EP2171047A1

EP2171047A1 - Removal of by-products from crosslinkable preparations

Info

Publication number: EP2171047A1
Application number: EP08774307A
Authority: EP
Inventors: Timothy O'connell; Karl-Heinz Maurer; Cornelia Kluin; Inken PRÜSER; Hanns Misiak; Michael Krebs
Original assignee: Henkel AG and Co KGaA
Current assignee: Henkel AG and Co KGaA
Priority date: 2007-07-23
Filing date: 2008-06-26
Publication date: 2010-04-07
Also published as: WO2009013093A1; US7968326B2; DE102007034726A1; US20100184121A1

Abstract

The present invention relates to the use of enzymes and/or whole-cell catalysts for the removal of undesired by-products from crosslinkable preparations.

Description

Removal of by-products from crosslinkable preparations

The present invention relates to the use of enzymes and / or whole-cell catalysts for removing unwanted by-products from crosslinkable preparations.

Some crosslinking reactions produce undesirable by-products. These are generally low molecular weight compounds which are liberated from the crosslinking components at the end of the crosslinking reaction. Thus, for example, methanol is produced as a by-product in the curing of certain silicone sealants which carry methoxy groups as a reactive group.

The object of the present invention was to enable the removal of such by-products and in particular to reduce the release of such by-products into the environment.

Surprisingly, it has now been found that the release of said unwanted by-products can be effectively suppressed by the use of enzymes as well as of these enzymes producing microorganisms. This was surprising in particular in that it could not be expected that the enzymes and microorganisms in question can be obtained in the crosslinkable preparations in the active or native state, in order to be able to effect an effective degradation of the unwanted by-products.

A first subject of the present invention is therefore the use of enzymes and / or microorganisms which produce these enzymes - also referred to below as "whole-cell catalysts" - for the removal of in particular unwanted by-products from crosslinkable preparations.

According to the invention, ^" crosslinkable (or crosslinking) preparation" is to be understood as meaning any preparation which contains crosslinkable or crosslinking components. With regard to the degree of crosslinking, these may be preparations in which the crosslinking reaction has not yet begun, in which preparations the crosslinking reaction has already begun, but has not yet been completed, the crosslinking reaction being only started as well as being at an advanced stage, as well as preparations in which the crosslinking reaction is already largely or completely completed.

The enzyme and / or the whole-cell catalyst may in this case be present both in the crosslinkable preparation itself, but they may also be added in the course of the application of the crosslinkable preparation. The addition may in this case both shortly before the application of the Preparation as well as shortly after the application of the preparation to the application site, in particular, for example, after the application of a jointing compound in the joint, carried out, so after the process of crosslinking has already begun.

A further subject of the present invention is therefore also a crosslinkable preparation, characterized in that it contains crosslinkable components, in particular crosslinkable monomers, as well as at least one enzyme and / or at least one whole-cell catalyst.

Another object of the present invention is therefore also a multi-component kit comprising a crosslinkable preparation and a preparation containing at least one enzyme and / or at least one whole-cell catalyst.

However, a further subject-matter of the present invention is therefore likewise a process for the removal of, in particular, unwanted by-products from crosslinkable preparations, characterized in that a crosslinkable preparation which releases undesired by-products during crosslinking is brought into contact with an enzyme and / or a whole-cell catalyst, to remove the by-product, wherein the enzyme and / or the whole-cell catalyst can either be incorporated into the crosslinkable preparation and / or this can be added in the course of application, that is before, during or after the application. By "adding in" is meant generally contacting between crosslinkable preparation and enzyme and / or whole-cell biocatalyst, i.e., both mixing and surface application may occur.

In a preferred embodiment, the application in this case takes place after the application of the crosslinkable preparation to the application site, in particular after the application of a jointing compound into the joint. The enzyme and / or the whole-cell catalyst are preferably added here in the form of a surfactant-containing preparation to the crosslinkable preparation applied to the site of application. At the same time, it is then possible to smooth-coat the crosslinkable preparation, in particular the jointing compound, for example using a rubber glove. The application is preferably carried out immediately after the application of the crosslinkable preparation, so that the crosslinking or the physical setting has only begun and the resulting by-product can be degraded immediately after release. However, it is also conceivable, although less preferred according to the invention, to carry out the application of enzyme and / or whole-cell catalyst only after completion of the crosslinking, since then released methanol can still be effectively removed.

A preferred subject of the invention is therefore a process for the removal of by-products, in particular unwanted by-products, from crosslinkable preparations, characterized in that a) initially a crosslinkable preparation on the Application site is applied and b) then a surfactant-containing preparation containing at least one enzyme and / or at least one whole-cell biocatalyst, is applied to the crosslinkable preparation.

The crosslinkable preparation is preferably a silane-curing preparation, in particular a crosslinkable silicone composition or crosslinkable silyl group-containing prepolymers such as MS polymers, silanated acrylates, silanized polyolefins, in particular silanized polyisobutene, or silanized polyurethanes or mixtures of these substances, where: The preparation containing the silicone composition or the crosslinkable silyl group-containing prepolymers is preferably a sealant, in particular a jointing compound. The term "silanized" in this context means that it is over alkoxy, acetate, oxime, benzamide or Aminsilangruppen crosslinking compounds.

The undesired by-product in a preferred embodiment is accordingly an alcohol, preferably ethanol or methanol, an organic acid, in particular acetic acid, an oxime, in particular a ketoxime, a benzamide or an amine.

The enzyme to be used in accordance with the invention and / or the enzyme produced by the whole cell catalyst to be employed according to the invention is selected in a preferred embodiment from alcohol-degrading, especially methanol-degrading enzymes, acetic acid-degrading enzymes, oxime-degrading, especially ketoxime-degrading enzymes, enzymes degrading benzamides and amines-degrading enzymes ,

The enzyme may in this case generally be selected from enzymes which convert the corresponding by-product into another product in some way. In addition to the degradation, therefore, about the conversion into another organic substance is conceivable.

As examples of inventively employable methanol-degrading enzymes are in particular called alcohol dehydrogenases (EC 1.1.1.1, 1.1.1.2 or 1.1.99.8), methanol dehydrogenase (EC 1.1.1.244), cyclohexanol dehydrogenase (EC 1.1.1.245), cholesterol Oxidase (EC 1.1.3.6), alcohol oxidase (EC 1.1.3.13), formaldehyde dismutase (EC 1.2.99.4), catalase (EC 1.11.1.6), methanol 5-hydroxybenzimidazolylcobamide co-methyltransferase (EC 2.1.1.90 ), Alcohol O-acetyltransferase (EC 2.3.1.84), sucrose phosphorylase (EC 2.4.1.7), levansucrase (EC 2.4.1.10), O-acetyl homoserine aminocarboxypropyltransferase (EC 2.5.1.49), alcohol sulfotransferase (EC 2.8. 2.2), fatty acyl ethyl ester synthase (EC 3.1.1.67), acid phosphatase (EC 3.1.3.2), phospholipase D (EC 3.1.4.4), venom exonuclease (EC 3.1.15.1), alpha-glucosidase ( EC 3.2.1.20) beta-glucosidase (EC 3.2.1.21), alpha-galactosidase (EC 3.2.1.22), beta-mannosidase (EC 3.2.1.25), xylan 1, 4-beta-xylosidase (EC 3.2.1.37), beta-N- Acetylhexosaminidase (EC 3.2.1.52), L-iduronidase (EC 3.2.1.76), glucan-1, 6-alphasomaltosidase (EC 3.2.1.94), glycopeptide alpha-N-acetylgalactosaminidase (EC 3.2.1.97), endoglycosylceramidase (EC 3.2.1.123), chymotrypsin (EC 3.4.21.1) and omega-amidase (EC 3.5.1.3).

Examples of acetic acid or acetate-degrading enzymes which can be used according to the invention are, in particular, hydroxymethylglutaryl-CoA reductase (NADPH) (EC 1.1.1.34), 3-ketosteroid reductase (EC 1.1.1.270), aldehydes ferredoxin oxidoreductase (EC 1.2.7.5) , Manganese peroxidase (EC 1.11.1.13), Arsenate reductase (donor) (EC 1.20.99.1), Selenate reductase (EC 1.97.1.9), Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2), Cysteine synthase (EC 2.5.1.47), Acetates kinase (EC 2.7.2.1), carbamate kinase (EC 2.7.2.2), formats kinase (EC 2.7.2.6), butyrate kinase (EC 2.7.2.7), propionate kinase (EC 2.7.2.15), propionate CoA-transferase (EC 2.8.3.1), acetate CoA-transferase (EC 2.8.3.8), butyrate-acetoacetate CoA-transferase (EC 2.8.3.9), glutaconate CoA-transferase (EC 2.8.3.12), 5-hydroxypentanoate CoA-transferase (EC 2.8. 3.14), carboxylesterase (EC 3.1.1.1), arylesterase (EC 3.1.1.2), triacylglycerol lipase (EC 3.1.1.3), acetylesterase (EC 3.1.1.6), acetylcholinesterase (EC 3 .1.1.7), cholinesterase (EC 3.1.1.8), tropinesterase (EC 3.1.1.10), pectin esterase (EC 3.1.1.11), sterol esterase (EC 3.1.1.13), retinyl palmitate esterase (EC 3.1.1.21), Dihydrocoumarin hydrolase (EC 3.1.1.35), lipoprotein lipase (EC 3.1.1.34), cephalosporin C deacetylase (EC 3.1.1.41), alpha-amino acid esterase (EC 3.1.1.43), 4-methyloxaloacetate esterase (EC 3.1. 1.44), i-alkyl-2-acetylglycerophosphocholine esterase (EC 3.1.1.47), wax-ester hydrolase (EC 3.1.1.50), 4-acetamidobutyryl-CoA deacetylase (EC 3.5.1.51), sialate O-acetylesterase (EC 3.1. 1.53), acetoxybutynylbithiophene deacetylase (EC 3.1.1.54), acetylsalicylate deacetylase (EC 3.1.1.55), methylumbelliferyl-acetate deacetylase (EC 3.1.1.56), bis (2-ethylhexyl) phthalate esterase (EC 3.1.1.60), 5- ( 3,4-diacetoxybut-1-ynyl) -2,2'-bithiophene deacetylase (EC 3.1.1.66), acetyl xylan esterase (EC 3.1.1.72), feruloyl esterase (EC 3.1.1.73), cutinase (EC 3.1.1.74) , Acetylmalazine esterase (EC 3.1.1.80), acetyl-CoA hydrolase (EC 3.1.2. 1), palmitoyl-CoA hydrolase (EC 3.1.2.2), glutathione thiolesterase (EC 3.1.2.7), [citrate (pro-3S) -lyase] thiolesterase (EC 3.1.2.16), ADP-dependent short-chain acyl -CoA hydrolase (EC 3.1.2.18), acyl-CoA hydrolase (EC 3.1.2.20), aryldialkylphosphatase (EC 3.1.8.1), amidase (EC 3.5.1.4), aryl-acylamidase (EC 3.5.1.13), N-acetylglucosamine 6-phosphate deacetylase (EC 3.5.1.25), chitin deacetylase (EC 3.5.1.41), N-acyl-D-amino acid deacylase (EC 3.5.1.81), citrate (pro-3S) -lyase (EC 4.1. 3.6), Citramalate lyase (EC 4.1.3.22), Acetate-CoA ligase (EC 6.2.1.1), Acetate-CoA ligase (ADP-forming) (EC 6.2.1.13), Acetoacetate-CoA ligase (EC 6.2.1.16), Propionate-CoA ligase (EC 6.2.1.17), [Citrate (pro-3S) -lyase] ligase (EC 6.2.1.22), benzoate-CoA ligase (EC 6.2.1.25) and phenylacetate-CoA ligase (EC 6.2.1.30) ,

As examples of oxime-degrading enzymes which can be used according to the invention, mention may be made in particular of aldehyde oxidase (EC 1.2.3.1), pyridoxal 5'-phosphate synthase (EC 1.4.3.5), cytochrome b5 reductase (EC 1.6.2.2), hydroxylamine reductase (NADH) ( EC 1.7.1.10), 4- Hydroxyphenylacetaldehyde oxime monooxygenase (EC 1.14.13.68), Camphor 5-monooxygenase (EC 1.14.15.1), isobutyraldoxime O-methyltransferase (EC 2.1.1.91), 3-hydroxymethylcephem carbamoyltransferase (EC 2.1.3.7), diacylglycerol O-acyltransferase (EC 2.3 .1.20), long-chain alcohol O-fatty acyltransferase (EC 2.3.1.75), oximinotransferase (EC 2.6.3.1), beta-lactamase (EC 3.5.2.6), aliphatic aldoxime dehydratase (EC 4.99.1.5), indoleacetaldoxime dehydratase (EC 4.99.1.6) and phenylacetaldoxime dehydratase (EC 4.99.1.7).

As examples of benzamide-degrading enzymes which can be used according to the invention, mention may be made in particular of NAD (P) H dehydrogenase (quinone) (EC 1.6.5.2), flavin-containing monooxygenase (EC 1.14.13.8), polygalacturonate 4-alpha-galacturonosyltransferase (EC 2.4.1.43) , Amidase (EC 3.5.1.4), urethanase (EC 3.5.1.75), nitrilase (EC 3.5.5.1) and aliphatic nitrilase (EC 3.5.5.7).

As whole-cell catalysts which naturally produce methanol-degrading enzymes, in particular microorganisms selected from Acetoctobacter methanolicus, Acetobacter pasteurianus, Achromobacter methanolophila, Acidomonas methanolica, Aeropyrum pernix, Alteromonas sp., Alteromonas thalassomethanolica, Aminomonas aminovorus, Amycolatopsis methanolica, Ancylobacter sp., Bacillus methanolicus, Bacillus sp., Bacillus stearothermophilus, Basidiomycete sp., Butyribacterium methylotrophicum, Candida boidinii, Candida cariosilignicola, Candida glabrata, Candida methanolica, Candida methanosorbosa, Candida molischiana, Candida sonorensis, Candida sp., Candida succiphila, Clostridium thermosaccharolyticum, Desulfotomaculum solfataricum, Hansenula polymorpha , Hansenula polymorphe, Hyphomicrobium denitrificans, Hyphomicrobium sp., Lactobacillus brevis, Methanolobus tindarius, Methanomicrococcus leaficola, Methanomonas methylovora, Methanomonas methylovora subsp. Thiaminophila, methanosarcina mazei, Methanosphaera stadtmanae, Methylobacillus glycogenes, Methylobacillus methanolovorus sp., Methylobacterium aminovorans, fujisawaense methylobacterium extorquens, methylobacterium, lusitanum methylobacterium, mesophilicum methylobacterium, organophilum methylobacterium, methylobacterium radiotolerans, rhodesianum methylobacterium, rhodinum methylobacterium, Methylobacterium sp., Suomiense methylobacterium, Methylobacterium zatmanii, Methylococcus capsulatus, Methylocystis sp., Methylomicrobium album, Methylomonas clara, Methylomonas methanica, Methylomonas probus, Methylomonas sp., Methylophaga marina, Methylophaga talassica, Methylophilus methylotrophus, Methylophilus sp., Methylosinus spoήum, Methylosinus trichosporium, Methylovorus glucosotrophus, Microcycle eburneus , Moorella mulderi, Mycobacterium gastri, Mycobacterium smegmatis, Ogataea pini, Paracoccus alcaliphilus, Paracoccus denitrificans, Paracoccus sp., Peniophora gigantean, Phanerochae chrysosporium, Pichia aganobii, Pichia angusta, Pichia cellobiosa, Pichia lindneri, Pichia methanolica, Pichia minuta var. minuta, Pichia pastoris, Pichia sp., Polyporus obtusus, Poria contigua, Protaminobacter candidus, Protaminobacter ruber subsp. machidanus, Protaminobacter thiaminophaga, Protaminobacter thiaminophagus, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas insueta, Pseudomonas methanolica, Pseudomonas polysaccharogenes, Pseudomonas putida, Pseudomonas sp., Pseudomonas viscogena, Radulum casearium, Rhodococcus rubber, Rhodococcus sp., Rhodopseudomonas acidophila, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Sporothrix nivea, Stenotrophomonas maltophilia, Streptomyces hygroscopicus, Sulfolobus solfataricus, Thermoanaerobacter brockii, Thermoanaerobacter ethanolicus, Thermomicrobium roseum, Thermotoga lettingae, Torulopsis domercqii, Torulopsis enokii, Torulopsis glabrata, Torulopsis ingeniosa, Torulopsis methanolovescens, Torulopsis methanophiles, Torulopsis methanosorbosa, Torulopsis methanothermo, Torulopsis sonorensis, Trichoderma lignorum, Wickerhamiella domercqiae and Xanthobacter autotrophicus.

To obtain an enzyme-containing preparation, a cell disruption of a microorganism which produces the desired enzyme, in particular one of the abovementioned microorganisms, be carried out and either the cell disruption can be used as such or the enzyme is further purified from this cell disruption and / or enriched.

Alternatively, the desired enzyme can also be expressed heterologously in other microorganisms, in particular bacteria, and the cell disruption can then also be used here, or else the enzyme can be further purified and / or enriched from the cell disruption.

Some of the enzymes mentioned need to react the by-product of other reactants, which are shown in Tables 1 to 4, for example. For example, depending on the enzyme chosen, it may be necessary to add another reactant selected from NAD ⁺ , sucrose or cellobiose, provided that it is not already present in the cell disruption and / or is produced by the whole-cell biocatalyst.

This further reactant is then incorporated into the crosslinkable preparation, preferably together with the enzyme and / or the whole-cell catalyst, or applied to the crosslinkable preparation together with the enzyme and / or the whole-cell catalyst.

Furthermore, it is of course also possible according to the invention that, for example, the enzyme and / or the whole-cell catalyst is incorporated in the crosslinkable preparation and the further reactant is introduced later into the crosslinkable preparation or applied to the crosslinkable preparation. It is likewise possible, conversely, for the further reactant to be contained in the crosslinkable preparation and for the enzyme and / or the whole-cell catalyst to be introduced later into the crosslinkable preparation or applied to the crosslinkable preparation. Furthermore, it is of course also possible that enzyme and / or whole-cell catalyst and further reactant both later introduced into the crosslinkable preparation or to the crosslinkable preparation are applied, but not in a single, but in two temporally successive steps.

Some reaction reactions can give rise to a product that itself is not particularly desirable. For example, the alcohol oxidase catalyzes the conversion of methanol and oxygen to formaldehyde and hydrogen peroxide. If such an enzyme as the alcohol oxidase is used, then other substances are preferably used which intercept or degrade these undesired secondary products. These may be, in particular, chemical reagents-in the case of formaldehyde, for example, amines-or else further enzymes and / or whole-cell catalysts which degrade or convert these undesired products. In this case, in particular, it is also possible to use a whole-cell catalyst which has a plurality of enzyme activities, such that, for example, the conversion of methanol into formaldehyde and its further degradation are catalysed by a single whole-cell catalyst.

According to the invention, the enzymes and / or whole-cell catalysts can be added in any form established according to the prior art. These include, for example, by granulation, extrusion, spray drying or lyophilization of the enzyme solution and / or cell dispersion together with other substances, preferably polymers, solid preparations or, especially in liquid or gel formulated solutions of the enzymes, advantageously as concentrated as possible, low in water and / or mixed with stabilizers. Alternatively, the enzymes and / or cells for both the solid and liquid dosage forms may be adsorbed and / or encapsulated on a solid support.

The encapsulated form lends itself to protecting the enzymes and / or cells from other ingredients or to allow controlled release. Depending on the size of these capsules, a distinction is made according to MiIIi, micro and nano capsules.

To produce the capsules containing enzyme and / or whole-cell catalyst, the enzyme and / or the whole-cell catalyst may first be mixed with a germinatable matrix substance such as sodium aiginate, agarose or Sephadex and optionally a filler such as quartz sand or silica. By precipitation of the mixture thus obtained, for example in an ion or temperature precipitation bath, it is possible to obtain spherical particles which, in principle, can already be used as such according to the invention. Preferably, however, further enveloping of the spherical particles thus obtained with an inert protective layer.

Alternatively, for example, encapsulation may also be accomplished by spray-drying or extruding the enzyme solution or cell dispersion together with a preferably natural polymer, or by embedding the enzyme or cells in a gel or core-shell type structure where the core is filled with water -, air and / or chemical impermeable Protective layer is coated. If desired, further active ingredients, for example stabilizers, emulsifiers, pigments or dyes may be applied in superposed layers. Such capsules are prepared 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.

The shell or protective layer of the capsules and / or the carrier may consist of natural, synthetic or semisynthetic materials, as well as mixtures thereof. As shell materials of natural origin, for example, saccharides or polysaccharides such as gum arabic, agar-agar, agarose, sucrose, maltodextrins, alginic acid and its salts, in particular sodium or calcium alginate, chitosan, starch, dextran or shellac, peptides, protein hydrolysates or polypeptides such as collagen, Albumin or gelatin, fats, fatty acids, cetyl alcohol, lecithins or waxes. In particular, chemically modified celluloses, in particular cellulose esters and ethers, such as cellulose acetate, ethylcellulose, hydroxypropylcellulose, hydroxypropylmethylcellulose, carbylmethylcellulose or nitrocellulose derivatives, and starch derivatives, in particular ethers and esters of amylose and amylopectin, can be used as semisynthetic shell materials. As synthetic shell materials, for example, polymers such as polyacrylates, polyamides, polyvinyl alcohol, polyvinyl acetate or polyvinylpyrrolidone can be used. In particular, compounds such as alginate-polylysine alginate, nylon, silicone rubber, nylon-polyethyleneimine, polylactic acid, polyglycolic acid, chitosan alginate, cellulose sulfate poly (dimethyldiallyl) - ammonium chloride, hydroxyethyl methacrylate-methyl methacrylate, chitosan carboxymethylcellulose or hydrogels for the production of the coating and / or used as a carrier.

The enclosure may in particular comprise polyelectrolyte complexes. Polyelectrolyte complexes are formed by interaction between polycations and polyanions. As polycations come here in particular natural products such as chitosan, but also synthetic polymers such as polyethyleneimine, Polydiethyldiallylammoniumchlorid, copolymers of diallyl ammonium salts and acrylamides, quaternized vinylpyrrolidine / vinylimidazole polymers, condensation products of polyglycols and amines, cationic silicone polymers such as amodimethicones, copolymers of adipic acid and Dimethylaminohydroxypropyldiethylentriamin, copolymers of Acrylic acid and dimethyldiallylammonium chloride, polyaminopolyamides and their crosslinked water-soluble polymers, condensation products of dihaloalkylene such as bis-dimethylamino-1, 3-propane and quaternized ammonium salt polymers into consideration. Examples of suitable polyanions are water-soluble cellulose derivatives, in particular carboxymethyl cellulose or cellulose sulfate, pectins and alginates, carboxylated or succinylated chitosan derivatives or synthetic polymers such as polyacrylic or polymethacrylic acids. In a preferred embodiment, the enzyme and / or the whole-cell catalyst is granulated together with a chemically inert carrier material and a chemically inert binder. The support material may in this case be selected from inorganic substances, such as, for example, clays, silicates or sulfates, in particular talc, silicic acids, metal oxides, in particular aluminum oxides and / or titanium dioxide, silicates, in particular phyllosilicates, sodium aluminum silicates, bentonites and / or aluminosilicates (zeolites). However, it may also be an organic compound such as polyvinyl alcohol (PVA), in particular at least partially hydrolyzed PVA.

Suitable binders in this embodiment are in particular non-crosslinked, polymeric compounds selected from the group of polyacrylates, polymethacrylates, methacrylic acid-ethyl acrylate copolymers, polyvinylpyrrolidones, polysaccharides or substituted polysaccharides, in particular cellulose ethers, and / or polyvinyl alcohols (PVA), preferably partially hydrolyzed polyvinyl alcohols and / or ethoxylated polyvinyl alcohols and their copolymers and mixtures. Due to their adsorption properties and their simultaneously present binding effect, PVA or its derivatives are thus suitable both as a carrier material and as a binder component. They can therefore be used as binders, if they are not already used as a carrier material.

Furthermore, it is possible according to the invention to assemble two or more enzymes together so that a single granulate has a plurality of enzyme activities.

The coating is preferably chosen so that upon application, the release of the enzyme and / or whole-cell catalyst is easy.

Furthermore, for example, metal, ceramic or limestone-based supports can also be used for immobilizing the enzyme and / or the whole-cell catalyst.

Apart from encapsulation and immobilization, the enzyme and / or the whole-cell catalyst can also be protected by addition of stabilizing substances during storage against damage such as inactivation, denaturation or disintegration such as by physical influences, oxidation or proteolytic cleavage.

One group of stabilizers useful in this invention are reversible protease inhibitors. Benzamidine hydrochloride, borax, boric acids, boronic acids or their salts or esters are frequently used for this purpose, including, in particular, derivatives with aromatic groups, for example ortho, meta or para-substituted phenylboronic acids, in particular 4-formylphenylboronic acid, or the salts or Esters of the compounds mentioned. Also, peptide aldehydes, that is oligopeptides with a reduced C-terminus, especially those of 2 to 50 monomers are used for this purpose. The peptidic reversible protease inhibitors include including ovomucoid and leupeptin. Also, specific, reversible peptide inhibitors for the protease subtilisin and fusion proteins from proteases and specific peptide inhibitors are suitable.

Other enzyme stabilizers are amino alcohols such as mono-, di-, triethanol- and -propanolamine and mixtures thereof, aliphatic carboxylic acids up to C ₁₂ , such as succinic acid, other dicarboxylic acids or salts of said acids. End-capped fatty acid amide alkoxylates are also suitable for this purpose. Certain organic acids used as builders are additionally capable of stabilizing a contained enzyme.

Lower aliphatic alcohols, but especially polyols such as glycerol, ethylene glycol, propylene glycol or sorbitol are other frequently used enzyme stabilizers. Di-glycerol phosphate also protects against denaturation due to physical influences. Likewise, calcium and / or magnesium salts are used, such as calcium acetate or calcium formate.

Polyamide oligomers or polymeric compounds such as lignin, water-soluble vinyl copolymers or cellulose ethers, acrylic polymers and / or polyamides stabilize the enzyme preparation, inter alia, against physical influences or pH fluctuations. Polyamine N-oxide containing polymers act simultaneously as enzyme stabilizers and as dye transfer inhibitors. Other polymeric stabilizers are linear C ₈ -C ₁₈ polyoxyalkylenes. Also, alkylpolyglycosides can stabilize the enzymatic components of the agent according to the invention and are able, preferably, to additionally increase their performance.

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

Particular preference is given to using combinations of stabilizers, for example of polyols, boric acid and / or borax, the combination of boric acid or borate, reducing salts and succinic acid or other dicarboxylic acids or the combination of boric acid or borate with polyols or polyamino compounds and with reducing salts. The effect of peptide-aldehyde stabilizers is favorably enhanced by the combination with boric acid and / or boric acid derivatives and polyols, and still further by the additional action of divalent cations, such as calcium ions.

As far as the enzyme and / or the whole-cell catalyst is incorporated into the polymerizable preparation, it is necessary that the enzyme and / or the whole-cell catalyst be in a dry state. Insofar as the enzyme and / or the whole-cell catalyst only during the application of the polymerizable preparation is added, enzyme and / or whole-cell catalyst can also be present in liquid, gel or pasty form.

To produce such liquid, gelatinous or pasty forms according to the invention, the enzymes and / or whole cell catalysts can be added starting from a prior art protein recovery and preparation in concentrated aqueous or nonaqueous solution, suspension or emulsion, but also in gel form or encapsulated or as dried powder. Such preparations according to the invention are generally prepared by simply mixing the ingredients, which can be added in bulk or as a solution in an automatic mixer.

Solvents which can be used in liquid, gelatinous or pasty preparations originate, for example, from the group of monohydric or polyhydric alcohols, alkanolamines or glycol ethers, provided they are miscible with water in the concentration range indicated. The solvents are preferably selected from ethanol, n- or i-propanol, butanols, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, diethylene glycol ethyl ether, propylene glycol methyl, -ethyl or -propyl ether, dipropylene glycol monomethyl, or -ethyl ether, diisopropylene glycol monomethyl, or ethyl ether, methoxy, ethoxy or butoxy triglycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether and mixtures of these solvents.

To adjust the viscosity, one or more thickeners or thickening systems can be contained in the liquid, gelatinous or pasty preparation. These high-molecular substances, which are also called swelling agents, usually absorb the liquids and swell up to finally pass into viscous true or colloidal solutions. Suitable thickeners are inorganic or polymeric organic compounds. The inorganic thickeners include, for example, polysilicic acids, clay minerals such as montmorillonites, zeolites, silicas and bentonites. The organic thickeners are derived from the groups of natural polymers, modified natural polymers and fully synthetic polymers. Such naturally derived polymers include, for example, agar-agar, carrageenan, tragacanth, gum arabic, alginates, pectins, polyoses, guar gum, locust bean gum, starch, dextrins, gelatin and casein. Modified natural products, which are used as thickeners, come mainly from the group of modified starches and celluloses. By way of example, carboxymethylcellulose and other cellulose ethers, hydroxyethyl and propylcellulose and core flour ethers may be mentioned here. Fully synthetic thickeners are polymers such as polyacrylic and polymethacrylic compounds, vinyl polymers, polycarboxylic acids, polyethers, polyimines, polyamides and polyurethanes. Crosslinkable preparations

Preferably, the crosslinkable preparations according to the invention are selected from adhesive, sealant and coating compounds, insulating materials, as well as sealants and adhesives. Particularly preferred sealants are jointing compounds, silicone adhesive, carpet fixer and tile adhesive.

Sealants and in particular jointing compounds typically contain organic polymers and, in many cases, mineral or organic fillers and other additives.

Suitable polymers are, for example, thermoplastic elastomers, as described in DE-A-3602526, preferably polyurethanes and acrylates. Suitable polymers are also mentioned in the published specifications DE-A-3726547, DE-A-029504 and DE-A-4009095 as well as in DE-A-19704553 and DE-A-4233077, to which reference is hereby fully made.

According to the invention, the equipment of the sealants according to the invention can be carried out both in the uncured or under 60 ⁰ C cured state. In the context of the invention, sealants are materials according to DIN EN 26927, in particular those which cure plastically or elastically as sealants. The sealants of the invention may contain all additives typical of the corresponding sealants, such as typical thickeners, reinforcing fillers, crosslinkers, crosslinking catalysts, pigments, adhesives or other bulk extenders. The active ingredients to be used can be prepared by dispersing in a manner known to those skilled in the art, for example by the use of dispersing equipment, kneaders, planetary mixers, etc., excluding moisture and oxygen, both in the finished and in parts of these sealants or together with one or more components Sealants are incorporated.

Even the treatment of already cured, crosslinked sealing compound surfaces can be carried out by applying solutions or suspensions of the enzymes according to the invention and / or whole-cell catalysts, wherein the enzyme and / or the whole-cell catalyst can be transported by swelling or diffusion into the sealant.

Sealants which can be used according to the invention can be produced both on silicone, urethane and on acrylic base or about on MS polymer basis. Urethane-based sealants are disclosed, for example, in Ullmann's Encyclopedia of Industrial Chemistry (8th Edition 2003, Chapter 4) and US 4,417,042. Silicone sealants are known to the person skilled in the art, for example from EP 0 118 030 A, EP 0 316 591 A, EP 0 327 847 A, EP 0 553 143 A, DE 19549 425 A and US 4,417,042. Examples of acrylic sealants are disclosed inter alia in WO 01/09249 or US 5,077,360. Examples of sealants based on MS polymers are described, for example, in EP 0 824 574, US Pat 3,971,751, US 4,960,844, US 3,979,344, US 3,632,557, DE 4029504, EP 601 021 or EP 370 464.

In a particularly preferred embodiment, the jointing compound is a silicone-based jointing compound, in particular selected from acetate, alkoxy, oxime, benzamide and amine silicones. The Fungedichtungsmasse contains here preferably as polyorganosiloxanes and as organosilicon compounds with hydrolyzable groups compounds such as are described in the patent US 5,378,406 in the amounts specified therein, the relevant disclosure of which is hereby made the subject of this patent application.

In particular, systems crosslinking at room temperature, for example as described in EP 0 327 847 or US Pat. No. 5,077,360, are preferred. These may be single-component or multicomponent systems, it being possible for catalyst and crosslinker to be present separately in the multicomponent systems (for example disclosed in US Pat. Nos. 4,891,400 and 5,502,144), or other so-called silicone RVT 2K systems, in particular platinum-free systems ,

Particularly preferred are so-called one-component systems which contain all ingredients for the construction of a sealant, are stored with the conclusion of humidity and / or atmospheric oxygen and cure at the site under reaction with the humidity. It is also possible to use so-called silicone neutral systems in which the reaction of crosslinking agents with the water of the ambient air does not lead to corrosive, acidic, basic or odor-intensive fission products. Examples of such systems are disclosed in DE 19549 425, US 4,417,042 or EP 0 327 847.

The sealants and especially jointing compounds may contain aqueous or organic solvents. Suitable organic solvents are hydrocarbons such as cyclohexane, toluene or else xylene or petroleum ether. Other solvents include ketones such as methyl butyl ketone or chlorinated hydrocarbons.

Furthermore, the sealants may contain other rubbery polymers. Here come relatively low molecular weight, commercially available types of polyisobutylene, polyisoprene or polybutadiene styrene in question. The co-use of degraded Naturkauschuk or neoprene rubber is possible. Here, even at room temperature still flowable types can be used, which are often referred to as "liquid rubber".

The sealing compounds of the invention can be used to connect or seal the most diverse materials. This is intended primarily for use on concrete, glass, plaster and / or enamel, as well as ceramics and porcelain. But also the bonding or sealing of moldings or profiles made of aluminum, steel, zinc or even plastics such as PVC or polyurethanes or acrylic resins is possible. Finally, the sealing of wood or wood materials with a variety of other materials is mentioned.

The stability of jointing compounds is usually achieved by the addition of finely divided solids - also called fillers. These can be distinguished in such organic and inorganic type. As inorganic fillers, for example silicic acid / silica (coated or uncoated), chalk-coated or uncoated, and / or zeolites may be preferred. The latter can also act as a desiccant. As organic filler z. B. PVC powder into consideration. The fillers generally contribute significantly to the sealant having a necessary internal hold after application such that leakage or debound of the sealant from vertical joints is prevented. The cited additives or fillers can be classified into pigments and thixotropic fillers, also abbreviated as thixotropic agents.

Suitable thixotropic agents are the known thixotropic agents such as bentones, kaolins or organic compounds such as hydrogenated castor oil or derivatives thereof with polyfunctional amines or the reaction products of stearic acid or ricinoleic acid with ethylenediamine. Particularly advantageous is the co-use of silica, in particular of silica from pyrolysis has been found. In addition, suitable thixotropic agents are essentially swellable polymer powders. Examples of these are polyacrylonitrile, polyurethane, polyvinyl chloride, polyacrylic acid esters, polyvinyl alcohols, polyvinyl acetates and the corresponding copolymers. Particularly good results can be obtained with finely divided polyvinyl chloride powder. In addition to the thixotropic agents, it is also possible to use additional adhesion promoters, such as, for example, mercaptoalkylsilane. Here it has proven to be expedient to use a Monomercaptoalkyltrialkoxysiian. Commercially available is, for example, mercaptopropyltrimethoxysilane.

The properties of a jointing compound can be further improved if further components are added to the plastic powder used as thixotropic agent. These are substances that fall under the category of plasticizers used for plastics or swelling agents and swelling aids.

It come z. As plasticizers, in particular for the sealing compounds based on urethane or acrylic from the class of phthalic acid into consideration. Examples of applicable compounds from this class of substances are dioctyl phthalate, dibutyl phthalate and benzyl butyl phthalate. Further suitable classes of substances are chloroparaffins, alkylsulfonic acid esters of, for example, phenols or cresols, and fatty acid esters. For the silicone sealants are as plasticizers silicone oils, particularly preferably polydimethylsiloxanes, and hydrocarbons and / or mixtures thereof, of which especially hydrocarbons or mixtures thereof having a boiling point of greater than 200 ° C, especially greater 230 ⁰ C, well suited.

Suitable source aids are those low molecular weight organic substances which are miscible with the polymer powder and the plasticizer. Such source aids can be found in the relevant plastic and polymer manuals for the expert. Preferred swelling aids for polyvinyl chloride powder are esters, ketones, aliphatic hydrocarbons, aromatic hydrocarbons and aromatic hydrocarbons with alkyl substituents.

Pigments and dyes used are the substances known for these uses, such as titanium dioxide, iron oxides and carbon black

To improve the storage stability known stabilizers such as benzoyl chloride, acetyl chloride, Toluolsulfonsäuremethylester, carbodiimides and / or polycarbodiimides are added to the sealants. As particularly good stabilizers, olefins having 8 to 20 carbon atoms have been found. In addition to the stabilizing effect, these can also fulfill the tasks of plasticizers or swelling agents. Preference is given to olefins having 8 to 18 carbon atoms, especially when the double bond is located in the 1,2-position. Best results are obtained when the molecular structure of these stabilizers is linear.

A further object of the present invention is a method for determining the amount of volatile by-product released in crosslinking processes, comprising the steps of: a) placing a solvent-containing shell on a larger shell enclosing it; b) on the peripheral free surface of the larger shell c) the solvent is optionally mixed, preferably using a stirring fish, d) after completion of the crosslinking reaction, the content of by-product contained in the solvent is determined analytically.

The solvent is preferably water, the volatile by-product preferably being a water-soluble by-product, in particular methanol. embodiments

Example 1: Measuring method

a) Method 1 (single-chamber system):

To investigate the liberated methanol of a methoxysilicone sealant was carried out - after completion of curing - the leaching of the air space of an airtight 50 ml to 1 L glass bottle with water. The curing took place over 12 to 48 hours. For leaching 10 to 100 ml of water were used. During curing, the bottle was stored horizontally (see Fig. 1). The product had no direct water contact. After curing at room temperature and 1, 5 h at 4 ° C, the vessels were vigorously shaken for 10 minutes. Incubation at 4 ° C causes a lower saturation limit for methanol in the gas phase. The resulting solutions were then analyzed by GC and the methanol content quantified.

b) Method 2 (two-chamber system):

The investigation of the liberated methanol of a methoxysilicone sealant was carried out - after completion of curing - in a hermetically sealed two-chamber vessel (see Fig. 2). The curing took place over 12 to 48 hours. For methanol absorption 3 to 100 ml of water were used. The product had no direct water contact. During the curing at room temperature and for 1, 5 h at 4 ° C, the water was constantly mixed to efficiently absorb the methanol. The outer plastic shell contains the product, the inner glass shell is filled with water. The water is stirred for better absorption of the liberated methanol. The outer shell is sealed airtight. The incubation at 4 ⁰ C causes a lower saturation limit for methanol in the gas phase. The resulting solutions were then analyzed by GC and the methanol content quantified.

Example 2 Determination of the liberated methanol in the one and two-chamber system The amount of liberated methanol was determined in the single-chamber system (method 1) and in the two-chamber system (method 2). It has been found that the amount of detectable released methanol can be better determined with the two-chamber system than with the single-chamber system. While it was possible to detect 1.2% by weight of methanol with the single-chamber system, it was possible with the two-chamber system to detect 1.6% by weight of methanol O ^', based in each case on the total amount of sealing compound used.

Example 3: Methanol degradation by the alcohol oxidase from Candida boidinii The bicameral system was used as described in Example 1. After applying the sealant, a powder of Candida boidinii alcohol oxidase was evenly distributed on the applied sealant and then the amount as described above released methanol determined. The amount of methanol released could thus be reduced by 15%.

Example 4: Methanol degradation by a crude cell extract from Pichia

The bicameral system was used as described in Example 1. After applying the

Sealant was applied to a cell crude extract of Pichia evenly on the

Spreading sealant and then as described above, the amount of released

Methanol determined. The amount of methanol released could thus be reduced by more than 50%.

Example 5: Methanol degradation by a mixture of alpha-glucosidase and D-cellobiose The bicameral system was used as described in Example 1. After applying the sealant, a mixture of alpha-glucosidase and D-cellobiose was evenly distributed on the applied sealant and then the amount of released methanol was determined as previously described. The addition of D-cellobiose is required here, since the alpha-glucosidase in addition to the methanol requires another substrate. The amount of methanol released could thus be reduced by about 50%.

Example 6: Overview of enzymes which can be used according to the invention

Table 1: Methanol-degrading enzymes

Table 2: Acetate-degrading enzymes Table 3: Oxime-degrading enzymes

Table 4: Benzamide degrading enzymes

pictures

In Fig. 1, a 1 L glass bottle is shown with introduced jointing compound. The amount of methanol released from the methoxysilicone is determined for comparison on the one hand with untreated and on the other hand with enzymes or whole-cell catalysts treated jointing compounds.

In Fig. 2, an inventive two-chamber system is shown. In the inner chamber is water, which is stirred with a stirring fish. On the bottom of the outer chamber, the jointing compound is applied and then optionally applied an enzyme or whole-cell catalyst-containing solution or suspension and then determines the content of methanol in the aqueous solution.

Claims

claims

1. Use of enzymes and / or whole-cell catalysts for the removal of by-products from crosslinkable preparations

2. Use according to claim 1, characterized in that the crosslinkable preparation is a preparation based on silicone, urethane, acrylic or on MS polymer.

3. Use according to claim 1 or 2, characterized in that it is a silane-curing preparation in the preparation.

4. Use according to claim 3, characterized in that the silane-curing preparation contains acetate, alkoxy, oxime, benzamide and / or amine silicones.

5. Use according to one of claims 1 to 4, characterized in that it is the by-product is an alcohol, an organic acid, an oxime, a benzamide or an amine.

Use according to any one of Claims 1 to 5, characterized in that the by-product is a toxic, odorous, corrosive, acidic or basic by-product.

7. Use according to one of the preceding claims, characterized in that it is the enzyme is an alcohol degrading enzyme.

8. Use according to claim 7, characterized in that it is a methanol-degrading enzyme in the alcohol-degrading enzyme.

9. Use according to claim 8, characterized in that the methanol-degrading enzyme is selected from alcohol dehydrogenases, methanol dehydrogenase, cyclohexanol dehydrogenase, cholesterol oxidase, alcohol oxidase, formaldehyde dismutase, catalase, methanol-5-hydroxybenzimidazolylcobamide Co methyltransferase, alcohol O-acetyltransferase, sucrose phosphorylase, levansucrase, O-acetyl homoserine aminocarboxypropyltransferase, alcohol sulfotransferase, fatty acyl ethyl ester synthase, acid phosphatase, phospholipase D, venom exonuclease, beta-glucosidase, alpha galactosidase , beta-mannosidase, xylan-1,4-beta-xylosidase, beta-N-acetylhexosaminidase, L-iduronidase, glucan-1, 6-alpha-isomaltosidase, glycopeptide-alpha-N-acetylgalactosaminidase, endoglycosylceramidase, chymotrypsin and omega-amidase ,

10. Use according to one of claims 1 to 6, characterized in that it is the enzyme is an acetic acid or acetate-degrading enzyme.

11. Use according to claim 10, characterized in that the acetic acid or acetate-degrading enzyme is selected from hydroxymethylglutaryl-CoA reductase (NADPH), 3-keto steroid reductase, aldehydes ferredoxin oxidoreductase, manganese peroxidase, arsenate reductase (donor), selenates reductase, phosphoribosylglycinamide formyltransferase, cysteine synthase, acetate kinase, carbamate kinase, kinase, butyrate kinase, propionate kinase, propionate CoA-transferase, acetates CoA-transferase, butyrate-acetoacetate CoA-transferase, glutaconate CoA-transferase, 5-hydroxypentanoate CoA transferase, carboxylesterase, arylesterase, triacylglycerol lipase, acetylesterase, acetylcholinesterase, cholinesterase, tropinesterase, pectinesterase, sterol esterase, retinyl palmitate esterase, dihydrocoumarin hydrolase, lipoprotein lipase, cephalosporin C deacetylase, alpha-amino acid esterase, 4-methyl oxaloacetate esterase , 1-alkyl-2-acetylglycerophosphocholines esterase, Wax-ester hydro lase, 4-acetamidobutyryl-CoA deacetylase, sialate O -acetylesterase, acetoxybutynylbithiophene deacetylase, acetylsalicylate deacetylase, methylumbelliferyl acetate deacetylase, bis (2-ethylhexyl) phthalate esterase, 5- (3,4-diacetoxybut-1-ynyl) -2, 2'-bithiophene deacetylase, acetyl xylan esterase, feruloyl esterase, cutinase, acetyl-maline esterase, acetyl-CoA hydrolase, palmitoyl-CoA hydrolase, glutathione thiolesterase, [citrate (pro-3S) -lyase] thiolesterase, ADP-dependent short-chain acyl-CoA hydrolase, acyl-CoA hydrolase, aryldialkylphosphatase, amidase, aryl-acylamidase, N-acetylglucosamine-6-phosphate deacetylase, chitin deacetylase, N-acyl-D-amino-acid deacylase, citrate (pro-3S) -lyase, Citramalate lyase, Acetate-CoA ligase, Acetate-CoA ligase (ADP-forming), Acetoacetate-CoA ligase, Propionate-CoA ligase, [Citrate (pro-3S) - lyase] ligase, Benzoate-CoA ligase and Phenylacetate-CoA ligase.

12. Use according to one of claims 1 to 6, characterized in that it is the enzyme is an oxime-degrading enzyme.

13. Use according to one of claims 1 to 6, characterized in that the oxime-degrading enzyme is selected from aldehyde oxidase, pyridoxal 5'-phosphate synthase, cytochrome b5 reductase, hydroxylamine reductase (NADH), 4-hydroxyphenylacetaldehyde oxime monooxygenase, Camphor 5-monooxygenase, isobutyraldoxime O-methyltransferase, 3-hydroxymethylcephem carbamoyltransferase, diacylglycerol O-acyltransferase, long-chain alcohol O-fatty acyltransferase, oximinotransferase, beta-lactamase, aliphatic aldoxime dehydratase, indoleacetaldoxime dehydratase and phenylacetaldoxime dehydratase.

14. Use according to one of claims 1 to 6, characterized in that it is the enzyme is a benzamide degrading enzyme.

15. Use according to claim 14, characterized in that the benzamide-degrading enzyme is selected from NAD (P) H dehydrogenase (quinone), flavin-containing monooxygenase, polygalacturonates 4-alpha-galacturonosyltransferase, amidase, urethanase, nitrilase and Aliphatic nitrilase.

16. Use according to claim 1, characterized in that the whole-cell catalyst is selected from Acetobacter methanolicus, Acetobacter pasteurianus, Achromobacter methanolophila, Acidomonas methanolica, Aeropyrum pernix, Alteromonas sp., Alteromonas thalassomethanolica, Aminomonas aminovorus, Amycolatopsis methanolica, Ancylobacter p., Bacillus methanolicus, Bacillus sp., Bacillus stearothermophilus, Basidiomycete sp., Butyribacterium methylotrophicum, Candida boidinii, Candida cariosilignicola, Candida glabrata, Candida methanolica, Candida methanosorbosa, Candida molischiana, Candida sonorensis, Candida sp., Candida succiphila, Clostridium thermosaccharolyticum, Desulfotomaculum solfataricum, Hansenula polymorpha , Hansenula polymorpha, Hyphomicrobium denitrificans, Hyphomicrobium sp., Lactobacillus brevis, Methanolobus tindarius, Methanomicrococcus leaficola, Methanomonas methylovora, Methanomonas methylovora subsp. Thiaminophila, methanosarcina mazei, Methanosphaera stadtmanae, Methylobacillus glycogenes, Methylobacillus methanolovorus sp., Methylobacterium aminovorans, fujisawaense methylobacterium extorquens, methylobacterium, lusitanum methylobacterium, mesophilicum methylobacterium, organophilum methylobacterium, methylobacterium radiotolerans, rhodesianum Methylobacteπum, rhodinum methylobacterium, Methylobacterium sp., Suomiense methylobacterium, Methylobacterium zatmanii, Methylococcus capsulatus, Methylocystis sp., Methylomicrobium album, Methylomonas clara, Methylomonas methanica, Methylomonas probus, Methylomonas sp., Methylophaga marina, Methylophaga talassica, Methylophilus methylotrophus, Methylophilus sp., Methylosinus sporium, Methylosinus trichosporium, Methylovorus glucosotrophus, Microcycle eburneus , Moorella mulderi, Mycobacterium gastri, Mycobacterium smegmatis, Ogataea pini, Paracoccus alcaliphilus, Paracoccus denitrificans, Paracoccus sp., Peniophora gigantean, Phanerochae chrysosporium, Pichia aganobii, Pichia angusta, Pichia cellobiosa, Pichia lindneri, Pichia methanolica, Pichia minuta var. minuta, Pichia pastoris, Pichia sp., Polyporus obtusus, Poria contigua, Protaminobacter candidus, Protaminobacter ruber subsp. machidanus, Protaminobacter thiaminophaga, Protaminobacter thiaminophagus, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas insueta, Pseudomonas methanolica, Pseudomonas polysaccharogenes, Pseudomonas putida, Pseudomonas sp., Pseudomonas viscogena, Radulum casearium, Rhodococcus rubber, Rhodococcus sp., Rhodopseudomonas acidophila, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Sporothrix nivea, Stenotrophomonas maltophilia, Streptomyces hygroscopicus, Sulfolobus solfataricus, Thermoanaerobacter brockii, Thermoanaerobacter ethanolicus, Thermomicrobium roseum, Thermotoga lettingae, Torulopsis domercqii, Torulopsis enokii, Torulopsis glabrata, Torulopsis Ingeniosa, Torulopsis methanolovescens, Torulopsis methanophiles, Torulopsis methanosorbosa, Torulopsis methanothermo , Torulopsis sonorensis, Trichoderma lignorum, Wickerhamiella domercqiae and Xanthobacter autotrophicus.

17. Use according to one of the preceding claims, characterized in that the enzyme and / or the whole-cell catalyst are present in encapsulated and / or immobilized form.

18. Use according to claim 17, characterized in that the shell material and / or the carrier are selected from polysaccharides such as gum arabic, agar-agar, agarose, sucrose, maltodextrins, alginic acid and their salts, chitosan, starch, dextran or shellac, peptides , Protein hydrolysates or polypeptides such as collagen, albumin or gelatin, fats, fatty acids, cetyl alcohol, lecithins or waxes, chemically modified celluloses, in particular cellulose esters and ethers such as cellulose acetate, ethylcellulose, hydroxypropylcellulose, hydroxypropylmethylcellulose, carbylmethylcellulose or nitrocellulose derivatives, starch derivatives, polymers such as polyacrylates, Polyamides, polyvinyl alcohol, polyvinyl acetate or polyvinyl pyrrolidone, alginate polylysine alginate, nylon, silicone rubber, nylon polyethyleneimine, polylactic acid, polyglycolic acid, chitosan alginate, cellulose sulfate-poly (dimethyldiallyl) ammonium chloride, hydroxyethyl methacrylate-methyl methacrylate, chitosanecarbo xymethylcellulose, hydrogels, Sephadex, metals, ceramics or limestone.

19. Use according to claim 17, characterized in that the shell material and / or the carrier comprises a polyelectrolyte complex, wherein the polycation is selected from chitosan, polyethyleneimine, polydiethyldiallylammonium chloride, copolymers of diallylammonium salts and acrylamides, quaternized vinylpyrrolidine / vinylimidazole polymers, condensation products of polyglycols and amines, cationic silicone polymers, copolymers of adipic acid and

Dimethylaminohydroxypropyldiethylenetriamine, copolymers of acrylic acid and dimethyldiallylammonium chloride, polyaminopolyamides and their crosslinked water-soluble polymers, condensation products of dihaloalkylene such as bis-dimethylamino-1, 3-propane and quaternized ammonium salt polymers, and the polyanine is selected from water-soluble cellulose derivatives, pectins, alginates, carboxylated or succinylated Chitosan derivatives and synthetic anionic polymers such as polyacrylic and polymethacrylic acids.

20. Use according to claim 17, characterized in that the shell material and / or the carrier is a first component selected from inorganic substances, such as clays, silicates or sulfates, in particular talc, silicic acids, metal oxides, in particular aluminum oxides and / or titanium dioxide, silicates, in particular phyllosilicates, sodium aluminum silicates, bentonites and / or aluminosilicates (zeolites) and organic substances such as polyvinyl alcohol (PVA) or partially hydrolyzed PVA, and a second component selected from non-crosslinked, polymeric compounds selected from the group of polyacrylates, polymethacrylates, methacrylic acid-ethyl acrylate Copolymers, polyvinylpyrrolidones, polysaccharides or substituted polysaccharides, in particular cellulose ethers, and / or polyvinyl alcohols (PVA), preferably partially hydrolyzed polyvinyl alcohols and / or ethoxylated polyvinyl alcohols and their copolymers and mixtures contains.

21. A process for the removal of by-products from polymerizable preparations, which comprises contacting a crosslinkable preparation with an enzyme and / or whole-cell catalyst to remove the by-product.

22. The method according to claim 21, characterized in that the enzyme and / or the whole-cell catalyst is incorporated in the crosslinkable preparation.

23. The method according to claim 21, characterized in that the enzyme and / or the whole-cell catalyst before, during or after the application of the crosslinkable preparation is added thereto.

24. The method according to claim 23, characterized in that the enzyme and / or the whole-cell catalyst in the form of a surfactant-containing preparation is applied to the applied to the application site crosslinkable preparation.

25. The method according to any one of claims 21 to 24, characterized in that the enzyme and / or the whole-cell catalyst is used in encapsulated, immobilized and / or otherwise stabilized form.

26. The method according to any one of claims 21 to 25, characterized in that it is the undesirable by-product is an alcohol, in particular methanol, an organic acid, in particular acetic acid, an oxime, in particular a ketoxime, a benzamide or a Amin acts.

27. The method according to any one of claims 21 to 26, characterized in that the crosslinkable preparation contains acetate, alkoxy, oxime, benzamide and / or Aminsilikon- monomers.

28. The method according to any one of claims 21 to 27, characterized in that it is the crosslinkable preparation is a sealant.

29. Crosslinkable preparation, characterized in that it contains at least one enzyme and / or at least one whole cell catalyst.

30. A crosslinkable preparation according to claim 29, characterized in that the enzyme and / or the whole-cell catalyst is capable of reacting a by-product formed in the Vernetzugsreaktion.

31. Crosslinkable preparation according to claim 30, characterized in that the by-product is an alcohol, in particular methanol, an organic acid, in particular acetic acid, an oxime, in particular a ketoxime, a benzamide or an amine.

32. Crosslinkable preparation according to one of claims 29 to 31, characterized in that the polymerizable preparation contains acetate, alkoxy, oxime, benzamide and / or amine silicone monomers.

33. Crosslinkable preparation according to one of the preceding claims, characterized in that the enzyme and / or the whole-cell catalyst are present in encapsulated, immobilized and / or otherwise stabilized form.

34. A multi-component kit comprising a crosslinkable preparation and a preparation containing at least one enzyme and / or a whole-cell catalyst.

35. A multi-component kit according to claim 25, characterized in that the enzyme and / or the whole-cell catalyst is capable of reacting a by-product formed in the crosslinking reaction.

36. A method for determining the amount of volatile by-product released in cross-linking processes, comprising the steps of: a) placing a solvent-containing shell on a larger shell enclosing it; b) applying the polymerizable composition to the peripheral free surface of the larger shell the larger shell is then closed by applying an impermeable seal, c) the solvent is optionally mixed, after completion of the crosslinking reaction, the content of by-product contained in the solvent is determined analytically.