of the pH range of 2 to 11, or salts thereof, with the proviso that at least one radical R ¹ , R ² , R ³ , R ^{4 is} a heteroatomic organic group having at least one positive charge without charged nitrogen, at least one quaternized N atom or at least one Aminogr uppe with a positive charge is.

bei der R¹ und R⁴ unabhängig voneinander für H oder einen linearen oder verzweigten Kohlenwasserstoffrest mit 1 bis 6 Kohlenstoffatomen steht; R² und R³ unabhängig voneinander für eine Alkyl-, Hydroxyalkyl-, oder Aminoalkylgruppe stehen, in denen der Alkylrest linear oder verzweigt ist und zwischen 1 und 6 Kohlenstoffatomen aufweist, wobei es sich vorzugsweise um eine Methylgruppe handelt; x und y unabhängig voneinander für ganze Zahlen zwischen 1 und 3 stehen. X repräsentiert ein Gegenion, vorzugsweise ein Gegenion aus der Gruppe Chlorid, Bromid, Iodid, Sulfat, Hydrogensulfat, Methosulfat, Laurylsulfat, Dodecylbenzolsulfonat, p-Toluolsulfonat (Tosylat), Cumolsulfonat, Xylolsulfonat, Phosphat, Citrat, Formiat, Acetat oder deren Mischungen.In the context of the present application, particularly preferred cationic or amphoteric polymers contain as monomer unit a compound of the general formula

in which R ¹ and R ⁴ are each independently H or a linear or branched hydrocarbon radical having 1 to 6 carbon atoms; R ² and R ^{3 are} independently an alkyl, hydroxyalkyl, or aminoalkyl group in which the alkyl group is linear or branched and has from 1 to 6 carbon atoms, preferably a methyl group; x and y independently represent integers between 1 and 3. X represents a counterion, preferably a counterion selected from the group consisting of chloride, bromide, iodide, sulfate, hydrogensulfate, methosulfate, laurylsulfate, dodecylbenzenesulfonate, p-toluenesulfonate (tosylate), cumene sulfonate, xylenesulfonate, phosphate, citrate, formate, acetate or mixtures thereof.

Preferred radicals R ¹ and R ⁴ in the above formula are selected from -CH ₃ , -CH ₂ -CH ₃ , -CH ₂ -CH ₂ -CH ₃ , -CH (CH ₃ ) -CH ₃ , -CH ₂ -OH , -CH ₂ -CH ₂ -OH, -CH (OH) -CH ₃ , -CH ₂ -CH ₂ -CH ₂ -OH, -CH ₂ -CH (OH) -CH ₃ , -CH (OH) -CH ₂ -CH ₃ , and - (CH ₂ CH ₂ -O) _n H.

werden im Falle von X = Chlorid auch als DADMAC (Diallyldimethylammonium-Chlorid) bezeichnet.Very particular preference is given to polymers which have a cationic monomer unit of the above general formula in which R ¹ and R ^{4 are} H, R ² and R ^{3 are} methyl and x and y are each 1. The corresponding monomer units of the formula

in the case of X = chloride, they are also referred to as DADMAC (diallyldimethylammonium chloride).

in der R¹, R², R³, R⁴ und R⁵ unabhängig voneinander für einen linearen oder verzweigten, gesättigten oder ungesättigen Alkyl-, oder Hydroxyalkylrest mit 1 bis 6 Kohlenstoffatomen, vorzugsweise für einen linearen oder verzweigten Alkylrest ausgewählt aus -CH₃, -CH₂-CH₃, -CH₂-CH₂-CH₃, -CH(CH₃)-CH₃, -CH₂-OH, -CH₂-CH₂-OH, -CH(OH)-CH₃, -CH₂-CH₂-CH₂-OH, -CH₂- CH(OH)-CH₃, -CH(OH)-CH₂-CH₃, und -(CH₂CH₂-O)_nH steht und x für eine ganze Zahl zwischen 1 und 6 steht.Further particularly preferred cationic or amphoteric polymers contain a monomer unit of the general formula

in which R ¹ , R ² , R ³ , R ⁴ and R ⁵ independently of one another are a linear or branched, saturated or unsaturated alkyl or hydroxyalkyl radical having 1 to 6 carbon atoms, preferably a linear or branched alkyl radical selected from -CH ₃ , -CH ₂ -CH ₃ , -CH ₂ -CH ₂ -CH ₃ , -CH (CH ₃ ) -CH ₃ , -CH ₂ -OH, -CH ₂ -CH ₂ -OH, -CH (OH) -CH ₃ , -CH ₂ -CH ₂ -CH ₂ -OH, -CH ₂ - CH (OH) -CH ₃ , -CH (OH) -CH ₂ -CH ₃ , and - (CH ₂ CH ₂ -O) _n H and x is an integer between 1 and 6.

werden im Falle von X^– = Chlorid auch als MAPTAC (Methyacrylamidopropyl-trimethylammonium-Chlorid) bezeichnet.For the purposes of the present application, very particular preference is given to polymers which have a cationic monomer unit of the above general formula in which R ^{1 is} H and R ² , R ³ , R ⁴ and R ^{5 are} methyl and x is 3. The corresponding monomer units of the formula

in the case of X ^- = chloride, also referred to as MAPTAC (methylacrylamidopropyltrimethylammonium chloride).

According to the invention preferred Polymers are used which are diallyldimethylammonium salts as monomer units and / or acrylamidopropyltrimethylammonium salts.

The The above-mentioned amphoteric polymers are not only cationic Groups, but also anionic groups or monomer units. Such anionic monomer units are derived, for example the group of linear or branched, saturated or unsaturated carboxylates, linear or branched, saturated or unsaturated phosphonates, the linear or branched, saturated or unsaturated Sulfates or the linear or branched, saturated or unsaturated sulfonates. Preferred monomer units are the acrylic acid, the (meth) acrylic acid, the (Dimethyl) acrylic acid, the (ethyl) acrylic acid, the Cyanoacrylic acid, vinylessingic acid, allylacetic acid, crotonic acid, maleic acid, fumaric acid, cinnamic acid and its derivatives, allylsulfonic acids, such as allyloxybenzenesulfonic acid and methallylsulfonic acid or the allylphosphonic acids.

preferred usable amphoteric polymers are from the group of alkylacrylamide / acrylic acid copolymers, the alkylacrylamide / methacrylic acid copolymers, the alkylacrylamide / methylmethacrylic acid copolymers, the alkylacrylamide / acrylic acid / alkylaminoalkyl (meth) acrylic acid copolymers, the alkylacrylamide / methacrylic acid / alkylaminoalkyl (meth) acrylic acid copolymers, the alkylacrylamide / methylmethacrylic acid / alkylaminoalkyl (meth) acrylic acid copolymers, the alkylacrylamide / alkymethacrylate / alkylaminoethylmethacrylate / alkylmethacrylate copolymers and the copolymer of unsaturated carboxylic acids, cationically derivatized unsaturated carboxylic acids and optionally further ionic or nonionic monomers.

Prefers usable zwitterionic polymers are from the group of Acrylamidoalkyltrialkylammonium chloride / acrylic acid copolymers and their alkali metal and ammonium salts, the acrylamidoalkyltrialkylammonium chloride / methacrylic acid copolymers and their alkali metal and ammonium salts and the Methacroylethylbetain / methacrylate copolymers.

Prefers are further amphoteric polymers, which in addition to one or more anionic monomers as cationic monomers Methacrylamidoalkyl-trialkylammonium chloride and dimethyl (diallyl) ammonium chloride.

Especially preferred amphoteric polymers are from the group of the Methacrylamidoalkyltrialkylammoniumchlorid / dimethyl (diallyl) ammonium chloride / acrylic acid copolymers, the Methacrylamidoalkyltrialkylammoniumchlorid / dimethyl (diallyl) ammonium chloride / methacrylic acid copolymers and the methacrylamidoalkyltrialkylammonium chloride / dimethyl (diallyl) ammonium chloride / alkyl (meth) acrylic acid copolymers as well as their alkali and ammonium salts.

Especially preference is given to amphoteric polymers from the group of methacrylamidopropyltrimethylammonium chloride / dimethyl (diallyl) ammonium chloride / acrylic acid copolymers, the methacrylamidopropyltrimethylammonium chloride / dimethyl (diallyl) ammonium chloride / acrylic acid copolymers and the methacrylamidopropyltrimethylammonium chloride / dimethyl (diallyl) ammonium chloride / alkyl (meth) acrylic acid copolymers as well as their alkali and ammonium salts.

• – die Verkapselung der Polymere mittels wasserlöslicher oder wasserdispergierbarer Beschichtungsmittel, vorzugsweise mittels wasserlöslicher oder wasserdispergierbarer natürlicher oder synthetischer Polymere;
• – die Verkapselung der Polymere mittels wasserunlöslicher, schmelzbarer Beschichtungsmittel, vorzugsweise mittels wasserunlöslicher Beschichtungsmittel aus der Gruppe der Wachse oder Paraffine mit einem Schmelzpunkt oberhalb 30°C;
• – die Cogranulation der Polymere mit inerten Trägermaterialien, vorzugsweise mit Trägermaterialien aus der Gruppe der wasch- oder reinigungsaktiven Substanzen, besonders bevorzugt aus der Gruppe der Builder (Gerüststoffe) oder Cobuilder.

In a particularly preferred embodiment of the present invention, the polymers are present in prefabricated form. For the preparation of the polymers is suitable inter alia

• The encapsulation of the polymers by means of water-soluble or water-dispersible coating compositions, preferably by means of water-soluble or water-dispersible natural or synthetic polymers;
• - The encapsulation of the polymers by means of water-insoluble, fusible coating compositions, preferably by means of water-insoluble coating agents from the group of waxes or paraffins having a melting point above 30 ° C;
• - The cogranulation of the polymers with inert support materials, preferably with support materials from the group of washing or cleaning-active substances, particularly preferably from the group of builders (builders) or cobuilders.

washing or detergents contain the aforementioned cationic and / or amphoteric polymers, preferably in amounts between 0.01 and 10 % By weight, based in each case on the total weight of the washing or cleaning agent. In the context of the present application, however, such washing or detergents in which the weight fraction of the cationic and / or amphoteric polymers between 0.01 and 8 wt .-%, preferably between 0.01 and 6% by weight, preferably between 0.01 and 4% by weight, particularly preferably between 0.01 and 2 wt .-% and in particular between 0.01 and 1 wt .-%, each based on the total weight of the automatic dishwashing detergent.

When Softening polymers are, for example, the sulfonic acid-containing Polymers which are used with particular preference.

Especially preferably used as sulfonic acid-containing polymers are copolymers of unsaturated carboxylic acids, Sulfonic acid-containing monomers and optionally further ionogenic or nonionogenic monomers.

In the context of the present invention are as unsaturated monomer 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 are -H, -CH ₃ , a straight-chain or branched saturated alkyl radical having 2 to 12 carbon atoms, a straight-chain or branched, mono- or polyunsaturated alkenyl radical having 2 to 12 carbon atoms, NH ₂ , -OH or -COOH substituted alkyl or alkenyl radicals or -COOH or -COOR ⁴ , wherein R ^{4 is} a saturated or unsaturated, straight-chain or branched hydrocarbon radical having 1 to 12 carbon atoms.

Among the unsaturated carboxylic acids which can be described by the above formula are in particular acrylic acid (R ¹ = R ² = R ³ = H), methacrylic acid (R ¹ = R ² = H, R ³ = CH ₃ ) and / or maleic acid (R ¹ = COOH; R ² = R ³ = H) is preferred.

In the sulfonic acid-containing monomers are 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 are -H, -CH ₃ , a straight-chain or branched saturated alkyl radical having 2 to 12 carbon atoms, a straight-chain or branched, mono- or polyunsaturated alkenyl radical having 2 to 12 carbon atoms, NH ₂ , -OH or -COOH substituted alkyl or alkenyl radicals or -COOH or -COOR ⁴ , wherein R ^{4 is} a saturated or unsaturated, straight-chain or branched hydrocarbon radical having 1 to 12 carbon atoms, and X is an optional 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 - 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 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 is an optional spacer group which is selected from - (CH ₂ ) - with n = 0 to 4, -COO- (CH ₂ ) _k - with k = 1 to 6, -C (O) -NH-C (CH ₃ ) ₂ - and -C (O) -NH-CH (CH ₂ CH ₃ ) -.

Especially preferred sulfonic acid-containing monomers are included 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-hydroxypropanesulfonic acid, allylsulfonic acid, Methallylsulfonic acid, allyloxybenzenesulfonic acid, Methallyloxybenzenesulfonic acid, 2-hydroxy-3- (2-propenyloxy) propanesulfonic acid, 2-methyl-2-propene-1-sulfonic acid, styrenesulfonic acid, Vinyl sulfonic acid, 3-sulfopropyl acrylate, 3-sulfopropyl methacrylate, Sulfomethacrylamide, sulfomethylmethacrylamide and water-soluble Salts of the acids mentioned.

Particularly suitable other ionic or nonionic monomers are ethylenically unsaturated compounds. The content of the polymers used in these other ionic or nonionic monomers is preferably less than 20% by weight, based on the polymer. Particularly preferred polymers to be used consist only of monomers of the formula R ¹ (R ² ) C =C (R ³ ) COOH and monomers of the formula R ⁵ (R ⁶ ) C =C (R ⁷ ) -X-SO ₃ H.

• i) einer oder mehreren ungesättigter Carbonsäuren aus der Gruppe Acrylsäure, Methacrylsäure und/oder Maleinsäure
• ii) einem oder mehreren Sulfonsäuregruppen-haltigen Monomeren der Formeln: H₂C=CH-X-SO₃H H₂C=C(CH₃)-X-SO₃H HO₃S-X-(R⁶)C=C(R⁷)-X-SO₃H, in der R⁶ und R⁷ unabhängig voneinander ausgewählt sind aus -H, -CH₃, -CH₂CH₃, -CH₂CH₂CH₃, -CH(CH₃)₂ und X für eine optional vorhandene Spacergruppe steht, die ausgewählt ist aus -(CH₂)_n- mit n = 0 bis 4, -COO-(CH₂)_k- mit k = 1 bis 6, -C(O)-NH-C(CH₃)₂- und -C(O)-NH-CH(CH₂CH₃)-
• iii) gegebenenfalls weiteren ionogenen oder nichtionogenen Monomeren.

Further particularly preferred copolymers consist of

• i) one or more unsaturated carboxylic acids from the group of acrylic acid, methacrylic acid and / or maleic acid
• ii) one or more sulfonic acid group-containing monomers of the formulas: H ₂ C = CH-X-SO ₃ H H ₂ C = C (CH ₃ ) -X-SO ₃ H 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 is an optional 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 - and - C (O) -NH-CH (CH ₂ CH ₃ ) -
• iii) optionally further ionogenic or nonionic monomers.

The Copolymers may be the monomers from groups i) and ii) and optionally iii) in varying amounts, wherein all representatives from the group i) with all Representatives from group ii) and all representatives from group iii) can be combined. Especially Preferred polymers have certain structural units which described below.

For example, copolymers which are structural units of the formula are preferred - [CH ₂ -CHCOOH] _m - [CH ₂ -CHC (O) -Y-SO ₃ H] _p - in which m and p are each an integer between 1 and 2,000 and Y is a spacer group selected from substituted or unsubstituted aliphatic, aromatic or substituted aromatic hydrocarbon radicals having 1 to 24 carbon atoms, wherein spacer groups in which Y. for -O- (CH ₂ ) _n - with n = 0 to 4, for -O- (C ₆ H ₄ ) -, for -NH-C (CH ₃ ) ₂ - or -NH-CH (CH ₂ CH ₃ ) - are, are preferred.

These polymers are prepared by copolymerization of acrylic acid with a sulfonic acid-containing acrylic acid derivative. When the acrylic acid derivative containing sulfonic acid groups is copolymerized with methacrylic acid, another polymer is obtained whose use is likewise preferred. The corresponding copolymers contain the structural units of the formula - [CH ₂ -C (CH ₃ ) COOH] _m - [CH ₂ -CHC (O) -Y-SO ₃ H] _p -, in which m and p are each an integer between 1 and 2000 and Y is a spacer group selected from substituted or unsubstituted aliphatic, aromatic or substituted aromatic hydrocarbon radicals having from 1 to 24 carbon atoms, wherein spacer groups in which Y represents O- (CH ₂ ) - where n = 0 to 4, -O- (C ₆ H ₄ ), -NH-C (CH ₃ ) ₂ - or -NH-CH (CH ₂ CH ₃ ) -, are preferred.

Acrylic acid and / or methacrylic acid can also be copolymerized completely analogously with methacrylic acid derivatives containing sulfonic acid groups, as a result of which the structural units in the molecule are changed. Thus, copolymers which are structural units of the formula - [CH ₂ -CHCOOH] _m - [CH ₂ -C (CH ₃ ) C (O) -Y-SO ₃ H] _p -, in which m and p are each an integer between 1 and 2,000 and Y is a spacer group selected from substituted or unsubstituted aliphatic, aromatic or substituted aromatic hydrocarbon radicals having 1 to 24 carbon atoms, wherein spacer groups in which Y. for -O- (CH ₂ ) _n - with n = 0 to 4, for -O- (C ₆ H ₄ ) -, for -NH-C (CH ₃ ) ₂ - or -NH-CH (CH ₂ CH ₃ ) -, are particularly preferred, just as preferred as copolymers, the structural units of the formula - [CH ₂ -C (CH ₃ ) COOH] _m - [CH ₂ -C (CH ₃ ) C (O) -Y-SO ₃ H] _p - in which m and p are each an integer between 1 and 2,000 and Y is a spacer group selected from substituted or unsubstituted aliphatic, aromatic or substituted aromatic hydrocarbon radicals having 1 to 24 carbon atoms, wherein spacer groups in which Y. for -O- (CH ₂ ) with n = 0 to 4, for -O- (C ₆ H ₄ ) -, for -NH-C (CH ₃ ) ₂ - or -NH-CH (CH ₂ CH ₃ ) - is, are preferred.

Instead of acrylic acid and / or methacrylic acid or in addition thereto, maleic acid can also be used as a particularly preferred monomer from group i). This gives way to inventively preferred copolymers, the structural units of the formula - [HOOCCH-CHCOOH] _m - [CH ₂ -CHC (O) -Y-SO ₃ H] _p - in which m and p are in each case an integer from 1 to 2000 and Y is a spacer group selected from substituted or unsubstituted aliphatic, aromatic or araliphatic hydrocarbon radicals having from 1 to 24 carbon atoms, wherein spacer groups in which Y represents -O- (CH ₂ ) where n = 0 to 4, -O- (C ₆ H ₄ ) -, -NH-C (CH ₃ ) ₂ - or -NH-CH (CH ₂ CH ₃ ) - , are preferred. Also preferred according to the invention are copolymers which contain structural units of the formula - [HOOCCH-CHCOOH] _m - [CH ₂ -C (CH ₃ ) C (O) OY-SO ₃ H] _p in which m and p are each an integer between 1 and 2000 and Y is a spacer group selected from substituted or unsubstituted aliphatic, aromatic or substituted aromatic hydrocarbon radicals having 1 to 24 carbon atoms, wherein spacer groups in which Y. for -O- (CH ₂ ) with n = 0 to 4, for -O- (C ₆ H ₄ ) -, for -NH-C (CH ₃ ) ₂ - or -NH-CH (CH ₂ CH ₃ ) - stands

In the polymers, the sulfonic acid groups completely or partially in neutralized form, d. H. that this acidic hydrogen atom of the sulfonic acid group in some or all sulfonic acid groups against metal ions, preferably Alkali metal ions and in particular against sodium ions, exchanged can be. The use of partially or fully neutralized sulfonic acid group-containing Copolymer is preferred according to the invention.

The Monomer distribution of the invention preferred copolymers used in copolymers which only Monomers from groups i) and ii), preferably in each case 5 to 95% by weight of i) or ii), particularly preferably 50 to 90% by weight Monomer from group i) and 10 to 50 wt .-% monomer from the group ii), in each case based on the polymer.

at Terpolymers are particularly preferred which contain from 20 to 85% by weight. Monomer from group i), 10 to 60 wt .-% monomer from the group ii) and 5 to 30 wt .-% of monomer from group iii).

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 end use. Preferred washing or cleaning agents are characterized in that the copolymers have molar masses of 2000 to 200,000 gmol ^-1 , preferably from 4000 to 25,000 gmol ^-1 and in particular from 5000 to 15,000 gmol ^-1 .

bleach

The bleaching agents are a particularly preferred washing or cleaning substance. Among the compounds serving as bleaches in water H ₂ O ₂ , sodium percarbonate, sodium perborate tetrahydrate and sodium perborate monohydrate are of particular importance. Other useful bleaching agents are, for example, peroxypyrophosphates, citrate perhydrates and H ₂ O ₂ -forming peracidic salts or peracids, such as perbenzoates, peroxophthalates, diperazelaic acid, phthaloiminoperacid or diperdodecanedioic acid.

Farther can also bleach from the group of organic Bleaching agents are used. Typical organic bleach are the diacyl peroxides, such as. B. dibenzoyl peroxide. Other typical Organic bleaches are the peroxyacids, wherein as Examples especially the alkylperoxy acids and the aryl peroxyacids to be named. Preferred representatives are (a) the peroxybenzoic acid and their ring-substituted derivatives, such as alkylperoxybenzoic acids, but also peroxy-α-naphthoic acid and magnesium monoperphthalate, (b) the aliphatic or substituted aliphatic peroxyacids, such as peroxylauric acid, peroxystearic acid, ε-phthalimidoperoxycaproic acid [Phthaliminoperoxyhexanoic acid (PAP)], o-carboxybenzamidoperoxycaproic acid, N-Nonenylamidoperadipic acid and N-Nonenylamidopersuccinate, and (c) aliphatic and araliphatic peroxydicarboxylic acids, such as 1,12-diperoxycarboxylic acid, 1,9-diperoxyazelaic acid, Diperocysebacic acid, diperoxybrassic acid, the Diperoxyphthalic acids, 2-decyldiperoxybutane-1,4-diacid, N, N-terephthaloyl-di (6-aminopercaproic acid).

When Bleaching agents can also chlorine or bromine releasing substances be used. Among the suitable chlorine or bromine releasing Materials include, for example, heterocyclic N-bromo- and N-chloroamides, for example, trichloroisocyanuric acid, tribromoisocyanuric acid, Dibromoisocyanuric acid and / or dichloroisocyanuric acid (DICH) and / or their salts with cations such as potassium and sodium into consideration. Hydantoin compounds, such as 1,3-dichloro-5,5-dimethylhydanthoin are also suitable.

According to the invention Washing or cleaning preparations, in particular automatic dishwashing detergents, preferably 1 to 35% by weight, preferably 2.5 to 30% by weight, particularly preferably from 3.5 to 20% by weight and in particular from 5 to 15 Wt .-% bleach, preferably sodium percarbonate.

Of the Active oxygen content of detergents or cleaners, in particular the automatic dishwashing detergent, in each case based on the total weight of the composition, preferably between 0.4 and 10 wt .-%, particularly preferably between 0.5 and 8 wt .-% and in particular between 0.6 and 5 wt .-%. Especially preferred Means have an active oxygen content above 0.3 wt .-%, preferably above 0.7 wt .-%, more preferably above 0.8 wt .-% and in particular above 1.0% by weight.

Bleach activators

Bleach activators are used in laundry detergents or cleaners, for example, to achieve an improved bleaching effect when cleaned at temperatures of 60 ° C and below. As bleach activators, it is possible to use compounds which, under perhydrolysis conditions, give aliphatic peroxycarboxylic acids having preferably 1 to 10 C atoms, in particular 2 to 4 C atoms, and / or optionally substituted perbenzoic acid. Suitable substances are those which carry O- and / or N-acyl groups of the stated C atom number and / or optionally substituted benzoyl groups. Preference is given to polyacylated alkylenediamines, in particular tetraacetylethylenediamine (TAED), acylated triazine derivatives, in particular 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, in particular tetraacetylglycoluril (TAGU), N- Acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates, in particular n-nonanoyl or isononanoyloxybenzenesulfonate (n- or iso-NOBS), carboxylic anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate and 2,5-diacetoxy- 2,5-dihydrofuran, n-methyl-morpholinium-acetonitrile-methylsulfate (MMA) and also acetylated sorbitol and mannitol or mixtures thereof (SORMAN), acylated sugar derivatives, especially pentaacetylglucose (PAG), pentaacetyl-fructose, tetraacetyl-xylose and octaacetyllactose as well as acetylated, optionally N- alkylated glucamine and gluconolactone, and / or N-acylated lactams, for example N-benzoyl-caprolactam. Hydrophilic substituted acyl acetals and acyl lactams are also preferred set. Combinations of conventional bleach activators can also be used.

These Bleach activators are preferably used in amounts of up to 10% by weight, in particular 0.1% by weight to 8% by weight, especially 2 to 8% by weight, and especially preferably 2 to 6 wt .-%, each based on the total weight the bleach activator-containing agent used.

in der R¹ für -H, -CH₃, einen C_2-24-Alkyl- oder -Alkenylrest, einen substituierten C_2-24-Alkyl- oder -Alkenylrest mit mindestens einem Substituenten aus der Gruppe -Cl, -Br, -OH, -NH₂, -CN, einen Alkyl- oder Alkenylarylrest mit einer C_1-24-Alkylgruppe, oder für einen substituierten Alkyl- oder Alkenylarylrest mit einer C_1-24-Alkylgruppe und mindestens einem weiteren Substituenten am aromatischen Ring steht, R² und R³ unabhängig voneinander ausgewählt sind aus -CH₂-CN, -CH₃, -CH₂-CH₃, -CH₂-CH₂-CH₃, -CH(CH₃)-CH₃, -CH₂-OH, -CH₂-CH₂-OH, -CH(OH)-CH₃, -CH₂-CH₂-CH₂-OH, -CH₂-CH(OH)-CH₃, -CH(OH)-CH₂-CH₃, -(CH₂CH₂-O)_nH mit n = 1, 2, 3, 4, 5 oder 6 und X ein Anion ist.Further bleach activators preferably used in the context of the present application are compounds from the group of cationic nitriles, in particular cationic nitriles of the formula

in the R ^{1 is} -H, -CH ₃ , a C _2-24 alkyl or alkenyl radical, a substituted C _2-24 alkyl or alkenyl radical having at least one substituent from the group -Cl, -Br, - OH, -NH ₂ , -CN, an alkyl or alkenylaryl radical having a C _1-24 -alkyl group, or represents a substituted alkyl or alkenylaryl radical having a C _1-24 -alkyl group and at least one further substituent on the aromatic ring, R ² and R ^{3 are} independently selected from -CH ₂ -CN, -CH ₃ , -CH ₂ -CH ₃ , -CH ₂ -CH ₂ -CH ₃ , -CH (CH ₃ ) -CH ₃ , -CH ₂ - OH, -CH ₂ -CH ₂ -OH, -CH (OH) -CH ₃ , -CH ₂ -CH ₂ -CH ₂ -OH, -CH ₂ -CH (OH) -CH ₃ , -CH (OH) - CH ₂ -CH ₃ , - (CH ₂ CH ₂ -O) _n H where n = 1, 2, 3, 4, 5 or 6 and X is an anion.

in der R⁴, R⁵ und R⁶ unabhängig voneinander ausgewählt sind aus -CH₃, -CH₂-CH₃, -CH₂-CH₂-CH₃, -CH(CH₃)-CH₃, wobei R⁴ zusätzlich auch -H sein kann und X ein Anion ist, wobei vorzugsweise R⁵ = R⁶ = -CH₃ und insbesondere R⁴ = R⁵ = R⁶ = -CH₃ gilt und Verbindungen der Formeln (CH₃)₃N⁽⁺⁾CH₂-CN X^–, (CH₃CH₂)₃N⁽⁺⁾CH₂-CN X^– (CH₃CH₂CH₂)₃N⁽⁺⁾CH₂-CN X^–, (CH₃CH(CH₃))₃N⁽⁺⁾CH₂-CN X^– oder (HO-CH₂-CH₂)₃N⁽⁺⁾CH₂-CN X^– besonders bevorzugt sind, wobei aus der Gruppe dieser Substanzen wiederum das kationische Nitril der Formel (CH₃)₃N⁽⁺⁾CH₂-CN X^–, in welcher X für ein Anion steht, das aus der Gruppe Chlorid, Bromid, Iodid, Hydrogensulfat, Methosulfat, p-Toluolsulfonat (Tosylat) oder Xylolsulfonat ausgewählt ist, besonders bevorzugt wird.Particularly preferred is a cationic nitrile of the formula

in which R ⁴ , R ⁵ and R ^{6 are} independently selected from -CH ₃ , -CH ₂ -CH ₃ , -CH ₂ -CH ₂ -CH ₃ , -CH (CH ₃ ) -CH ₃ , wherein R ⁴ additionally also -H may be and X is an anion, preferably R ⁵ = R ⁶ = -CH ₃ and in particular R ⁴ = R ⁵ = R ⁶ = -CH ₃ and compounds of the formulas (CH ₃ ) ₃ N ⁽⁺⁾ CH ₂ -CN X ^- , (CH ₃ CH ₂ ) ₃ N ⁽⁺⁾ CH ₂ -CN X ^- (CH ₃ CH ₂ CH ₂ ) ₃ N ⁽⁺⁾ CH ₂ -CN X ^- , (CH ₃ CH (CH ₃ )) ₃ N ⁽⁺⁾ CH ₂ -CN X ^- or (HO-CH ₂ -CH ₂ ) ₃ N ⁽⁺⁾ CH ₂ -CN X ^{- are} particularly preferred, wherein in turn from the group of these substances, the cationic nitrile of Formula (CH ₃ ) ₃ N ⁽⁺⁾ CH ₂ -CN X ^- in which X represents an anion selected from the group consisting of chloride, bromide, iodide, hydrogensulfate, methosulfate, p-toluenesulfonate (tosylate) or xylenesulfonate, is particularly preferred.

bleach catalysts

additionally to the conventional bleach activators or in their place also so-called bleach catalysts can be used. In these Substances are bleach-enhancing transition metal salts or transition metal complexes such as Mn, Fe, Co, Ru or Mo saline complexes or carbonyl complexes. Also Mn, Fe, Co, Ru, Mo, Ti, V and Cu complexes with N-containing Tripod ligands and Co, Fe, Cu and Ru ammine complexes are known as Bleach catalysts usable.

Bleach-enhancing transition metal complexes, in particular with the central atoms Mn, Fe, Co, Cu, Mo, V, Ti and / or Ru, preferably selected from the group of manganese and / or Cobalt salts and / or complexes, more preferably the cobalt (ammin) complexes, the cobalt (acetate) complexes, the cobalt (carbonyl) complexes, the Chlorides of cobalt or manganese, manganese sulfate are used in common Quantities, preferably in an amount up to 5 wt .-%, in particular from 0.0025 wt.% to 1 wt.%, and more preferably from 0.01 Wt .-% to 0.25 wt .-%, each based on the total weight of inventive agent used. In special cases however, more bleach activator can also be used.

It is particularly preferred to use complexes of manganese in the oxidation state II, III, IV or IV, which preferably contain one or more macrocyclic ligands with the donor functions N, NR, PR, O and / or S. Preferably, ligands are used which have nitrogen donor functions. It is particularly preferred to use bleach catalyst (s) in the compositions of the invention, which as macromolecular ligands 1,4,7-trimethyl-1,4,7-triazacyclononan (Me-TACN), 1,4,7-triazacyclononane (TACN ), 1,5,9-trimethyl-1,5,9-triazacyclododecane (Me-TACD), 2-methyl-1,4,7-trimethyl-1,4,7-triazacyclononane (Me / Me-TACN) and or 2-methyl-1,4,7-triazacyclononane (Me / TACN). suitable Manganese complexes are, for example, [Mn ^III ₂ (μ-O) ₁ (μ-OAc) ₂ (TACN) ₂ ] (ClO ₄ ) ₂ , [Mn ^III Mn ^IV (μ-O) ₂ (μ-OAc) ₁ (TACN). ₂ ] (BPh ₄ ) ₂ , [Mn ^IV ₄ (μ-O) ₆ (TACN) ₄ ] (ClO ₄ ) ₄ , [Mn ^III ₂ (μ-O) ₁ (μ-OAc) ₂ (Me-TACN) ₂ ] (ClO ₄ ) ₂ , [Mn ^III Mn ^IV (μ-O) ₁ (μ-OAc) ₂ (Me-TACN) ₂ ] (ClO ₄ ) ₃ , [Mn ^IV ₂ (μ-O) ₃ (Me -TACN) ₂ ] (PF ₆ ) ₂ and [M ^IV ₂ (μ-O) ₃ (Me / Me-TACN) ₂ ] (PF ₆ ) ₂ (OAc = OC (O) CH ₃ ).

To increase the washing or cleaning performance of detergents or cleaners, the detergents and cleaners according to the invention may contain further enzymes. These include in particular proteases, amylases, lipases, hemicellulases, cellulases or oxidoreductases, and preferably mixtures thereof. These enzymes are basically of natural origin; Starting from the natural molecules, improved variants are available for use in detergents and cleaners, which are preferably used accordingly. Detergents or cleaning agents contain enzymes preferably in total amounts of 1 × 10 ^-6 to 5 wt .-% based on active protein. The protein concentration can be determined by known methods, for example the BCA method or the biuret method.

Under Proteases are preferred to those of the subtilisin type. Examples these are the subtilisins BPN 'and Carlsberg and their more advanced forms, the protease PB92, the subtilisins 147 and 309, the Bacillus lentus alkaline protease, subtilisin Dy and the subtilases, but not the subtilisins in the In the narrower sense, enzymes thermitase, proteinase K and the proteases TW3 and TW7.

Examples for amylases usable according to the invention are the α-amylases from Bacillus licheniformis, from B. amyloliquefaciens, from B. stearothermophilus, from Aspergillus niger and A. oryzae as well as those for use in detergents and cleaners improved developments of the aforementioned amylases. Furthermore For this purpose Bacillus α-amylase is used sp. A 7-7 (DSM 12368) and cyclodextrin glucanotransferase (CGTase) from B. agaradherens (DSM 9948).

Usable according to the invention are still lipases or cutinases, especially because of their Triglyceride-cleaving activities, but also to make suitable Precursors generate in situ peracids. These include for example, originally from Humicola lanuginosa (Thermomyces lanuginosus) available, respectively further developed lipases, in particular those with the amino acid exchange D96L. Furthermore, for example, the cutinases can be used, originally from Fusarium solani pisi and Humicola insolens have been isolated. Also usable are lipases, or cutinases whose initial enzymes originally from Pseudomonas mendocina and Fusarium solanii have been isolated.

Farther enzymes can be used under the term Hemicellulases are summarized. These include for example mannanases, xanthan lyases, pectin lyases (= pectinases), Pectinesterases, pectate lyases, xyloglucanases (= xylanases), pullulanases and β-glucanases. Other usable enzymes are carrageenases as well as tannases.

As well can in the inventive compositions Perhydrolases are used.

to Increasing the bleaching effect can further according to the invention Oxidoreductases, for example further oxidases, oxygenases, catalases, Peroxidases such as halo, chloro, bromo, lignin, glucose or Manganese peroxidases, dioxygenases or laccases (phenol oxidases, Polyphenoloxidasen) can be used. Advantageously additionally preferably organic, more preferably added aromatic compounds interacting with the enzymes, to enhance the activity of the oxidoreductases in question (Enhancer) or at very different redox potentials between the oxidizing enzymes and the soiling the electron flow to ensure (mediators).

The Enzymes can be established in any of the prior art Form are used. These include, for example, the obtained by granulation, extrusion or lyophilization solid Preparations or, in particular in liquid or gel agents, solutions of enzymes, advantageously as concentrated as possible, low in water and / or mixed with stabilizers.

Alternatively, the enzymes may be encapsulated for both the solid and liquid dosage forms, for example by spray-drying or extruding the enzyme solution together with a preferably natural polymer or in the form of capsules, for example those in which the enzymes are entrapped as in a solidified gel or in those of the core-shell type, in which an enzyme-containing core is coated with a water, air and / or chemical impermeable protective layer. In superimposed layers, additional active ingredients, for example stabilizers, emulsifiers, pigments, Bleaching or dyes are applied. Such capsules are applied by methods known per se, for example by shaking or rolling granulation or in fluid-bed processes. Advantageously, such granules, for example by applying polymeric film-forming agent, low in dust and storage stable due to the coating.

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

One Protein and / or enzyme may be especially during storage against damage such as inactivation, denaturation or decay by physical influences, oxidation or proteolytic cleavage. In microbial Obtaining the proteins and / or enzymes is inhibiting the Proteolysis particularly preferred, especially if the means Contain proteases. Detergents or cleaners can contain stabilizers for this purpose; the provision of such funds represents a preferred embodiment of the present invention Invention.

Glass corrosion inhibitors

Glass corrosion inhibitors prevent the appearance of turbidity, streaks and scratches but also the iridescence of the glass surface by machine cleaned glasses. Preferred glass corrosion inhibitors are derived from the group of magnesium and zinc salts as well as the magnesium and zinc complexes.

The Spectrum of the invention preferred zinc salts, preferably organic acids, more preferably organic Carboxylic acids, ranging from salts that are heavy or difficult in water are not soluble, so a solubility below 100 mg / l, preferably below 10 mg / l, especially below 0.01 mg / l, to such salts which have a solubility in water above 100 mg / l, preferably above 500 mg / l, more preferably above 1 g / l and in particular above 5 g / l (all solubility at 20 ° C water temperature). To the first group of zinc salts For example, zinc citrate, zinc oleate and the zinc stearate, to the group of soluble zinc salts For example, the zinc formate, zinc acetate, the zinc lactate and the zinc gluconate.

With Particular preference is given as a glass corrosion inhibitor at least one Zinc salt of an organic carboxylic acid, particularly preferred a zinc salt from the group zinc stearate, zinc oleate, zinc gluconate, Zinc acetate, zinc lactate and zinc citrate used. Also zinc ricinoleate, Zinc-absate and zinc oxalate are preferred.

In the context of the present invention, the content of zinc salt in detergents or cleaners is preferably between 0.1 and 5% by weight, preferably between 0.2 and 4% by weight and in particular between 0.4 and 3% by weight. , or the content of zinc in oxidized form (calculated as Zn ²⁺ ) between 0.01 to 1 wt .-%, preferably between 0.02 to 0.5 wt .-% and in particular between 0.04 to 0, 2 wt .-%, each based on the total weight of the glass corrosion inhibitor-containing agent.

corrosion inhibitors serve to protect the items to be washed or the machine, wherein in the field of automatic dishwashing, especially silver protectants have a special meaning. It is possible to use the known substances of the prior art. In general, especially silver protectants selected from the group of triazoles, benzotriazoles, bisbenzotriazoles, aminotriazoles, alkylaminotriazoles and the transition metal salts or complexes used become. Particularly preferred to use are benzotriazole and / or Alkylaminotriazole. According to the invention are preferred 3-amino-5-alkyl-1,2,4-triazoles or their physiologically acceptable Salts used, these substances with particular preference in a concentration of 0.001 to 10 wt .-%, preferably 0.0025 used to 2 wt .-%, particularly preferably 0.01 to 0.04 wt .-% become. Preferred acids for salt formation are hydrochloric acid, sulfuric acid, phosphoric acid, Carbonic acid, sulphurous acid, organic carboxylic acids such as acetic, glycolic, citric, succinic acid. Most notably 5-pentyl, 5-heptyl, 5-nonyl, 5-undecyl, 5-isononyl, 5-Versatic-10-acid-alkyl-3-amino-1,2,4-triazoles and mixtures of these substances.

In addition, cleaner formulations often contain active chlorine-containing agents which can markedly reduce the corrosion of the silver surface. In chlorine-free cleaners are particularly oxygen and nitrogen-containing organic redox-active compounds such as di- and trihydric phenols, eg. As hydroquinone, pyrocatechol, hydroxyhydroquinone, gallic acid, phloroglucinol, pyrogallol or derivatives of these classes of compounds used. Also, salt and complex inorganic compounds, such as salts of the metals Mn, Ti, Zr, Hf, V, Co and Ce are often used. Preference is given here to the transition metal salts which are selected from the group of manganese and / or cobalt salts and / or complexes, especially before to the cobalt (ammin) complexes, the cobalt (acetate) complexes, the cobalt (carbonyl) complexes, the chlorides of cobalt or manganese and manganese sulfate. Also, zinc compounds can be used to prevent corrosion on the items to be washed.

Instead of of or in addition to the silver protectants described above, for example, the benzotriazoles, redox-active substances be used. These substances are preferably inorganic redox-active substances from the group of manganese, titanium, zirconium, Hafnium, vanadium, cobalt and cerium salts and / or complexes, wherein the metals preferably in one of the oxidation states II, III, IV, V or VI are present.

The used metal salts or metal complexes should at least partially be soluble in water. The suitable for salt formation Counterions include all the usual one, two or three times negatively charged inorganic anions, e.g. As oxide, sulfate, nitrate, Fluoride, but also organic anions such. Stearate.

Particularly preferred metal salts and / or metal complexes are selected from the group MnSO ₄ , Mn (II) citrate, Mn (II) stearate, Mn (II) acetylacetonate, Mn (II) - [1-hydroxyethane-1,1- diphosphonate], V ₂ O ₅ , V ₂ O ₄ , VO ₂ , TiOSO ₄ , K ₂ TiF ₆ , K ₂ ZrF ₆ , CoSO ₄ , Co (NO ₃ ) ₂ , Ce (NO ₃ ) ₃ , and mixtures thereof, such that the metal salts and / or metal complexes are selected from the group MnSO ₄ , Mn (II) citrate, Mn (II) stearate, Mn (II) acetylacetonate, Mn (II) - [1-hydroxyethane-1,1- diphosphonate], V ₂ O ₅ , V ₂ O ₄ , VO ₂ , TiOSO ₄ , K ₂ TiF ₆ , K ₂ ZrF ₆ , CoSO ₄ , Co (NO ₃ ) ₂ , Ce (NO ₃ ) _{3 are used} with particular preference ,

The inorganic redox-active substances, in particular metal salts or metal complexes are preferably coated, d. H. Completely with a waterproof, but easily soluble at the cleaning temperatures Material coated to their premature decomposition or To prevent oxidation during storage. Preferred coating materials, those by known methods, such as melt coating method according to Sandwik from the food industry, are paraffins, Microwaxes, waxes of natural origin such as carnauba wax, Candellila wax, beeswax, higher melting alcohols such as hexadecanol, soaps or fatty acids.

The mentioned metal salts and / or metal complexes are in cleaning agents, preferably in an amount of 0.05 to 6 wt .-%, preferably 0.2 to 2.5 wt .-%, each based on the total agent.

Around to facilitate the disintegration of prefabricated moldings is it is possible disintegration aids, so-called disintegrants, to work into these remedies to reduce disintegration times. Among tablet disintegrants and decay accelerators are Excipients understood that for the rapid disintegration of tablets in water or other media and for the release of the Active ingredients provide.

These Substances which are also referred to as "explosives" due to their effect increase their volume when they enter the water, on the one hand, increasing the intrinsic volume (swelling), on the other hand also on the release of gases pressure can be generated, which disintegrate the tablet into smaller particles leaves. Well-known disintegration aids are For example, carbonate / citric acid systems, including other organic acids can be used. Swelling disintegration aids are for example synthetic Polymers such as polyvinylpyrrolidone (PVP) or natural Polymers or modified natural products such as cellulose and starch and their derivatives, alginates or casein derivatives.

Prefers are disintegration aids in amounts of 0.5 to 10 wt .-%, preferably 3 to 7% by weight and in particular 4 to 6% by weight, respectively based on the total weight of the desintegrationshilfsmittelhaltigen By means of, used.

Preferred disintegrating agents are cellulosic disintegrating agents, so that preferred washing or cleaning agents comprise such cellulose-based disintegrants in amounts of from 0.5 to 10% by weight, preferably from 3 to 7% by weight and in particular from 4 to 6% by weight. % contain. Pure cellulose has the formal gross composition (C ₆ H ₁₀ O ₅ ) _n and formally represents a β-1,4-polyacetate of cellobiose, which in turn is composed of two molecules of glucose. Suitable celluloses consist of about 500 to 5000 glucose units and therefore have average molecular weights of 50,000 to 500,000. Cellulose-based disintegrating agents which can be used in the context of the present invention are also cellulose derivatives obtainable by polymer-analogous reactions of cellulose. Such chemically modified celluloses include, for example, products of esterifications or etherifications in which hydroxy hydrogen atoms have been substituted. But also celluloses in which The hydroxy groups have been replaced by functional groups that are not bound by an oxygen atom, can be used as cellulose derivatives. The group of cellulose derivatives includes, for example, alkali metal celluloses, carboxymethylcellulose (CMC), cellulose esters and ethers, and aminocelluloses. The cellulose derivatives mentioned are preferably not used alone as disintegrating agents based on cellulose, but used in admixture with cellulose. The content of these mixtures of cellulose derivatives is preferably below 50% by weight, particularly preferably below 20% by weight, based on the cellulose-based disintegrating agent. It is particularly preferred to use cellulose-based disintegrating agent which is free of cellulose derivatives.

The Cellulose used as disintegration aid is preferably not used in finely divided form, but before mixing transformed into a coarser form to the premixes to be pressed, for example, granulated or compacted. The particle sizes such disintegrating agents are usually above 200 μm, preferably at least 90 wt .-% between 300 and 1600 microns and in particular at least 90 wt .-% between 400 and 1200 microns.

When another disintegrating agent based on cellulose or as an ingredient This component can be used microcrystalline cellulose. This microcrystalline cellulose is made by partial hydrolysis of Celluloses obtained under such conditions, only the amorphous ones Areas (about 30% of the total cellulose mass) of the celluloses attack and completely dissolve the crystalline areas (about 70%) but leave undamaged. A subsequent disaggregation the resulting from the hydrolysis microfine celluloses provides the microcrystalline celluloses, the primary particle sizes of about 5 microns and, for example, to granules with a mean particle size of 200 microns are compactable.

preferred Disintegration aid, preferably a disintegration aid based on cellulose, preferably in granular, cogranulated or compacted form, are in disintegrating agents in amounts of from 0.5 to 10% by weight, preferably from 3 to 7% by weight and in particular from 4 to 6 wt .-%, each based on the total weight of the disintegrant-containing agent.

According to the invention preferred In addition, gases can continue to evolve Effervescent systems used as Tablettenendesintegrationshilfsmittel become. The gas-developing effervescent system can consist of a single Substance that releases a gas on contact with water. Among these compounds is in particular the magnesium peroxide to call, which releases oxygen on contact with water. Usually However, the gas-releasing effervescent system in turn from at least two components that are together under gas formation react. While a variety of systems are and executable, for example, nitrogen, oxygen or release hydrogen, that will turn into the detergent and cleaning agent used Sprudelsystem both on the basis of economic as also select from ecological points of view to let. Preferred effervescent systems consist of alkali metal carbonate and / or bicarbonate and an acidifier, the is suitable from the alkali metal salts in aqueous Solution to release carbon dioxide.

When Acidifier, consisting of the alkali salts in aqueous Solution Release carbon dioxide are, for example, boric acid and alkali metal hydrogen sulfates, alkali metal dihydrogen phosphates and other inorganic salts. However, preference is given organic acidifier used, the citric acid a particularly preferred acidifying agent. Preferred are Acidifier in effervescent system from the group of organic Di-, tri- and oligocarboxylic acids or mixtures.

When Perfume oils or fragrances may be in the frame the individual invention fragrance compounds, for. B. the synthetic products of the ester type, ethers, aldehydes, ketones, Alcohols and hydrocarbons are used. To be favoured However, mixtures of different fragrances are used together create an appealing scent. Such perfume oils may also contain natural fragrance mixtures, as they are accessible from plant sources, eg. B. Pine, citrus, jasmine, patchouly, rose or ylang-ylang oil.

In order to be perceptible, a fragrance must be volatile, whereby besides the nature of the functional groups and the structure of the chemical compound, the molecular weight also plays an important role. For example, most odorants have molecular weights up to about 200 daltons, while molecular weights of 300 daltons and above are more of an exception. Due to the different volatility of fragrances, the smell of a perfume or fragrance composed of several fragrances changes during evaporation, whereby the odor impressions in "top note", "middle note" or "body note" ) and "base note" (end note or dry out). Because the smell perception to a large extent is based on the odor intensity, the top note of a perfume or fragrance is not only from volatile compounds, while the base note for the most part consists of less volatile, ie adherent fragrances. For example, in the composition of perfumes, more volatile fragrances can be bound to certain fixatives, preventing them from evaporating too quickly. In the subsequent classification of the fragrances in "more volatile" or "adherent" fragrances so nothing about the olfactory impression and whether the corresponding fragrance is perceived as a head or middle note, nothing said.

The Fragrances can be processed directly, but it can also be advantageous to apply the fragrances on carriers, by a slower release of fragrance for long-lasting Provide scent. As such carrier materials, for example Cyclodextrins proven, the cyclodextrin-perfume complexes in addition can still be coated with other excipients.

dyes

preferred Dyes whose selection does not present any difficulty to the skilled person have a high storage stability and insensitivity compared to the other ingredients of the funds and against light as well as no pronounced substantivity compared to those to be treated with the dye-containing agents Substrates such as textiles, glass, ceramics or plastic crockery, so as not to stain them.

When choosing the colorant, it must be taken into account that the colorants have a high storage stability and insensitivity to light. At the same time, it should also be taken into account when choosing suitable colorants that colorants have different stabilities to oxidation. In general, water-insoluble colorants are more stable to oxidation than water-soluble colorants. Depending on the solubility and thus also on the sensitivity to oxidation, the concentration of the colorant in the detergents or cleaners varies. In the case of readily water-soluble colorants, colorant concentrations in the range of a few 10 ^-2 to 10 ^-3 % by weight are typically selected. By contrast, in the case of the particularly preferred, but less readily water-soluble, pigment dyes due to their brilliance, the suitable concentration of the colorant in detergents or cleaners is typically about 10 ^-3 to 10 ^-4 % by weight.

It Dyes which oxidatively in the washing process are preferred can be destroyed and mixtures thereof with suitable blue dyes, so-called blue toners. It has proven to be advantageous to use dyes, in water or at room temperature in liquid organic Substances are soluble. Suitable examples are anionic Colorants, z. B. anionic nitrosofarbstoffe.

additionally to the components described in detail so far the detergents and cleaners contain other ingredients, which the application technology and / or aesthetic Properties of these funds continue to improve. Preferred agents contain one or more substances from the group of electrolytes, pH regulators, fluorescers, hydrotopes, foam inhibitors, Silicone oils, anti redeposition agents, optical brighteners, Grayness inhibitors, inlet preventer, anti-crease agents, Color transfer inhibitors, antimicrobial agents, Germicides, fungicides, antioxidants, antistatic agents, ironing aids, Phobic and impregnating agents, swelling and anti-slip agents as well as UV absorbers.

As electrolytes from the group of inorganic salts, a wide number of different salts can be used. Preferred cations are the alkali and alkaline earth metals, preferred anions are the halides and sulfates. From a manufacturing point of view, the use of NaCl or MgCl ₂ in the washing or cleaning agents is preferred.

Around the pH of detergents or cleaners in the desired The use of pH-adjusting agents may be indicated be. Can be used here all known acids or alkalis, provided that their use is not from application technology or ecological reasons or for reasons consumer protection. Usually exceeds the amount of these adjusting agents 1 wt .-% of the total formulation not.

Suitable foam inhibitors are, inter alia, soaps, oils, fats, paraffins or silicone oils, which may optionally be applied to support materials. Suitable carrier materials are, for example, inorganic salts such as carbonates or sulfates, cellulose derivatives or silicates and mixtures of the abovementioned materials. In the context of the present application preferred agents include paraffins, preferably unbranched paraffins (n-paraffins) and / or silicones, preferably linear-polymeric silicones, which are constructed according to the scheme (R ₂ SiO) _x and are also referred to as silicone oils. These silicone oils usually are clear, colorless, neutral, odorless, hydrophobic liquids having a molecular weight between 1,000 and 150,000, and viscosities between 10 and 1,000,000 mPa · s.

suitable Anti redeposition agent, also referred to as soil repellents are, for example, nonionic cellulose ethers such as methyl cellulose and methylhydroxypropylcellulose with a proportion of methoxy groups from 15 to 30% by weight and of hydroxypropyl groups from 1 to 15% by weight, in each case based on the nonionic cellulose ether and the known from the prior art polymers of phthalic acid and / or Terephthalic acid or derivatives thereof, in particular Polymers of ethylene terephthalates and / or polyethylene glycol terephthalates or anionic and / or nonionic modified derivatives of these. Especially preferred of these are the sulfonated derivatives the phthalic and terephthalic acid polymers.

optical Brighteners (so-called "whiteners") can the detergents or cleaners are added to graying and to eliminate yellowing of the treated textiles. These Substances attract to the fiber and cause a whitening and fake bleaching effect by emitting invisible ultraviolet radiation convert into visible longer wavelength light, the Ultraviolet light absorbed from sunlight is weak bluish fluorescence is emitted and with the yellow tint the gray or yellowed laundry results in pure white. Suitable compounds are derived, for example, from the substance classes 4,4'-diamino-2,2'-stilbenedisulfonic acids (flavonic acids), 4,4'-distyrylbiphenyls, methylumbelliferones, coumarins, dihydroquinolinones, 1,3-diarylpyrazolines, naphthalimides, benzoxazole, Benzisoxazole and benzimidazole systems and by heterocycles substituted pyrene derivatives.

graying have the task, the detached from the fiber dirt to keep suspended in the fleet and so the recovery of the Prevent dirt. These are water-soluble colloids mostly organic nature suitable, for example, the water-soluble Salts of polymeric carboxylic acids, glue, gelatin, salts of Ether sulfonic acids of starch or cellulose or salts of acidic sulfuric acid esters of cellulose or the strength. Also water-soluble, acidic groups containing polyamides are suitable for this purpose. Farther can be soluble starch preparations and use other than the above starch products, z. As degraded starch, aldehyde levels, etc. Also Polyvinylpyrrolidone is useful. Can be used as grayness inhibitors are also cellulose ethers such as carboxymethylcellulose (Na salt), Methylcellulose, hydroxyalkylcellulose and mixed ethers such as methylhydroxyethylcellulose, Methylhydroxypropylcellulose, methylcarboxy-methylcellulose and their mixtures.

There textile fabrics, in particular of rayon, rayon, Cotton and its blends may tend to wrinkle, because the individual fibers against bending, bending, pressing and squeezing are sensitive to the grain direction, synthetic Anti-crease agents are used. These include, for example synthetic products based on fatty acids, fatty acid esters, Fatty acid amides, alkylol esters, alkylolamides or fatty alcohols, which are mostly reacted with ethylene oxide, or based products of lecithin or modified phosphoric acid ester.

Phobic and impregnation processes are used to furnish textiles with substances that prevent the deposition of dirt or facilitate its leaching ability. Preferred repellents and impregnating agents are perfluorinated fatty acids, also in the form of their aluminum u. Zirconium salts, organic silicates, silicones, polyacrylic acid esters with perfluorinated alcohol component or with perfluorinated acyl or sulfonyl radical coupled, polymerizable compounds. Antistatic agents may also be included. The antisoiling equipment with repellents and impregnating agents is often classified as an easy-care finish. The penetration of the impregnating agent in the form of solutions or emulsions of the active substances in question can be facilitated by adding wetting agents which reduce the surface tension. A further field of application of repellents and impregnating agents is the water-repellent finishing of textiles, tents, tarpaulins, leather, etc., in which, in contrast to waterproofing, the fabric pores are not closed, so the fabric remains breathable (hydrophobing). The water repellents used for hydrophobizing coat textiles, leather, paper, wood, etc. with a very thin layer of hydrophobic groups, such as longer alkyl chains or siloxane groups. Suitable water repellents are z. As paraffins, waxes, metal soaps, etc. with additions of aluminum or zirconium salts, quaternary ammonium compounds with long-chain alkyl radicals, urea derivatives, fatty acid-modified melamine resins, chromium complex salts, silicones, tin-organic compounds and glutaric dialdehyde as well as perfluorinated compounds. The hydrophobized materials do not feel greasy; nevertheless, similar to greasy substances, water droplets emit from them without moistening. So z. Silicone-impregnated textiles have a soft feel and are water and dirt repellent; Stains from ink, wine, fruit juices and the like are lighter to remove.

to Control of microorganisms can be antimicrobial Active ingredients are used. Here one differentiates depending on Antimicrobial spectrum and mechanism of action between bacteriostats and Bactericides, fungistats and fungicides etc. Important substances These groups include, for example, benzalkonium chlorides, alkylarylsulfonates, Halogenphenols and Phenolmercuriacetat, where also completely on these compounds can be dispensed with.

Around undesirable, by oxygen action and other oxidative Processes caused changes to the detergents and cleaners and / or to prevent the treated textiles the agents contain antioxidants. To this class of connection include, for example, substituted phenols, hydroquinones, Catechols and aromatic amines and organic sulfides, polysulfides, Dithiocarbamates, phosphites and phosphonates.

One increased wearing comfort can from the additional Use of antistatics will result. Enlarge antistatic agents the surface conductivity and allow thus an improved drainage of formed charges. Outer Antistatic agents are usually substances with at least one hydrophilic Molecule ligands and give on the surfaces a more or less hygroscopic film. These mostly surface-active Antistatic agents can be transformed into nitrogenous (amines, amides, quaternary Ammonium compounds), phosphorus-containing (phosphoric acid esters) and sulfur-containing (alkyl sulfonates, alkyl sulfates) antistatic agents. Lauryl (resp. Stearyl) dimethylbenzylammonium chlorides are also suitable as Antistatics for textiles or as an additive to detergents, In addition, a smoothing effect is achieved.

to Improvement of water absorbency, rewettability treated textiles and to facilitate ironing The treated textiles may contain silicone derivatives become. These additionally improve the rinsing behavior of detergents or cleaners by their foam-inhibiting Properties. Preferred silicone derivatives are, for example, polydialkyl or alkylaryl siloxanes in which the alkyl groups are one to five Have C atoms and are completely or partially fluorinated. Preferred silicones are polydimethylsiloxanes which may optionally be derivatized can and then be amino-functional or quaternized or Si-OH, Si-H and / or Si-Cl bonds. Further preferred Silicones are the polyalkylene oxide-modified polysiloxanes, ie Polysiloxanes having, for example, polyethylene glycols and the polyalkylene oxide-modified dimethylpolysiloxanes.

After all can according to the invention also UV absorbers which are applied to the treated textiles and improve the light fastness of the fibers. Links, which have these desired properties are, for example the compounds which are active by radiationless deactivation and Derivatives of benzophenone with substituents in the 2 and / or 4-position. Furthermore, substituted benzotriazoles, in the 3-position phenyl-substituted Acrylates (cinnamic acid derivatives), optionally with cyano groups in the 2-position, salicylates, organic Ni complexes and natural products like umbelliferone and the body's own urocanic acid suitable.

protein are due to their fiber care effect more in the context of present invention preferred active substances from the field of detergents and cleaners. Protein hydrolysates are product mixtures, by acid, base or enzymatically catalyzed degradation of Proteins (proteins) are obtained. According to the invention Protein hydrolysates of both vegetable and animal origin be used. Animal protein hydrolysates are for example Elastin, collagen, keratin, silk and milk protein protein hydrolysates, which may also be present in the form of salts. According to the invention preferred is the use of protein hydrolysates of plant origin, z. Soybean, almond, rice, pea, potato and wheat protein hydrolysates. Although the use of protein hydrolysates is preferred as such may, if appropriate, also be otherwise obtained amino acid mixtures or individual amino acids such as arginine, lysine, histidine or pyrroglutamic acid be used. Also possible is the use of Derivatives of protein hydrolysates, for example in the form of their fatty acid condensation products.

The The following examples further illustrate the invention, but without restricting it.

Examples

All molecular biology work steps follow standard methods, such as those in the Handbook of Fritsch, Sambrook and Maniatis "Molecular cloning: a laboratory manual", Cold Spring Harbor Laboratory Press, New York, 1989 , or similar relevant works. Enzymes and kits were used according to the instructions of the respective manufacturers.

example 1

Isolation and identification of the proteolytic active bacterial strain DSM ID 01-189

0.1 g of a soil sample was suspended in 1 ml of sterile 0.9% NaCl solution and on agar plates containing milk powder (1.5% agar, 0.5% NaCl, 0.1% K ₂ HPO ₄ , 0.1%). Yeast extract, 2% peptone, 1% milk powder, pH 10). A proteolytically active bacterium was isolated on the basis of a clarification laboratory and was identified as Bacillus sp. By the strain information available from the German Collection of Microorganisms and Cell Cultures (DSMZ). identified and deposited under the accession number DSM ID 01-189 at the German Collection of Microorganisms and Cell Cultures (DSMZ).

Example 2

Isolation and cloning of the new serine protease from the soil

The proteolytically active bacterium Bacillus sp. DSM ID 01-189 was added in Horikoshi medium pH9 (0.1% K ₂ HPO ₄ , 0.5% yeast extract, 1% peptone, 0.02% MgSO ₄ , 0.3% Na ₂ CO ₃ ) for 72 h Cultured at 37 ° C and 200 rpm. The chromosomal DNA of this bacterium was prepared according to standard methods, treated with the restriction enzyme Sau 3A and the resulting fragments cloned into the vector pAWA22. This is a pBC16-derived expression vector for use in Bacillus species ( Bernhard et al. (1978), J. Bacteriol., Vol. 133 (2), p. 897 et seq. ). This vector was inserted into the protease-negative host strain Bacillus subtilis DB 104 ( Kawamura and Doi (1984), J. Bacteriol., Vol. 160 (1), pp. 442-444 ).

The Transformants were first regenerated on DM3 medium and then on milk powder-containing agar plates (TBY Skimmilk plates; see Example 1). Proteolytically active clones were identified by their lysis farms. From the preserved proteolytically active clones were selected one whose plasmid (Vector) isolated and the gene fragment contained in this vector (Insert) sequenced by standard methods.

The Approximately 2kb insert contains an open reading frame of about 1 kb, its nucleic acid sequence (DNA sequence) for a protease of the type of highly alkaline subtilisins encoded (SEQ ID NO. 1). The sequence was amplified by PCR, cloned in the E. coli vector pUC19 and according to the Budapest Treaty with the DSMZ-German Collection of Microorganisms and cell cultures GmbH (Inhoffenstraße 7B, D-38124 Braunschweig) deposited under the number DSM 19494.

Example 3

Determination of similarities the amino acid sequence of the mature protease (SEQ ID NO. 3)

It was a homology comparison with the previously known proteases in the "Non-redundant Genbank" ( Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs "; Nucleic Acids Res., 25, pp. 3389-3402 .) carried out. The identity values were (available from InforMax, Inc., Bethesda, USA) determined using the computer program Vector NTI ^® Suite 7.0 with the preset default parameters. The results are summarized in Table 1 below. Table 1: % Identity AAB93489._mature CAB46075.1_mature (B.sphaericus) SUBT_BACS9_mature S25835_mature SEQ ID NO. 1 of US2004 / 0209343 SEQ ID NO. 3 72.4 72.7 67.2 67.5 94.1

As already described above, the next similar enzyme identified was the protease, which as SEQ ID NO. 1 is disclosed in US patent application US 2004/0209343. The determined identity at the amino acid level is 94.1% based on the mature enzyme according to SEQ ID NO. 3. Further identity values to amino acid sequences of subsequent database entries which gave lower identity values in the homology comparison are also given in Table 1 above.

Description of the figures

1 : Alignment of the mature protease according to the invention (SEQ ID NO: 3) with proteases from the prior art, calculated using the program Vector NTI Suite Ver. 7 (InforMax, Inc. Bethesda, USA) under standard parameters.

In this mean: SEQ ID NO. 3: Alkaline protease according to the invention according to SEQ ID NO. 3 (mature enzyme) US 2004/0209343 (SEQ ID NO: 1): Protease according to SEQ ID NO. 1 of US patent application US 2004/0209343 Blap WT: Alkaline protease from Bacillus lentus DSM 5483 ( WO 92/21760 A1 )

It follows Sequence listing according to WIPO St. 25. This can of the official publication platform of the DPMA become.

QUOTES INCLUDE IN THE DESCRIPTION

This list The documents listed by the applicant have been automated generated and is solely for better information recorded by the reader. The list is not part of the German Patent or utility model application. The DPMA takes over no liability for any errors or omissions.

Cited patent literature

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Cited non-patent literature

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Claims (43)

Protease comprising an amino acid sequence, which is selected from the group consisting of a) Amino acid sequence corresponding to that shown in SEQ ID NO. 3 specified Amino acid sequence is at least 94.2% identical b) Amino acid sequence corresponding to that shown in SEQ ID NO. 2 specified Amino acid sequence is at least 59% identical Protease according to claim 1, characterized in that that it comprises an amino acid sequence selected is made up of the group a) amino acid sequence, which corresponds to that shown in SEQ ID NO. 3 indicated amino acid sequence increasingly preferably at least 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5%, and most preferably is 100% identical b) Amino acid sequence to the in SEQ ID NO. 2 indicated amino acid sequence to at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% and especially preferably 100% identical. Protease, characterized in that it is at least one and increasingly preferably two, three or four matching antigenic determinants having one of the claims 1 or 2 designated protease. Protease according to one of claims 1 to 3, which is naturally present in an organism, the can be isolated from a natural habitat. A protease according to claim 4, which is a Microorganism is, preferably a fungus, a Gram-negative or a Gram-positive bacterium, and particularly preferred among them around one of the genus Bacillus. Protease according to one of claims 1 to 5, characterized in that they are in the bacterial strain Bacillus sp. DSM ID 01-189 is naturally present. Protease, characterized in that it consists of a Protease according to one of claims 1 to 6 as starting molecule is obtainable by fragmentation, deletion, insertion or Includes substitution mutagenesis and an amino acid sequence, those over a length of at least 300 and increasingly preferably at least 290, 280, 270, 260, 250, 240, 230, 220, 210, 200, 190, 180, 170, 160, 150, 140, 130, 120, 110, 100, 90, 80, 70, 60 and 50 contiguous amino acid positions matches the parent molecule. Protease, characterized in that it consists of a Protease according to one of claims 1 to 6 as starting molecule is obtainable and one or more amino acid substitutions in positions corresponding to positions 3, 4, 36, 42, 47, 56, 61, 69, 87, 96, 99, 101, 102, 104, 114, 118, 120, 130, 139, 141, 142, 154, 157, 188, 193, 199, 205, 211, 224, 229, 236, 237, 242, 243, 255 and 268 of the alkaline protease from Bacillus lentus according to SEQ ID NO. 4 are assigned in an alignment. Protease according to one of claims 1 to 8, characterized in that it additionally stabilized is, preferably by covalent coupling to a polymer. Protease according to one of claims 1 to 9, characterized in that it has at least one chemical modification having. Nucleic acid molecule, encoding for a protease according to any one of claims 1 to 10th Nucleic acid molecule according to claim 11, characterized in that it comprises a nucleic acid sequence, which is selected from the group consisting of a) Nucleic acid sequence corresponding to that shown in SEQ ID NO. 1 indicated Nucleic acid sequence in a portion of at least 300 contiguous nucleotides at least 59% identical is b) Nucleic acid sequence corresponding to the amino acid sequence shown in SEQ ID NO. 1 indicated nucleic acid sequence in the positions 343 at least 59% identical by 1269 c) nucleic acid sequence, which corresponds to that shown in SEQ ID NO. 1 indicated nucleic acid sequence at least 59% identical. Vector containing a nucleic acid according to one of claims 11 or 12. Vector according to claim 13, characterized it is a cloning vector or an expression vector. Non-human host cell that is a protease according to any one of claims 1 to 10 or a fragment thereof contains or which can be stimulated to produce them, preferably using a vector according to claim 13 or 14. Host cell according to claim 15, characterized in that that they are the protease or a fragment of them into the host cell surrounding medium secreted. Host cell according to claim 15 or 16, characterized that she is a bacterium. Host cell according to claim 17, characterized in that that the bacterium is selected from the group of genera of Escherichia, Klebsiella, Bacillus, Staphylococcus, Corynebacterium, Arthrobacter, Streptomyces, Stenotrophomonas and Pseudomonas. Host cell according to claim 17 or 18, characterized that the bacterium is selected from the group of Escherichia coli, Klebsiella planticola, Bacillus licheniformis, Bacillus lentus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus alcalophilus, Bacillus globigii gibsonii, Bacillus pumilus, Staphylococcus carnosus, Corynebacterium glutamicum, Arthrobacter oxidans, Streptomyces lividans, Streptomyces coelicolor and Stenotrophomonas maltophilia. Host cell according to claim 15 or 16, characterized that it has a nucleus. Process for the preparation of a protease after a of claims 1 to 10. The method of claim 21 using a nucleic acid according to one of claims 11 or 12, preferably below Use of a vector according to any one of claims 13 or 14, more preferably using a host cell after one of claims 15 to 20. Means, characterized in that it is at least a protease according to any one of claims 1 to 10. Agent according to claim 23, characterized that it is a detergent, hand wash, dishwashing detergent, hand dishwashing detergent, Machine dishwashing detergents, cleaning agents, dentures or contact lens care products, rinsing agents, disinfectants, cosmetic, pharmaceutical or other means of Treatment of filter media, textiles, furs, paper, skins or Leather, is. Agent according to claim 23 or 24, characterized that it is a laundry detergent or dishwashing detergent is. Agent according to one of claims 23 to 25, characterized in that it is present as a one-component system. Agent according to one of claims 23 to 25, characterized in that it is divided into several components is. Agent according to one of claims 23 to 27, characterized in that it contains the protease in an amount from 2 μg to 20 mg, preferably from 5 μg to 17.5 mg, more preferably from 20 μg to 15 mg and whole more preferably from 50 μg to 10 mg per g of the agent contains. Agent according to one of claims 23 to 28, characterized in that it is in solid form. Agent according to claim 29, characterized that it is a free-flowing powder with a bulk density from 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l. Agent according to one of claims 23 to 28, characterized in that it is in pasty or liquid form is present. Agent according to one of claims 23 to 31, characterized in that the protease with a at room temperature or impermeable to the protease in the absence of water Substance is sheathed. Agent according to one of claims 23 to 31, further comprising one or more further enzymes. Agent according to claim 33, characterized that at least one other enzyme is a protease, amylase, cellulase, Hemicellulase, mannanase, tannase, xylanase, xanthanase, β-glucosidase, Carrageenase, oxidase, oxidoreductase or a lipase is. Agent according to one of claims 23 to 34, characterized in that there is at least one further component contains, selected from the group consisting of Surfactants, builders, acids, alkaline substances, hydrotropes, Solvents, thickeners, bleaches, dyes, Perfumes, corrosion inhibitors, sequestering agents, electrolytes, optical brighteners, grayness inhibitors, silver corrosion inhibitors, Color transfer inhibitors, foam inhibitors, abrasives, UV absorbers, solvents, antistatic agents, pearlescing agents and skin protection products. Agent according to one of claims 23 to 35, further comprising - 5 wt .-% to 70 wt .-%, in particular 5 wt .-% to 30 wt .-% surfactants and / or 10% by weight to 65 wt .-%, in particular 12 wt .-% to 60 wt .-% water-soluble or water-dispersible inorganic builder material and / or - 0.5 Wt .-% to 10 wt .-%, in particular 1 wt .-% to 8 wt .-%, water-soluble organic builders and / or - 0.01 to 15 Wt .-% solid inorganic and / or organic acids or acid salts and / or 0.01 to 5% by weight of complexing agent for heavy metals and / or 0.01 to 5% by weight Grayness inhibitor and / or 0.01 to 5% by weight Color transfer inhibitor and / or - 0,01 to 5% by weight foam inhibitor The agent of claim 36, further comprising 0.01 up to 5% by weight of optical brightener. Use of an agent according to one of the claims 23 to 37 for the removal of protease-sensitive stains on textiles or hard surfaces. Process for cleaning textiles or hard Surfaces, characterized in that in at least a method step, an agent according to one of the claims 23 to 37 is applied. Process for cleaning textiles or hard Surfaces, characterized in that in at least a method step, a protease according to one of the claims 1 to 10 is proteolytically active. Method according to claim 40, characterized in that that the protease in an amount of 40 micrograms to 4 g, preferably from 50 μg to 3 g, more preferably from 100 μg to 2 g and most preferably from 200 μg to 1 g is used per application. Use of a protease according to any one of the claims 1 to 10 for cleaning textiles or hard surfaces. Use according to claim 42, wherein the protease in an amount of 40 μg to 4 g, preferably 50 μg to 3 g, more preferably from 100 μg to 2 g and whole more preferably used from 200 μg to 1 g per application is.