DE10203135A1 - New catalytic activities of oxidoreductases for oxidation and / or bleaching - Google Patents

Abstract

An oxidation and/or bleaching system is disclosed, comprising: a) oxidoreductases such as laccases and/or peroxidases applied individually or in combination, in the presence of the corresponding co-substrate 0<sb>2</sb>, H<sb>2</sb>0<sb>2</sb>, organic peroxides, per-acids etc., for the activation of compounds of the class of oxohydrocarbons, the class of urazoles and hydrazides, the class of hydantoins and the class of nitriles (cyano) compounds and b) additional carbonyl compounds (ketones, aldehydes) are applied which can form active oxygen species, such as dioxiranes, dioxetanes and peroxy compounds, amongst others, or other reactive compounds, or transition states such as radicals, cationic radicals, anionic radicals or reactive (redox-active) neutral compounds with the activated compounds.

Description

It is known that enzymes such as e.g. B. peroxidases, especially Horseradish Peroxidase (HRP) and the lignolytic enzymes belonging to lignin peroxidase and manganese peroxidase and certain oxidases such as (also counting to the lignolytic enzymes) laccase in the presence of H ₂ O ₂ , organic peroxides or peracids (Peroxidases) or atmospheric oxygen or O ₂ (oxidases / laccases) can oxidize corresponding substrates, the substrate spectrum for these enzymes being generally very large.

A number of applications of these enzymes have been published or published in recent years Patent pending such. B. as mild oxidants in chemical synthesis or in Food sector, as oxidants in the decolorization of dyes z. B. in waste water, as Labeling enzymes for special analysis methods and in biosensors etc.

Also in recent years, some processes have been published and / or patented, whereby these enzymes were used together with special mediator compounds (WO 96/18770 /, WO 94/29510, WO 94/12619, WO 94/12620 and WO 94/12621).

Laccases were and are preferably used as enzymes, with laccases today are commercially available.

On the one hand, these mediator compounds enable the oxidation of substrates with higher ones Oxidation potentials that normally could not be oxidized and secondly since they are low molecular weight and freely diffusible, they transfer the enzyme (laccase) / mediator System also capable of substrates in substances that are not freely accessible, e.g. B. Lignin in To break down pulp fibers. Free enzyme would have no significant breakdown here because of its cause too large molecular weight (in addition to the insufficient oxidation power).

In the case of lignin degradation in pulp, only the manganese peroxidase system (MnP system), which occurs in white rot fungi and works with the help of the "natural mediator" → chelated Mn ³⁺ , could be used "as an in vivo system". However, with regard to its performance, the strong H ₂ O ₂ dependency of the MnP and the very difficult production of the MnP, the system shows decisive disadvantages which have so far made it impossible to use it on an industrial scale.

The use of lignin peroxidase does not lead to delignification, since none has so far efficient mediators were found and fiber penetration because of the too large Molecular weight (see above) is not possible.

Despite the good performance of the Laccase mediator systems (LMS systems) and the good ones Pulp properties that are obtained hinder e.g. Currently the high price of the mediators who required relatively large amounts (the reactions are almost all stoichiometric and not catalytically) and the often ecological risks (substance toxicity) in addition to the increased Cost pressure on the pulp manufacturer side the wide application of these systems. Indeed is still z. B. in pulp bleaching for alternative bleaching systems more urgent Need, v. a. Because of the constraint, closed circuits close due to cost reasons must what with the ECF bleach (elemental chlorine free) with chlorine dioxide as Main bleaching agent (→ corrosion problem) is difficult.

It is therefore the object of the present invention to provide an oxidation bleaching system To make available, which does not have the disadvantages of the above systems.

• a) Oxidoreduktasen wie Laccasen und/oder Peroxidasen - einzeln oder in Kombination - in Gegenwart ihrer jeweiligen Co-Substrate O₂, H₂O₂, organische Peroxide, Persäuren u. a. eingesetzt werden zur Aktivierung von Verbindungen aus der Klasse der Oxokohlenstoffe, aus der Klasse der Urazole und Hydrazide, aus der Klasse der Hydantoine, und der Klasse der Nitril (Cyan)-Verbindungen und dass
• b) zusätzlich Carbonylverbindungen (Ketone, Aldehyde) eingesetzt werden, die mit den aktivierten Verbindungen aktive Sauerstoffspezies wie Dioxirane, Dioxetane, Peroxyverbindungen u. a. oder (entsprechend z. B. nach der Literatur: K. Deuchert et. al., Angewandte Chemie 90, S. 927-938, 1978) andere reaktive Verbindungen oder Übergangsstufen wie Radikale, Kationradikale, Anionradikale oder reaktive (redox-aktive) Neutralverbindungen bilden können
  Dabei werden als Oxokohlenstoffe solche Verbindungen eingesetzt entsprechend:
  Chemie in unserer Zeit, 16. Jahrgang 1982, Nr. 2, S. 57-67 inklusive der dort angeführten Literatur, insbesondere R. West et al., Oxocarbons and their Reactions, in J. Zabicky ed., "The chemistry of the Carbonyl Group", Wyley (Interscience), 1970; R. West, Oxocarbons, Academic Press, 1980 und Römpp Chemie Lexikon, Thieme Verlag, 1995, S. 3175-3177.
  Insbesondere werden eingesetzt:
  Verbindungen der allgemeinen Formel I, wie α-Hydroxycarbonylverbindungen
  der allg. Formel Ia, α-Dicarbonylverbindungen
  der allgemeinen Formel Ib, β-Hydroxy-carbonyl-verbindungen der allgemeinen Formel Ic, sowie β-Dicarbonylverbindungen der allgemeinen Formel Id,
  
  
  wobei die Reste R¹ bis R⁸ unabhängig voneinander jeweils eine der folgenden Atome der Atomgruppen darstellen können: Wasserstoff, Halogen, Alkyl, Alkyloxy, Aryl, Aryloxy, Hydroxy, Oxo, Formyl, Thioxo, Mercapto, Alkylthio, Sulfeno, Sulfino, Sulfo, Sulfamoyl, Amino, Imino, Amido, Amidino, Hydroxycarbamoyl, Hydroximino, Nitroso, Nitro, Hydrazono und wobei die Reste R¹ und R²; R³ und R⁴; R⁵ und R⁶; R⁷ und R⁸ eine gemeinsame Gruppe bilden können und wobei n ≥ 1 ist.

This is achieved in that a method for oxidation and / or bleaching is provided, which is characterized in that

• a) Oxidoreductases such as laccases and / or peroxidases - individually or in combination - in the presence of their respective co-substrates O ₂ , H ₂ O ₂ , organic peroxides, peracids etc. are used to activate compounds from the class of oxocarbons, from the class the urazoles and hydrazides, from the class of hydantoins, and the class of nitrile (cyan) compounds and that
• b) in addition carbonyl compounds (ketones, aldehydes) are used which, with the activated compounds, active oxygen species such as dioxiranes, dioxetanes, peroxy compounds, etc. or (corresponding, for example, according to the literature: K. Deuchert et. al., Angewandte Chemie 90, p 927-938, 1978) can form other reactive compounds or transition stages such as radicals, cation radicals, anion radicals or reactive (redox-active) neutral compounds
  Such compounds are used as oxocarbons accordingly:
  Chemistry in our time, 16th year 1982, No. 2, pp. 57-67 including the literature cited there, in particular R. West et al., Oxocarbons and their Reactions, in J. Zabicky ed., "The chemistry of the Carbonyl Group ", Wyley (Interscience), 1970; R. West, Oxocarbons, Academic Press, 1980 and Römpp Chemie Lexikon, Thieme Verlag, 1995, pp. 3175-3177.
  In particular, the following are used:
  Compounds of general formula I, such as α-hydroxycarbonyl compounds
  of the general formula Ia, α-dicarbonyl compounds
  of the general formula Ib, β-hydroxycarbonyl compounds of the general formula Ic, and also β-dicarbonyl compounds of the general formula Id,
  
  
  where the radicals R ¹ to R ⁸ can each independently represent one of the following atoms of the atomic groups: hydrogen, halogen, alkyl, alkyloxy, aryl, aryloxy, hydroxy, oxo, formyl, thioxo, mercapto, alkylthio, sulfeno, sulfino, sulfo, Sulfamoyl, amino, imino, amido, amidino, hydroxycarbamoyl, hydroximino, nitroso, nitro, hydrazono and where the radicals R ¹ and R ² ; R ³ and R ⁴ ; R ⁵ and R ⁶ ; R ⁷ and R ⁸ can form a common group and where n ≥ 1.

Compounds of the general formula II are particularly preferred, open-chain compounds having a double bond (enols),


where the radicals R ⁹ to R ¹⁰ can each independently represent one of the following atoms or atom groups: hydrogen, halogen, alkyl, alkyloxy, aryl, aryloxy, hydroxy, oxo, formyl, thioxo, mercapto, alkylthio, sulfeno, sulfino, sulfo, Sulfamoyl, amino, imino, amido, amidino, hydroxycarbamoyl, hydroximino, nitroso, nitro, hydrazono and where the radicals R ⁹ and R ¹⁰ can form a common group.

Likewise particularly preferred are compounds of general structure III, cyclic compounds, residues not OH, derivatives of squaric acid, OH group derivatized,


where the radicals R ¹¹ to R ¹² can each independently represent one of the following atoms or atom groups: hydrogen, halogen, alkyl, alkyloxy, aryl, aryloxy, hydroxy, oxo, formyl, thioxo, mercapto, alkylthio, sulfeno, sulfino, sulfo, Sulfamoyl, amino, imino, amido, amidino, hydroxycarbamoyl, hydroximino, nitroso, nitro, hydrazono and m ≥ 0.

Cyclic oxocarbons of the general formula IV (general empirical formula: H ₂ C _x O _x , and also their dianions of the general formula C _x O _x ^2- where x 3 3) are particularly preferred. structural element

The following are particularly preferred: triangular acid

square acid

crocodile acid

rhodizonic

Also particularly preferred is tetrahydroxy-p-benzoquinone, its salts and Derivatives and the corresponding salts and derivatives of triangular acid, square acid, Croconic acid and rhodizonic acid. In particular, are derivatives of squaric acid preferred, which in the literature: K. Deuchert et. al., Angewandte Chemie, 90, 1978, p. 927-938 are listed.

From the group of amides such. B. the hydrazides or urazoles, compounds of the general formulas V (amides) and VI (hydrazides) are preferably used:


where X stands for C = O or O = S = O. (Carboxylic acid or sulfonic acid amides). The radicals R can be the same or different and independently represent hydrogen, alkyl, aryl or acyl groups (carboxylic acid or sulfonic acid residues).

Cyclic hydrazides of the general formula VII are particularly preferred

Where X stands for C = O or O = S = O (cyclic hydrazides of dicarboxylic acids or disulfonic acids).

The radicals R can be the same or different and independent of one another Represent hydrogen, alkyl, aryl or acyl groups.

G stands for the following atoms or groups of atoms: CH ₂ , CH ₂ -CH ₂ , CHR ¹ -CHR ¹ , CH = CH, CR ² = CR ² , NH, NR ³ , C = O, ortho-C ₆ H ₄ (ortho substituted phenyl radical), ortho C ₁₀ H ₆ (ortho substituted naphthyl radical), where the radicals R ¹ to R ^{3 can be} identical or different and can independently represent hydrogen, alkyl, aryl or acyl radicals.

Also preferred are urazoles (formula VIII) and phthalhydrazides (formula IX)

Where R ⁴ can be hydrogen, alkyl, alkoxy, carboxy, nitro or amino. The radicals R can be the same or different and independently of one another are hydrogen, alkyl, aryl or.

The following compounds are particularly preferred:
Maleic hydrazide, 2-nitrobenzhydrazide, p-toluenesulphonylhydrazide, Nicotinic hydrazide, Isonicotinic acid hydrazide, 4,4'-oxydibenzenesulfonylhydrazide, Bencoic hydrazide, Phthalhydrazide, 3-aminophthal hydrazide, 1-Naphthoic hydrazide-3-hydrazide , Oxamic hydrazide, Oxalyl dihydrazide, Terephthalic dihydrazide, Isophthalic-dihydrazide, L-Tyrosine hydrazide, Oxalic-bis- (benzylidenehydrazide), Salicyliden salicylhydrazide, Thiophene-2-carbonic acid hydrazide, Furan-2-carbonic acid hydrazide.

5-Amino-5-hydroxypyrazoles, 2,3-dihydro-1,4- phthalazinedione, phthalhydrazides, 7-nitroindazoles and 1,2-dihydropyrazine-3,6- dion.

The following compounds are also particularly preferred:
4-phenylurazole, 1-phenylurazole, 4-methylurazole, 4-tert-butylurazole and urazole, in particular:
4-tert-butylurazole and urazole.

From the group of imides such. B. the hydantoins, compounds of the general formula X (imides) are preferred:

The radicals R can be the same or different and independent of one another Represent hydrogen, alkyl, aryl, acyl or amino groups.

Imides of the general formula XI are particularly preferred:

The radicals R can be the same or different and independent of one another Represent hydrogen, alkyl, aryl, acyl or amino groups.

Cyclic imides of the general formula XII are also particularly preferred:

The radicals R can be identical or different and independently represent hydrogen, alkyl, aryl, acyl or amino groups, and where the group G represents one of the following atoms or atom groups: CH ₂ , CHR ¹ , CR ¹ R ² , CH = CH, CR ³ = CR ⁴ , NH, NR ⁵ , C = O, O, and where R ¹ to R ^{5 can be the} same or different and can independently represent one of the following groups: hydrogen, alkyl, aryl, alkoxy, carboxy.

The derivatives of hydantoin XIII are also particularly preferred:

The following compounds are particularly preferred:
Diethyl 5-hydantoyl phosphonate, 5-methyl-5-phenyl-hydantoin, hydantoyl-5-acetic acid, 1,3-dibromo-5,5-dimethylhydantoin.

Compounds according to Römpp Chemie Lexikon, Thieme Verlag, 1995, pp. 3012-3013 with the corresponding quotes from a .: Chem. Our Time, 18, 1984, pp. 1-16.

Cyanamide and dicyandiamide are particularly preferred.

enzymes

Oxidoreductases are preferably used as enzymes. In the sense of the Invention, the term enzyme also encompasses enzymatically active proteins or peptides or prosthetic groups of enzymes. The enzymes of Wild type strains or from genetically modified host strains. The particularly preferred enzymes include laccases and Peroxidases, the peroxidases because of their z. T. much further into that alkaline milieu reaching pH-Optimums considerable advantages in the Can have application for the bleaching of pulp.

Enzymes in the oxidation bleaching system according to the invention Class 1.1.1 oxidoreductases. to 1.97 according to the International Enzyme Nomenclature: Committee of the International Union of Biochemistry and Molecular Biology (Enzyme Nomenclature, Academic Press, Inc., 1992, p. 24-154) can be used.

The following enzymes are preferably used:
Class 1.1 enzymes, particularly preferably the class 1.1.5 enzymes with quinones as acceptors and the class 1.1.3 enzymes. with oxygen as acceptor, cellobiose: quinone-1-oxidoreductase (1.1.5.1) is particularly preferred in this class.

Enzymes of class 1.2 can also be used. Are particularly preferred here the enzymes of group (1.2.3) with oxygen as the acceptor.

Enzymes of class 1.3 can also be used. Here are the enzymes too the class (1.3.3) with oxygen as acceptor and (1.3.5) with quinones etc. as Particularly preferred acceptor.

Bilirubin oxidase (1.3.3.5) is particularly preferred.

Class 1.4 enzymes can also be used. Are also particularly preferred here class 1.4.3 enzymes with oxygen as acceptor.

Enzymes of class 1.5 can also be used. Here too are special prefers enzymes with oxygen (1.5.3) and with quinones (1.5.5) as Acceptors.

Enzymes of class 1.6 can also be used. Particularly preferred here are class 1.6.5 enzymes with quinones as acceptors.

Enzymes of class 1.7 can also be used. Here are special prefers class 1.7.3 with oxygen as acceptor.

Enzymes of class 1.8 can also be used. Particularly preferred is class 1.8.3 with oxygen and (1.8.5) with quinones as acceptors. Enzymes of class 1.9 can also be used. The is particularly preferred here Group 1.9.3 with oxygen as acceptor (cytochrome oxidases).

There are also class 1.12 enzymes and class 1.13 and 1.14 enzymes (Oxigenases / Lipoxigenases) into consideration.

Enzymes of class 1.15 which are based on superoxide radicals can also be used Acceptors work. Superoxide dismutase is particularly preferred here (15/1/11).

Enzymes of class 1.16 can also be used. Particularly preferred here are class 1.16.3.1 enzymes (ferroxidase, e.g. ceruloplasmin). Enzymes belonging to groups 1.17 and 1.18 should also be mentioned (Effect on reduced ferredoxin as donor) and 1.19 (Effect on reduced Flavodoxin as donor) and 1.97 (other oxidoreductases).

The very particularly preferred enzymes include those of class 1.10. Of the enzymes in this class, the enzymes are in particular catechol oxidase (Tyrosinase) (1.10.3.1), L-ascorbate oxidase (1.10.3.3), O-aminophenol Oxidase (1.10.3.4) and laccase (benzene diol: oxigen oxidoreductase) (1.10.3.2) is preferred, the laccases being particularly preferred. The enzymes of group 1.11 are also particularly preferred.

The cytochrome-C peroxidases (1.11.1.5) are very particularly preferred here, Catalase (1.11.1.6), the peroxidase (1.11.1.6) the iodide peroxidase (1.11.1.8), the glutathione peroxidase (1.11.1.9), the chloride peroxidase (1.11.1.10), the L-ascorbate peroxidase (1.11.1.11), the Phospholipid hydroperoxide glutathione peroxidase (1.11.1.12), the manganese peroxidase (1.12.1.13), the Diarylpropane peroxidase (ligninase, lignin peroxidase (1.12.1.14).

The enzymes mentioned are commercially available or can be copied Win standard procedures. As organisms for the production of the enzymes For example, plants, bacteria and fungi come into consideration. in principle can be both naturally occurring and genetically modified Organisms are enzyme producers. Parts of unicellular or multicellular organisms conceivable as enzyme producers, especially cell cultures. In particular for the production of the preferred enzymes of group 1.11.1, and Enzymes of group 1.10.3, especially for the production of laccases and other ligninolytic enzymes (lignin peroxidases, manganese peroxidases), white rot fungi etc. such as Pleurotus, Phlebia and Trametes, Agaricus, Lentinus, Botrytis, Cryphonectria, Hypholoma, Heterobasidion, Phanerochaete u. a. used.

For example, air, oxygen, peroxides such as H ₂ O ₂ , organic peroxides, peracids such as peracetic acid, performic acid, persulfuric acid, persitric acid, metachloroperoxibenzoic acid, per compounds such as perborates, percarbonates, persulfates or oxygen species such as OH radicals, OOH radicals can be used as co-substrates , OH ⁺ radicals, superoxide (O ^- ₂ ) and singlet oxygen can be used.

With the exception of benzophenones, benzilene and aromatic ketones, compounds of the general formula XIV are used as carbonyl compounds (ketones, aldehydes).

The radicals R ¹ and R ² can be the same or different and represent aliphatic or aromatic groups. Furthermore, the radicals R ¹ and R ^{2 can form} a ring which, in addition to carbon, can also contain heteroatoms such as nitrogen, oxygen and sulfur.

1,2-Diketones (formula XV) and 1,3-diketones (formula XVI) or polyketones (polyketides) and the tautomeric enols (formula XVII) are particularly preferred,


where the radicals R ³ to R ^{6 can} each be the same or different and can represent aliphatic or aromatic groups. Furthermore, the radicals R ³ and R ⁴ and the radicals R ⁵ and R ^{6 can form} a common ring which, in addition to carbon, can also contain heteroatoms such as nitrogen, oxygen or sulfur.

Here is the possibility of tautomerization or the formation of a resonance hybrid really important.

Particularly preferred ketones are generally hydroxy ketones, α, β-unsaturated ketones and Oxicarbonsäuren.

Carbonyl compounds such as:
Acetone, methyl ethyl ketone, diethyl ketone, methyl n-butyl ketone, methyl isobutyl ketone, cyclohexanone, cyclopentanone, 2-methylcyclohexanone, 3-methylcyclohexanone, 4-methylcyclohexanone, dihydroxyacetone, diacetyl (monohydrazone), diacetyl (dihydrazone), hydroxophenophenophenophenone 1-phenylbutan-3-one, pentan-3-one, heptan-4-one, nonan-2-one, cycloheptanone, cyclooctanone, cyclodecanone, cyclododecanone, cyclohexanone, 2-methylcyclohexanone, 3-methylcyclohexanone, 4-methylcyclohexanone, cyclopentanone, 2- methylcyclopentanone, 3-methylcyclopentanone, dimethyl ketone, ethyl propyl ketone, methyl amyl ketone, acetyl acetone, pinacoline, methyl isopropyl ketone, methyl isoamyl ketone, ethyl amyl ketone, diisopropyl ketone, diisobutyl ketone, methyl vinyl ketone, methylisopropl oxyacetone, meso-methoxy-oxy-acetone, meso-oxy-oxy-acetone, meso-phenoxy-oxy-acetone, meso-methoxy-oxy-acetone, meso-methoxy-oxy-acetone, meso-methoxy-oxy-acetone, meso-methoxy-oxy-acetone, meso-methoxy-pentone-2 2,3-hexanedione, phenylacetone, propiophenone, benzophenone, benzoin, benzil, 4,4'-dimethoxybenzil, 4'-methoxyacetophenone, 3'-methoxyacetophenone, O-ethylbenzoin, (2-methoxyphenyl) ace clay, (4-methoxyphenyl) acetone, methoxy-2-propanone, glyoxylic acid, benzylglyoxylate, benzylacetone, benzylmethyl ketone, cyclohexylmethyl ketone, 2-decanone, dicyclohexyl ketone, diethyl ketone, diisopropyl ketone, 3,3-dimethyl-2-butanone, isobutylmethyl ketone
2-methyl-3-heptanone, 5-methyl-3-heptanone, 6-methyl-5-hepten-2-one, 5-methyl-2-hexanone, 2-nonaon, 3-nonaon, 5-nonaon, 2- Octanone, 3-octanone, 2-undecanone, 1,3-dichloroacetone, 1-hydroxy-2-butanone, 3-hydroxy-2-butanone, 4-hydroxy-4-methyl-2-pentanone, 2-adamantanone, anthrone, Bicyclo (3.2.0) hept-2-en-6-one, cis-bicyclo (3.3.0) octan-3,7-dione, (1S) - (-) - camphor, p-chloroanil, cyclobutanone, cyclododecanone, 1,3-cyclohexanedione, 1,4-cyclohexanedione monoethylene ketal, dibenzosuberone, ethyl 4-oxocyclohexane carboxylate, fluoren-9-one, 1,3-indanedione, methylcyclohexanone, phenylcyclohexanone, 4-propylcyclohexanone, 1,2,3,4-tetrahydro- 1-naphthalinone, 1,2,3,4-tetrahydro-2-naphthalinone, 3,3,5-trimethylcyclohexanone, 3-acetoxy-2-cyclohexen-1-one,
Benzylidene acetone, (R) - (-) - carvone, (S) - (-) - carvone, curcumin, 2-cyclohexen-1-one, 2,3-diphenyl-2-cyclopropen-1-one, 2-hydroxy- 3-methyl-2-cyclopenten-1-one, isophorone, α-Jonon, β-Jonon, 3-methoxy-2-cyclohexen-1-one, 3-methyl-2-cyclopenten-1-one, 3-methyl- 3-penten-2-one, methyl vinyl ketone, (R) - (+) - pulegon, tetraphenyl-2,4-cyclopentadien-I-one, 2,6,6-trimethyl-2-cyclohexen-1,4-dione, 2-acetylbenzoic acid, 1-acetylnaphthalene, 2-acetylnaphthalene, 3'-aminoacetophenone, 4'-aminoacetophenone, 4'-cyclohexylacetophenone, 3 ', 4'-diacetoxyacetophenone, diacetylbenzene, 2', 4'-5'-dihydroxy - dihydroxyacetophenone, 2 ', 6'-dihydroxyacetophenone, 3,4-dimethoxyacetophenone, 2'-hydroxyacetophenone, 4'-hydroxyacetophenone, 3'-methoxyacetophenone, 4'-methoxyacetophenone, 2'-methylacetophenone, 4'-methylac Nitroacetophenone, 3'-nitroacetophenone, 4'-nitroacetophenone, 4'-phenylacetophenone, 3 ', 4', 5'-trimethoxyacetophenone, 4'-aminopropiophenone, benzoylacetone, benzoylpropionic acid, benzylidene acetophenone, C yclohexylphenyl ketone, deoxybenzoin, 4 ', 4'-dimethoxybenzil, 1,3-diphenyl-1,3-propanedione, ethyl benzoyl acetate, ethyl (phenylglyoylate), 4'-hydroxypropiophenone, 1,3-indanedione, 1-indanone, isopropylphenyl ketone , 6-methoxy-1,2,3,4-tetrahydro-naphthalin-1-one, methylphenylglyoxylate, phenylglyoxylonitrile, propiophenone, valerophenone, 2-acetyl-butyrolactone, 2-acetylpyrrole, 1-benzylpiperidin-4-one, dehydroacetic acid , 3,4-dihydro-4,4-dimethyl-2H-pyran-2-one, 1,4-dihydro-4-pyridinone, N-ethoxycarbonyl-4-piperidinone, 2-furylmethyl ketone, 5-hydroxy-2-hydroxymethyl -4H-pyran-4-one, 3-hydroxy-2-methyl-4-pyranone, 3-indolyl methyl ketone, isatin, 1-methyl-4-piperidinone, methyl 2-pyridyl ketone, methyl 3-pyridyl ketone, methyl 4 -pyridyl ketone, methyl 2-thienyl ketone, phenyl 2-pyridyl ketone, phenyl 4-pyridyl ketone, tetrahydrofuran-2,4-dione, tetrahydro-4H-pyran-4-one, 2,2,6,6-tetramethyl-4 -piperidone, xanthone, acenaphthenequinone,
Pyruvic acid, (1R) - (-) - camphorquinone, (1S) - (+) - camphorquinone, 3,5-di-tert-butyl-top-quinone, 1,2-dihydroxycyclobutene-3,4-dione, ethyl- (2nd -amino-4-thiazolyl) glyoxylate, ethyl (phenylglyoxylate), ethyl pyruvate, 2,3-hexanedione, 3,4-hexanedione, 3-methyl-2-oxo-butyric acid, 3-methyl-2-oxo-valeric acid, 4-methyl-2-oxo-valeric acid, methyl phenylglyoxylate, 2-oxobutyric acid, 2,3-pentanedione, 9,10-phenanthrenequinone, acetoacetanilide, 2-acetyl-γ-butyric acid lactone, 2-acetylcyclopentanone, allyl-acetoacetate, benzoylacetone, ter-butylacetoacetate, 1,3-cyclopentanedione, diethyl-3-oxoglutarate, dimethyl-acetylsuccinate, dimethyl-3-oxoglutarate, 1,3-diphenyl-1,3-propanedione, ethyl acetoacetate, ethyl-benzoylacetate, ethyl-butyl-acrylate, ethyl- 2-oxocyclohexane carboxylate, ethyl 2-phenylacetoacetate, methyl acetoacetate, 2-methyl-1,3-cyclohexanedione, 2-methyl-1,3-cyclopentanedione, methyl isobutyryl acetate, methyl 3-oxopentanoate, methyl pivaloyl acetate, 3-oxoglutaric acid, tetrahydrofuran-2, 4-dione, 2,2,6,6-tetrameth yl-3,5-heptanedione, 3-benzoylpropionic acid, 1,4-cyclohexanedione, dimethyl-acetylsuccinate, ethyl levulinate, 2-aminoanthraquinone, anthraquinone, p-benzoquinone, 1,4-dihydroxyanthraquinone, 1,8-dihydroxyanthraquinone, 2-ethylanthraquinone Methyl-p-benzoquinone, 1,4-naphthoquinone, tetramethyl-p-benzoquinone, 2,2-dimethyl-1,3-dioxane-4,6-dione, 2-benzoylbenzoic acid, 3-benzoylpropionic acid, 5,6-dimethoxyphthalaldehyde acid, Glyoxylic acid, levolinic acid, methyl (trans-4-oxo-2-pentenoate), phthalaldehyde acid, terephthalaldehyde acid, dibutyl maleate, dibuthyl succinate, dibutyl phthalate, dicyclohexyl phthalate, diethyl acetamidomalonate, diethyl adipate, diethyl benzyl ethylene malonate ethyl malylate malate, ethyl malylate malate, ethoxylate Diethyl ethyl malonate, diethyl fumarate, diethyl glutarate,
Diethyl isopropylidene malonate, diethyl maleinate, diethyl malonate, diethyl methyl malonate, diethyl oxalate, diethyl 3-oxoglutarate, diethyl phenyl malonate, diethyl phthalate, diethyl pimelate, diethyl sebacate, diethyl suberate, diethyl succinate, dimethyl boryl acetate, diisobutyl acetate acetyl succinate, dimethyl adipate, dimethyl 2-minoterephthalate, dimethyl fumarate, dimethyl glutaconate, dimethyl glutarate,
Dimethyl isophthalate, dimethyl malonate, dimethyl methoxymalonate, dimethyl (methylene succinate), dimethyl oxalate, dimethyl 3-oxoglutarate, dimethyl phthalate, dimethyl succinate, dimethyl terephthalate, ethylene glycol diacetate, ethylene glycol dimethacrylate, monoethylomomethyl pate, monoethyl methyl malateate Triethyl methane tricarboxylate, trimethyl 1,2,3-propane tricarboxylate, 3-acetoxy-2-cyclohexen-1-one, allyl acetoacetate, allyl (cyanoacetate), benzylacetoacetate, tert-butylacetoacetate, butylcyanoacetate, chlorogenic acid hemihydrate, cumene 3-carboxylic acid, diethylethoxycarbonylmethanephosphonate, dodecyl gallate, dodecyl 3,4,5-trihydroxybenzoate, (2,3-epoxypropyl) methacrylate, (2-ethoxyethyl) acetate, ethyl (acetamidocyanate acetate), ethyl acetoacetate, ethyl 2-aminobenzoate, ethyl - (3-aminopyrazole-4-carboxylate), ethyl benzoxy acetate, ethyl butyrylacetate, ethyl cyanoacetate, ethyl (2-cyano-3-ethoxyacrylate), ethyl cyano formate, ethyl 2 cyanopropionate, ethyl (3,3-diethoxypropionate),
Ethyl 1,3-dithiane-2-carboxylate, ethyl (2-ethoxyacetate), ethyl 2-furan carboxylate, ethyl gallate, ethyl levulinate, ethyl mandelate, ethyl 2-methyl lactate, ethyl 4-nitrocinnamate, ethyl oxamate, ethyl 2- oxocyclohexane carboxylate, ethyl 4-oxocyclohexane carboxylate, ethyl 5-oxohexanoate, ethyl 2-phenylacetoacetate, ethyl 2-phenylacetoacetate, ethyl (phenylglyoxylate), ethyl 4-piperidinecarboxylate, ethyl 2-pyridinecarboxylate, ethylcarboxylate, ethyl Ethyl 4-pyridinecarboxylate, ethyl pyruvate, ethyl thioglycolate, ethyl 3,4,5-trihydroxybenzoate, (2-hydroxyethyl) methacrylate, (2-hydroxypropyl) methacrylate, 3-indole acetate, (2-methoxyethyl) acetate, (1 Methoxy-2-propyl) acetate, methyl acetoacetate, methyl 2-aminoabenzoate, methyl 3-aminocroconate, methyl cyanoacetate, methyl (4-cyanobenzoate), methyl (4-formylbenzoate), methyl 2-furan carboxylate, Methyl isobutyrylacetate, methyl methoxy acetate, methyl 2-methoxybenzoate, methyl 3-oxopentanoate, methyl phenylglyoxylate, methyl phenylsulfinyl acetate, methyl pivaloylacetate, methyl 3 -pyridinecarboxylate, 5-nitrofurfurylidene diacetate, propyl gallate, propyl 3,4,5-trihydroxybenzoate, methyl (3-methylthiopropionate), acetamide, acetanilide, benzamide, benzanilide, N, N-diethylacetamide, N, N-dimethylformamide, N, N -Diethyl-3-methylbenzamide, diethyltoluamide, N, N-dimethylacetamide, N, N-dimethylformamide, N, N-diphenylacetamide, N-methylformamide, N-methylformanilide, N-acetylthiourea, adipic acid diamide, 2-aminobenzamide, 4-aminobenzamide, berneamidamide , Malonic acid diamide, N, N'-methylenediacrylamide, oxalic acid diamide, pyrazine-2-carboxylic acid amide, pyridine-4-carboxylic acid amide, N, N, N ', N'-tetramethylsuccinic acid diamide, N, N, N', N ', - tetramethylglutaric acid diamide, acetoacetamide , Benzohydroxamic acid, cyanoacetamide, 2-ethoxybenzamide, diethyl acetamidomalonate, ethyl (acetamidocyanacetate), ethyl oxamate, hippuric acid Na salt, N- (hydroxymethyl) acrylamide, L - (-) michic acid amide, 2'-nitroacetanilide, 3'- Nitroacetanilide, 4'-nitroacetanilide, paracetamol, piperine, salicylanilide, 2-acetyl-γ-butyr olactone, γ-butyrolactone, E-caprolactone, dihydrocumann, 4-hydroxycumann, 2 (5H) - furanone, 2,5-dihydro-5-methoxy-2-furanone, phthalide, tetrahydrofuran-2,4-dione, 2.2 , 6-trimethyl-1,3-dioxin-4-one, γ-valerolactone, 4-amino-1,3-dimethyluracil, barbituric acid, O-benzylooxycarbonyl-N-hydroxy-succinimide, succinimide, 3,6-dimethylpiperazin-2 , 5-dione, 5,5-diphenylhydantoin, ethyl 1,3-dioxoisoindoline-2-carboxylate, 9-fluorenylmethylsuccinimidyl carbonate, hydantoin, maleimide, 3-methyl-1-phenyl-2-pyrazolin-5-one, 1 -Methyl- 2-pyrrolidone, methyluracil, 6-methyluracil, oxindole, phenytoin, 1 (2H) -phthalazinone, phthalimide, 2, 5-piperazinedione, 2-piperidinone, 2-pyrrolidone, rhodanine, saccharin, 1,2,3, 6- tetrahydrophthalimide, 1,2,3,4-tetrahydro-6,7-dimethoxy-quinazoline-2,4-dione, 1,5,5-trimethylhydantoin, 1-vinyl-2-pyrrolidone, di-tert-butyl dicarbonate, Diethyl carbonate, dimethyl carbonate, dimethyl dicarbonate, diphenyl carbonate, 4,5-diphenyl-1,3-dioxol-2-one, 4,6-diphenylthieno (3,4-d) -1,3-dioxol-2-one-5.5 -d ioxide, ethylene carbonate, magnesium methoxide methyl carbonate, monomethyl carbonate sodium salt, propylene carbonate, N-allyl urea, azodicarboxylic acid diamide, N-benzyl urea, biuret, 1,1'-carbonyl dimidazole, N, N-dimethyl urea, N-ethyl urea, N-formyl urea , Urea, n-methylurea, N-phenylurea 4-phenylsemicarbazide, tetramethylurea, semicarbazide hydrochloride, diethyl azodicarboxylate, methyl carbamate, 1- (4-methoxyphenyl) -2- (2-methoxy-phenoxy) ethanone, 1- (4-methoxyphenyl ) -2- (2-methoxy-phenoxy) -ethanol.

Anhydrides such as:
Benzoic anhydride, benzene-1,2,4,5-tetracarboxylic acid-1,2,4,5-dianhydride, 3,3 ', 4,4'-benzophenonetetracarboxylic acid anhydride, succinic acid anhydride, butyric acid anhydride, crotonic acid anhydride, cis-1,2-cyclohexanedicarboxylic acid anhydride, Di-tert-butyl dicarbonate, dimethyl dicarbonate, dodecenylsuccinic anhydride, Epicon B4400, acetic anhydride, glutaric anhydride, hexanoic anhydride, isatoic anhydride, isobutyric anhydride, isovaleric anhydride, maleic anhydride, naphthalic anhydride 5-naphthalenic anhydride , 2nd phenylbutyric anhydride, pivalic anhydride, propionic anhydride, cis-1,2,3,6-tetrahydrophthalic anhydride and valeric anhydride.

Areas of application of the oxidation or bleaching system according to the invention is v. a. the Use in pulp bleach or pulp bleach, use in oxidative Treatment of all types of waste water, use in the manufacture of Wood composites, the use as an enzymatic deinking system, the use as an oxidative Agent in organic synthesis, use as a bleaching system in detergents Use as a bleaching agent or oxidizing agent in the textile industry (e.g. stone washing and bleaching of fabrics) and the use in coal liquefaction of brown or Hard coal, because the new inventive system has many of the disadvantages of purely chemical Systems (e.g. significant environmental problems) or other enzymatic systems (often too low performance and high costs). The application of the Systems are not limited to these applications.

• a) Oxidoreduktasen wie Laccasen und/oder Peroxidasen - einzeln oder in Kombination - in Gegenwart ihrer jeweiligen Co-Substrate O₂, H₂O₂, organische Peroxide, Persäuren u. a. eingesetzt werden zur Aktivierung von Verbindungen aus der Klasse der Oxokohlenstoffe, aus der Klasse der Urazole und Hydrazide, aus der Klasse der Hydantoine, und der Klasse der Nitril (Cyan)- Verbindungen und dass
• b) zusätzlich Carbonylverbindungen (Ketone, Aldehyde) eingesetzt werden, die mit den aktivierten Verbindungen aktive Sauerstoffspezies wie Dioxirane, Dioxetane, Peroxyverbindungen u. a. oder (entsprechend z. B. nach der Literatur: K. Deuchert et. al., Angewandte Chemie 90, S. 927-938, 1978) andere reaktive Verbindungen oder Übergangsstufen wie Radikale, Kationradikale, Anionradikale oder reaktive (redoxaktive) Neutralverbindungen bilden können,
  eine Delignifizierung von Zellstoff (erhebliche Reduktion der Kappazahl) erzielt wurde.

It has now been found, completely surprisingly, that when using the oxidation and / or bleaching system according to the invention, which is characterized in that

• a) Oxidoreductases such as laccases and / or peroxidases - individually or in combination - in the presence of their respective co-substrates O ₂ , H ₂ O ₂ , organic peroxides, peracids etc. are used to activate compounds from the class of oxocarbons, from the class of urazoles and hydrazides, from the class of hydantoins, and the class of nitrile (cyan) compounds and that
• b) in addition carbonyl compounds (ketones, aldehydes) are used which, with the activated compounds, active oxygen species such as dioxiranes, dioxetanes, peroxy compounds, etc. or (corresponding, for example, according to the literature: K. Deuchert et. al., Angewandte Chemie 90, p 927-938, 1978) can form other reactive compounds or transition stages such as radicals, cation radicals, anion radicals or reactive (redox-active) neutral compounds,
  cellulose delignification (significant reduction in kappa number) was achieved.

Furthermore, surprisingly, a considerable bleaching effect was possible in the Bleaching of wood pulps and bleaching of fabrics after deinking processes being found.

In the oxidative treatment of waste water, such as waste water from the Manufacture of wood pulp (wood pulp, refiner), from the pulp industry and contaminated with dye Sewage, e.g. B. the textile industry, could also surprisingly one oxidative polymerization of lignin and / or lignin-like substances and / or Discoloration can be demonstrated.

This oxidative polymerization of lignin and / or lignin-like was also able Surprisingly, substances used in the manufacture of Wood composites (binder and / or adhesive production by oxidative polymerization of the existing polyphenylpropane body) can be confirmed.

In addition, surprisingly, an ink detachment at Deink process (probably by swelling of the lignin-containing waste paper fibers caused) can be demonstrated.

Surprisingly, coal liquefaction properties were also used in the Treatment of brown or hard coal found.

In addition, surprisingly, there was also a high and selective oxidizing power when used as an "oxidizing agent" in organic synthesis, a strong bleaching power when using bleach in detergents and when general bleaching of textile fabrics or special bleaching for Use in stone wash processes, namely as a replacement for the mechanical Color removal and / or post-bleaching demonstrated in these processes.

The system described in German application: DE 198 20 947.9-45 differs from the present invention primarily in the addition of suitable ketone compounds. which should usually be aliphatic. No benzophenones, benziles and organic carbonyl compounds listed there are used because they have been proven to be ineffective. Another great advantage is that no pressurization with O _{2 is} necessary. Furthermore, it could be demonstrated that the system according to the invention with the addition of suitable ketones and z. B. oxocarbons for the first time a catalytic oxidation with very high performance (z. B. 30% delignification of pulp with the addition of only 200 g oxocarbon per ton of pulp) is possible with the corresponding commercial advantages.

It may also be advantageous to add primary, secondary or tertiary amines (see accordingly, the z. B. according to the literature: K. Deuchert et. al .. Angewandte Chemie 90th S. 927-938, 1978) in order to obtain certain types of radicals (e.g. similar types of sausage Etc.)

As additional systems for the oxidation and / or bleaching system according to the invention, in simultaneous combination or in any chronological order that in WO 98/59108 and DE 101 26 988.9 described HOS system (hydrolase mediated oxidation system), consisting of lipases (or similar hydrolases), peroxide, ketones and fatty acids / fats as well as the oxidation systems described in DE 101 26 988.9 with the active oxidants 1) peroxynitrite, 2) ferrocene / peroxide, 3) activated sulfite, superoxide and ketones → Dioxirane formation or 4) organosulfonic acids / peroxide and ketones → dioxirane formation or the Systems with laccases (oxidoreductases) + NO-NOH and / or HRNOH compounds [also described in WO 98/59108 and DE 101 26 988.9 (Appendix 1)] used become.

• A) Einsatz in der Zellstoff/Holzstoffbleiche,
• B) Einsatz:
  • a) bei der Behandlung von v. a. Holzstoffabwässern der Papierindustrie und
  • b) Abwässer anderer Industriezweige,
• C) Einsatz bei der Herstellung von Ligninlösungen oder Gelen, von entsprechenden Bindern/Klebern und von Holzverbundstoffen,
• D) Einsatz als enzymatisches Deinksystem,
• E) Einsatz als Oxidationssystem bei der organischen Synthese
• F) Einsatz als Bleichmittel in Waschmitteln
• G) Einsatz in der Bleiche/Entfärbung von Textilgeweben.
• H) Einsatz bei der Verflüssigung von Kohle

Description of the various applications of the enzymatic oxidation and / or bleaching system according to the invention

• A) use in pulp / wood pulp bleaching,
• B) Use:
  • a) in the treatment of pulp waste from the paper industry and
  • b) waste water from other branches of industry,
• C) use in the production of lignin solutions or gels, of appropriate binders / adhesives and of wood composites,
• D) use as an enzymatic deinking system,
• E) Use as an oxidation system in organic synthesis
• F) Use as a bleach in detergents
• G) Use in the bleaching / decolorization of textile fabrics.
• H) Use in the liquefaction of coal

I) Use of the enzymatic oxidation and / or bleaching system according to the invention in the pulp / pulp bleach

The sulfate and sulfite processes are the main processes used today for pulp production. Both methods produce pulp under cooking and under pressure. The sulfate process works with the addition of NaOH and Na ₂ S, while in the sulfite process Ca (HSO ₃ ) ₂ + SO ₂ are used, or today, because of their better solubility, the sodium or ammonium salts of hydrogen sulfite.

The main aim of all methods is the removal of the lignin from the one used Plant material, wood or annual plants.

The lignin, which is the main component of the cellulose and hemicellulose Plant material (stem or stem) must be removed, otherwise it will not it is possible to produce non-yellowing and mechanically heavy-duty papers.

The wood fabrication processes work with stone grinders (wood sanding) or with refiners (TMP) that the wood after appropriate pretreatment (chemical, thermal or chemical-thermal) defibrillate by grinding.

These wood materials still contain a large part of the lignin. You will v. a. for the production used by newspapers, magazines etc.

For some years now, the possibilities of using enzymes for lignin degradation explored. The mechanism of action of such lignolytic systems is only a few years ago has been elucidated when it succeeded through suitable growing conditions and inductor additives sufficient amounts of enzyme in the white rot fungus Phanerochaete chrysosporium come. The previously unknown lignin peroxidases and Manganese peroxidases discovered. Since Phanerochaete chrysosporium is a very effective lignin degrader, one tried to isolate its enzymes and in purified form for lignin degradation use. However, this did not work because it turned out that the enzymes were primarily one Repolymerization of the lignin and not lead to its degradation.

The same applies to other lignolytic enzyme species such as laccases, which the lignin contains Oxidatively decompose with the help of oxygen instead of hydrogen peroxide. It was found that there are similar processes in all cases. They become radicals formed, which react with each other again and thus lead to polymerization.

Today there are only processes that work with in-vivo systems (mushroom systems). The main focus of optimization attempts is the so-called biopulping and that Biobleaching.

Biopulping is the treatment of wood chips with living ones Pilz systems.

• 1. Vorbehandlung von Hackschnitzeln vor dem Refinern oder Mahlen zum Einsparen von Energie bei der Herstellung von Holzstoffen (z. B. TMP oder Holzschliff).
  Ein Vorteil ist die meist vorhandene Verbesserung der mechanischen Eigenschaften des Stoffes, ein Nachteil die schlechtere Endweiße.
• 2. Vorbehandlung von Hackschnitzeln (Softwood/Hardwood) vor der Zellstoffkochung (Kraftprozess, Sulfitprozess).
  Hier ist das Ziel, die Reduzierung von Kochchemikalien, die Verbesserung der Kochkapazität und "extended cooking".

There are 2 types of application forms:

• 1. Pretreatment of wood chips before refining or grinding to save energy in the manufacture of wood pulp (e.g. TMP or wood pulp).
  One advantage is the mostly existing improvement in the mechanical properties of the fabric, one disadvantage is the poorer final whiteness.
• 2. Pretreatment of wood chips (Softwood / Hardwood) before cellulose cooking (power process, sulfite process).
  The goal here is to reduce cooking chemicals, improve cooking capacity and "extended cooking".

The benefits of improved kappa reduction after cooking are also compared reached for a boil without pretreatment.

Disadvantages of these procedures are clearly the long treatment times (several weeks) and V. a. the unresolved risk of contamination during treatment if you look at the probably wants to forego uneconomic sterilization of the wood chips.

Biobleaching also works with in-vivo systems. The boiled pulp (Softwood / Hardwood) is inoculated with the fungus before bleaching and treated for days to weeks. Only after this long treatment period is there a significant reduction in the kappa number and whiteness, making the process uneconomical for implementation in the makes common bleaching sequences.

Another application, usually carried out with immobilized fungal systems, is Treatment of pulp wastewater, especially bleaching wastewater their decolorization and reduction of the AOX (reduction of chlorinated compounds in the Waste water that cause chlorine or chlorine dioxide bleaching stages).

In addition, hemicellulases and the like are known. a. Xylanases, mannanases as "bleach boosters" use.

These enzymes are mainly intended to partially counteract residual lignin after the cooking process overlapping, reprecipitated xylan act and by its degradation the accessibility of the Lignins for the bleaching chemicals used in the subsequent bleaching sequences (especially Chlorine dioxide). The savings in bleaching chemicals demonstrated in the laboratory were only partially confirmed on a large scale, so that this enzyme type can at best be called Can classify bleach additive.

In the application PCT / EP 87/00635 a system for removing lignin from Lignin cellulosic material with simultaneous bleaching described with lignolytic enzymes from white rot fungi with the addition of reducing and Oxidizing agents and phenolic compounds work as mediators.

In DE 40 08 893 C2, in addition to the Red / Ox system, "mimic substances", which the Simulate active center (prosthetic group) of lignolytic enzymes, added. So it was possible to achieve a significant improvement in performance.

In the application PCT / EP 92/01086, a redox cascade is included as an additional improvement Help of phenolic or non-phenolic "tuned" in the oxidation potential Aromatics used.

In all three processes, the limitation for large-scale use is Applicability for low consistencies (up to a maximum of 4%) and for the last two Registrations additionally the risk of "leaching" of metals when using the Chelate compounds v. a. with downstream peroxide bleaching stages to destroy the Peroxide can lead.

Methods are known from WO 94/12619, WO 94/12620 and WO 94/12621 in which the Peroxidase activity is promoted by means of so-called enhancer substances. The enhancer substances are described in WO 94/12619 on the basis of their half-life characterized.

According to WO 94/12620, enhancer substances are characterized by the formula A = N-N = B, where A and B are each defined cyclic radicals.

According to WO 94/12620, enhancer substances are organic chemicals that have at least two contain aromatic rings, at least one of which has defined radicals is substituted.

All three applications concern "dye transfer inhibition" and the use of the respective Enhancer substances together with peroxidases as a detergent additive or detergent Composition in the detergent area.

Although in the description of the application on a usability for treating Lignin referred, but own experiments with those specifically disclosed in the registrations Substances showed that they act as mediators to increase the bleaching effect of the peroxidases showed no effect when treating materials containing lignin!

WO 94/29510 and WO 96/18770 describe a process for the enzymatic Delignification, in which enzymes are used together with mediators. As mediators compounds having the structure NO, NOH or HRNOH are generally disclosed.

• - Es ist nur zu relativ hohen Preisen und nicht in hinreichenden Mengen verfügbar.
• - Es reagiert unter Delignifizierungsbedingungen zu 1H-Benzotriazol und gefärbten anderen Produkten.
• - Diese Verbindung ist relativ schlecht abbaubar und kann in größeren Mengen eine Umweltbelastung darstellen.
• - Es führt in gewissem Umfang zu einer Schädigung von Enzymen.
• - Seine Delignifizierungsgeschwindigkeit ist nicht allzu hoch.

Of the mediators listed in WO 94/29510 and WO 96/18770, 1-hydroxy-1H-benzotriazole (HBT) provides the best results in delignification. However, HBT has several disadvantages:

• - It is only available at relatively high prices and not in sufficient quantities.
• - It reacts under delignification conditions to 1H-benzotriazole and colored other products.
• - This compound is relatively poorly degradable and can be an environmental impact in large quantities.
• - It damages enzymes to some extent.
• - Its delignification speed is not too high.

Further mediators of the described NO, NOH and HRN-OH types show the most of these disadvantages are not, but still have the disadvantage of being relatively high Chemical use, the chemicals used v. a. also through their physiological reactivity cannot be entirely harmless (mostly NO radical formation). It is therefore desirable to use systems for changing, breaking down or bleaching lignin, to provide lignin-containing materials or similar substances that the named Do not have disadvantages or to a lesser extent.

This can be done by using the oxidation and bleaching system according to the invention achieved that does not have these disadvantages, i. H. it was completely surprising found that when using the inventive enzymatic oxidation system special combination of the components in comparison to the above efficiency superior to enzymatic systems can be achieved.

IIa) The use of the enzymatic oxidation and / or Bleaching system for the enzymatic treatment of special waste water (Paper industry waste water e.g. from wood pulping plants or refiner plants), or II b) Use for the enzymatic treatment of waste water from other branches of industry

In contrast to most enzymes, oxidases and peroxidases have a low level Substrate specificity, i. H. they can contain a wide range of substances, usually phenolic in nature. Without mediators, the oxidases tend, but also many Peroxidases to radical polymerize phenolic substances, a property that z. B. the laccase belonging to the oxidases is also attributed in nature. This Ability to use suitable substances such as B. polymerize lignins, d. H. the corresponding To enlarge molecules by "coupling reactions", for. B. for treatment lignin-containing waste water from the paper industry such as TMP waste water (waste water from production thermomechanical pulp by means of refiners) and grinding waste water from wood grinding plants be used.

The water-soluble lignin compounds contained in this waste water (Polyphenolpropane bodies) are mainly responsible for the high COD (chemical Oxygen requirement = high pollution with organic material) and can be with conventional Technology cannot be removed. In the wastewater treatment plant and the following waters are it does not degrade, or degrades only very slowly. These connections can even be too high Concentrations have an inhibiting effect on the bacteria in a sewage treatment plant and lead to malfunctions. In this application, the enzyme effect is immediately reduced by a rapid clouding of the to recognize treated wastewater, caused by the enlarged and therefore insoluble lignin molecules. So enlarged by molecular weight enzymatic catalysis, the target molecules (polymerized lignin) can be treated appropriately (Flocculation, precipitation e.g. with aluminum sulfate / sodium aluminate, possibly with the addition of Remove polyelectrolytes / cationic or anionic or sedimentation). The sewage then shows a significantly reduced COD. It therefore causes an initiation lower environmental pollution, or increased safety, under the permitted COD Load limits remain what v. a. with a "driving style" at the limit, which is often the case Case is, is important.

In this treatment with e.g. B. only laccase, however, represents the effort for removal the reaction products of the enzymatic treatment by flocculation, sedimentation or precipitation or combinations of several methods the vast majority the cost of the overall process.

It has now been found, completely surprisingly, that when using the inventive enzymatic oxidation and bleaching system with a special combination of components an efficiency that is superior to the enzymatic systems described above can be achieved, d. H. the inventive method contrasts with the above mentioned systems with oxidoreductases (such as laccases) as oxidation catalysts significantly improved systems, the advantages of v. a. in their higher oxidizing power, in the Use of very easily degradable system components, which is the COD Increase at short notice, but easy to remove in the subsequent wastewater treatment plant steps are.

Other special compounds (polymerization catalysts) are added to these systems. given that serve as condensation nuclei and the oxidative lignin polymerization essential can strengthen, so that a main goal of this enzymatic wastewater treatment, the the lowest possible use of cost-intensive precipitant can be achieved.

All other wastewater from industries where phenolic or general Oxidizable substances are contained (e.g. lignin, dyes, etc.), can in principle with z. B. the above-mentioned oxidoreductases are treated. So there are z. B. sewage from wineries, olive mills, from dye shops in the textile industry, waste water Pulp mills etc. in question for such treatment. However, if possible contaminated sub-streams before being mixed with other wastewater to be treated optimally To achieve efficiency.

Here too it was surprisingly found that the use of the invention enzymatic oxidation system works very well to treat the above mentioned wastewater is suitable and z. T. has performance advantages over oxidoreductase systems.

Here, too, is the addition of the special compounds mentioned above:
Polymerization catalysts are provided.

Such substances can be phenols, phenol derivatives or other phenolic polycycles with a Series of oxidizable hydroxyl groups.

Such polymerization catalysts e.g. B. are preferably those as in WO 98/59108 and DE 101 26 988.9.

III) Use of the enzymatic oxidation and / or bleaching system according to the invention in the production of lignin solutions or gels, from corresponding Binders / adhesives and wood composites

The present invention has set itself the goal of a method for enzymatic Polymerization and / or modification of lignin or lignin-containing materials to provide, e.g. B. for use in the production of wood compositions or wood composites such as B. "fiber board" made of frayed wood or "particle board" from wood shavings or pieces of wood (→ chipboard, plywood, wood composite beams).

From the literature and patent specifications such. B. WO 94/01488, WO 93/23477, WO 93/25622 and DE 30 37 992 C2 it is known that laccases, lignin peroxidases or peroxidases too were used for this purpose. However, the main disadvantage is the v. a. in case of Laccases and lignin peroxidases present difficult production of these enzymes and that low yields even with genetically modified systems.

It has now been found, completely surprisingly, that here too the inventive one enzymatic oxidation system a superior performance to that in the prior art described enzymatic systems for the polymerization and / or modification of lignin and / or lignin-containing materials.

The enzymatic oxidation system according to the invention is combined with lignin (e.g. Lignosulfonates and / or non-evaporated or evaporated sulfite waste liquor and / or Sulfate lignin → "Kraft lignin", e.g. B. indulin) and / or lignin-containing material brought together.

The lignin and / or the lignin-containing material can either be at higher pH values be pre-incubated, d. H. at pH values above pH 8, preferably at pH values between 9.5 to 10.5 at 20 to 100 ° C (preferably at 60 to 100 ° C) and then the pH below pH 7 are shifted, depending on the optimal active pH range of the enzymatic Oxidation system or with an alkaline active optimum of the enzymatic oxidation system the system and lignin and / or lignin-containing material can be put together immediately done without pretreatment. Pretreatment or treatment at alkaline pH has the purpose of the much easier solubility of the lignin at these higher pH values exploit what is of great advantage for the use according to the invention, since then without organic solvents can be worked.

The described combination of the enzymatic oxidation system and lignin and / or Lignin-containing material therefore mainly serves the purpose of oxidizing a Bring about activation of the substrates (polyphenylpropane), d. H. through radical Polymerization (modification) the lignin and / or the lignin-containing material in one to transfer activated and active binder, which then, brought together with connecting (to be glued) wood fibers and / or wood parts under the influence of pressure and increased temperature to solid wood composite parts such as the above-mentioned wood materials, z. B. "fiber boards" or "particle boards" can harden.

The main advantage is the reduction or saving of normally z. B. at the Particle board production for "gluing" used urea-formaldehyde resins, which in addition to toxicological concerns, they are only partially moisture-resistant or Phenol formaldehyde resins, which have an unfavorable swelling behavior and long pressing times (also in turn next to the toxicological question).

By adding certain chemical polymerization catalysts such as. B. Polydiphenylmethyl diisocyanate (PMDI) and others, also in the polymerization of Polymerization catalysts used in lignin-containing wastewater, can the polymerizing and / or modifying effect of the enzymatic Oxidation system are further strengthened. Such substances can be phenols, phenol derivatives or other phenolic polycycles with a number of oxidizable hydroxyl groups, that have already been listed above (wastewater treatment).

IV) Use of the enzymatic oxidation and / or bleaching system according to the invention as an enzymatic deinking system

Under deinking, as is still practiced conventionally as flotation thinking is basically a two-step process.

The goal is to remove ink and other color particles from waste paper, whereby as so-called waste paper mostly the so-called "household collectibles", which mainly consist of Newspapers and magazines exist, is used.

The first treatment stage is used primarily for the mechanical / chemical removal of the color particles adhering to the paper fibers. This is done by "returning" the paper to a uniform pulp, ie by opening (shredding) the waste paper in so-called pulps, drums or the like while adding detachment-enhancing and yellowing-preventing and thus also bleaching chemicals such as sodium hydroxide solution, fatty acid, water glass and hydrogen peroxide (H ₂ O ₂ ).

The fatty acid serves as a so-called collector of the color particles, in the second Treatment stage, the flotation, also as a foam generator.

The flotation is carried out after the waste paper has been opened and a certain contact time has elapsed mentioned chemicals by blowing air into special flotation containers performed. The color particles attach themselves to the foam bubbles and become part of it carried this out, d. H. the color is separated from the paper fibers.

Today one prefers a "driving style" in a neutral pH environment, which means the use of certain detergents instead of the fatty acid.

The use of an oxidoreductase or laccase system is known from the literature (WO 91/14820, WO 92 20857), which is characterized, in particular, by the addition of special substances which, on the one hand, mainly have the optimum pH action of the laccase from Trametes shift versicolor, which is normally in the pH range of approx. pH 4-5, into the weakly alkaline range (pH 8 to 8.7), which is urgently required for use as a deinking system due to the CaSO ₄ problem occurring under pH 7, and on the other hand, do not "optimize" the laccase effect into a polymerizing or purely depolymerizing mode of action, but only cause a certain swelling of the fibers.

However, this is (like one of the main effects of caustic soda in the purely chemical Deinking systems) as a detachment mechanism for the color particles, a main performance feature.

The only other addition to this enzymatic system with oxidoreductases are Detergents necessary for foam generation.

Almost all of the detergents in question also have a color-releasing effect.

In addition, the use of sodium hydroxide solution and peroxide in conventional deinking systems Whiteness increases due to the bleaching effect of these chemicals. This bleaching effect is associated with the enzyme system according to the prior art cannot be reached due to the system.

It has now been found, completely surprisingly, that the enzymatic according to the invention Oxidation system by appropriate selection of conditions the efficiency of others outperform enzymatic deinking systems with lignin-containing deinked material and v. a. the advantage the bleaching effect of the purely chemical systems at least z. T. is compensated.

The above-mentioned addition of the special polymerization catalysts, i. H. Substances, mostly phenolic in nature and in particular with several hydroxyl groups also for enzymatic wastewater treatment and general polymerization reactions as in the production of binder / glue from lignin or lignin-containing substances v. a. to Manufacture of wood composites as polymerisation additives can find a further improvement in ink separation.

V) Use of the enzymatic oxidation and / or bleaching system according to the invention as an oxidation system in organic synthesis

In recent years, enzymes have also been increasingly used for chemical reactions used in organic synthesis.

• 1. Hydroxylierungsreaktionen
  • a) Synthese von Alkoholen
  • b) Hydroxylierung von Steroiden
  • c) Hydroxylierung von Terpenen
  • d) Hydroxylierung von Benzolen
  • e) Hydroxylierung von Alkanen
  • f) Hydroxylierung von aromatischen Verbindungen
  • g) Hydroxylierung von Doppelbindungen
  • h) Hydroxylierung von unaktivierten Methylgruppen
  • i) Dihydroxylierung von aromatischen Verbindungen
• 2. Oxidation von ungesättigten Aliphaten
  • a) Herstellung von Epoxiden
  • b) Herstellung von Verbindungen über Epoxierung
  • c) Herstellung von Arenoxiden
  • d) Herstellung von Phenolen
  • e) Herstellung von cis Dihydrodiolen
• 3. Baeyer-Villiger Oxidationen
  • a) Baeyer-Villiger Conversion von Steroiden
• 4. Oxidation von Heterocyclen
  • a) Transformation von organischen Sulfiden
  • b) Oxidation von Schwefelverbindungen
  • c) Oxidation von Stickstoffverbindungen (Bildung von N-Oxiden etc.)
  • d) Oxidation von anderen Heteoatomen
• 5. Kohlenstoff-Kohlenstoff Dehydrogenierungen
  • a) Dehydrogenierung von Steroiden
• 6. Andere Oxidationsreaktionen
  • a) Oxidation von Alkoholen und Aldehyden
  • b) Oxidation von aromatischen Methylgruppen zu Aldehyden
  • c) Oxidative Kupplung von Phenolen
  • d) Oxidativer Abbau von Alkylketten (β-Oxidation etc.)
  • e) Bildung von Peroxiden oder Perverbindungen
  • f) Initiierung von Radikalkettenreaktionen

In: Preperative Biotransformations, (Whole Cell and Isolated Enzymes in Organic Synthesis, SM Roberts; K. Wiggins; G. Casy, J. Wiley & Sons Ltd. 1992/93; Organic Synthesis With Oxidative Enzymes, HL Holland; VCH, 1992; Biotransformation in Organic Chemistry, K. Faber; Springer Verlag, 1992
Here are some examples that show a selection of oxidative reactions that can be carried out with enzymatic systems:

• 1. Hydroxylation reactions
  • a) Synthesis of alcohols
  • b) hydroxylation of steroids
  • c) Hydroxylation of terpenes
  • d) hydroxylation of benzenes
  • e) Hydroxylation of alkanes
  • f) hydroxylation of aromatic compounds
  • g) hydroxylation of double bonds
  • h) Hydroxylation of inactivated methyl groups
  • i) Dihydroxylation of aromatic compounds
• 2. Oxidation of unsaturated aliphates
  • a) Production of epoxides
  • b) Preparation of epoxy compounds
  • c) Production of arene oxides
  • d) production of phenols
  • e) Production of cis dihydrodiols
• 3. Baeyer-Villiger oxidations
  • a) Baeyer-Villiger conversion of steroids
• 4. Oxidation of heterocycles
  • a) Transformation of organic sulfides
  • b) Oxidation of sulfur compounds
  • c) Oxidation of nitrogen compounds (formation of N-oxides etc.)
  • d) Oxidation of other heteroatoms
• 5. Carbon-carbon dehydrogenation
  • a) Dehydrogenation of steroids
• 6. Other oxidation reactions
  • a) Oxidation of alcohols and aldehydes
  • b) Oxidation of aromatic methyl groups to aldehydes
  • c) Oxidative coupling of phenols
  • d) Oxidative degradation of alkyl chains (β-oxidation etc.)
  • e) formation of peroxides or per compounds
  • f) initiation of radical chain reactions

Here, too, it was surprisingly found that with the help of the enzymatic oxidation system according to the invention a variety of oxidation reactions from the exemplary enumeration shown above.

VI) Use of the enzymatic oxidation and / or bleaching system according to the invention as a bleach in detergents

The conventional bleaching systems in household detergents are unsatisfactory, particularly in the low temperature range. The standard bleach H ₂ O ₂ / sodium perborate / sodium percarbonate must be activated below 60 ° C by adding chemical bleach activators such as TAED and SNOBS. There is also a search for better biodegradable, biocompatible and low-dose bleaching systems for low-temperature laundry. While enzymes are already in technical use for protein, starch and fat solutions and for fiber treatment in the washing process, no enzymatic principle has been available for detergent bleaching.

WO 1/05839 describes the use of various oxidizing enzymes (oxidases and Peroxidases) to prevent dye transfer. Are peroxidases known to be able to use various pigments (3-hydroxyflavone and betaine Horseradish peroxidase, carotene by peroxidase) to "decolorize".

The cited patent application describes the decolorization (also called "bleaching") of textile dyes detached from the laundry and present in the liquor (conversion of a colored substrate into an undyed, oxidized substance). The enzyme is said to z. B. hypochlorite, which also attacks the dye on or in the tissue, have the advantage of decolorizing only the dye present in solution, hydrogen peroxide or a corresponding precursor or hydrogen peroxide generated in situ being involved in the catalysis of the decolorization. The enzyme reaction can be partially by adding additional oxidizable enzyme substrate, e.g. B. metal ions such as Mn ⁺⁺ , halide ions such as Cl ^- or Br ^- or organic phenols such as p-hydroxycinnamic acid and 3,4-dichlorophenol.

This involves the formation of short-lived radicals or other oxidized states of the added substrate postulated for bleaching or other modification of the colored substance are responsible.

In US 4 077 6768 the use of "iron porphin", "haemin chloride" or "iron phthalocynanine "or derivatives together with hydrogen peroxide to prevent the "Dye transfers" described. However, these substances are used with an excess of peroxide quickly destroyed, which is why the hydrogen peroxide formation must take place in a controlled manner.

Methods are known from WO / 126119, WO 94/12620 and WO 94/12621 in which the Peroxidase activity is promoted by means of so-called enhancer substances. Such enhancer substances are described in WO 94/12620 based on their half-life characterized.

According to WO 94/12621, enhancer substances are characterized by the formula A = N-N = B, where A and B are each defined cyclic radicals.

According to WO 94/12620, enhancer substances are organic chemicals that have at least two contain aromatic rings, at least one of which has defined radicals is substituted.

All three applications concern "dye transfer inhibition" and the use of the respective Enhancer substances together with peroxidases as a detergent additive or detergent Composition in the detergent area. The combination of these enhancer substances is limited to peroxidases.

The use of mixtures containing peroxidases is also known from WO 92/18687. Finally, WO 94/29425, DE 44 45 088.5 and WO 97/48786 contain multi-component bleaching systems for use with wash-active substances consisting of:
Oxidation catalysts and oxidizing agents and aliphatic, cycloaliphatic, heterocyclic or aromatic compounds containing NO, NOH or H-NR-OH.

A disadvantage of all previously known "enzymatically enhanced" detergent bleach systems is that the cleaning and bleaching effect is still unsatisfactory or the Mediator substances must be added in too large an amount and are therefore environmentally friendly and economic problems can arise.

It has now been found, completely surprisingly, that the inventive enzymatic Oxidation system exceeds the performance of the above systems and those mentioned Does not have disadvantages of the prior art.

VII) Use of the enzymatic oxidation and / or bleaching system according to the invention in the bleaching and / or discoloration of textile fabrics

Enzymes are used today in increasing quantities and for various applications in the Textile industry used.

For example, the use of amylases plays a major role in the "desizing process", which prevents the use of strong acids, bases or oxidizing agents can be.

Cellulases are also used for so-called bio-polishing as well as for so-called Bio-stoning is used, a process that is mostly combined with the conventional process of stone washing with pumice stones when treating Denim jeans are used to remove the indigo dye. WO 94/29510, WO / 96/18770, DE 196 12 194 A1 and DE 44 45 088 A1 describe Process for enzymatic delignification, in which enzymes together with Mediators are used. In general, connections with the Structure NO, NOH, or HRNOH disclosed.

However, these systems are limited to use in pulp bleaching. Because of the mechanisms involved in lignin-removing pulp bleaching and such The process here is based, completely different to a decolorization, Removal and / or "destruction" of denim dyes in the jeans area such as v. a. Indigo dyes etc., it is completely surprising that a number of substances of the mentioned NO, NOH, HNROH type is also suitable for this application. WO 97/06244 describes systems for the bleaching of cellulose, the "dye transfer inhibition" and the bleaching of stains when using detergents with enzymes (Peroxidases, laccases) and enzyme-enhancing (hetero) aromatic compounds how nitroso compounds work etc. are described.

However, as in the patents WO 94/12619, WO 94/12620 and WO 94/12621 only the use described above is provided.

The mechanisms of discoloration of stains during detergent bleaching or "dye transfer inhibition" are completely different from those used in decolorization, removal and / or "destruction" of indigo dyes, e.g. B. in denim treatment too Basically lie.

Therefore, it is also completely surprising that a number of substances mentioned above NO-, NOH-, HNROH-types is also suitable for this application.

Methods are mentioned in WO 94/12619, WO 94/12620 and WO 94/12621 known in which the activity of the peroxidase by means of so-called Enhancer substances are promoted. Such enhancer substances are described in WO 94/12620 characterized by their half-life. According to WO 94/12621 Enhancer substances characterized by the formula A = N-N = B, where A and B are each defined cyclic radicals. According to WO 94/12621 are enhancer substances organic chemicals containing at least two aromatic rings, one of which at least one is substituted with respectively defined radicals.

All three applications concern (as already mentioned) "dye transfer inhibition" and the Use of the respective enhancer substances together with peroxidases as detergent Additive or detergent composition in the detergent area as well Pulp bleaching area. The combination of these enhancer substances is on peroxidases limited.

Oxidoreductases, mainly laccases, have also recently become available Peroxidases are used to treat mainly denim jeans.

From patent application WO 96/12846 it is known that laccase or also peroxidase + certain enhancer substances, especially phenothiazine or phenoxazine derivatives, for two forms of application in the treatment of cellulose-containing tissues such as cotton, viscose, rayon, (rayon) ramie, Linen, Tencelm, silk or mixtures of these fabrics or mixtures of these fabrics with synthetic fibers such. B. Mixtures of cotton and spandex (stretch denim), but mainly denim fabrics (mainly jeans) are used:
On the one hand, the system (oxidoreductases + enhancer substances) is to be used to bleach denim instead of the usual hypochlorite bleach, usually after stone washing pretreatment, whereby this enzymatic treatment only leads to a partial replacement of hypochlorite, since the desired bleaching result is not achieved can.

Secondly, the system can be used together with cellulase in stone washing instead of usual mechanical treatment by pumice stones are used, which the Performance of "cellulase-only treatment" is said to improve.

• 1. Es muss Laccase in erheblichen Mengen eingesetzt werden (ca. 10 IU/g Denim), um das gewünschte Ergebnis zu erzielen.
• 2. Die optimale Behandlungsdauer ist z. T. 2-3 Stunden.
• 3. Der bevorzugte Mediator (hier Phenothiazin-10-propionsäure) muss in ca. 2 bis ca. 14 mg pro g Denim eigesetzt werden, was erhebliche Kosten verursacht.
• 4. Es muss in Puffersystemen (ca. 0.1 Mol/L) gearbeitet werden, da ansonsten keine Performance erreicht werden kann, was das System ebenso erheblich verteuert. Dies ist z. B. bei den erfindungsgemäßen Systemen nicht nötig.
• 5. Durch die Färbung der Enhancerkomponente (langlebiges Radikal) wird eine "Verbräunung" des Gewebes hervorgerufen.

The main disadvantages of the system described in WO / 96/12846 include the following:

• 1. Large amounts of laccase must be used (approx. 10 IU / g denim) in order to achieve the desired result.
• 2. The optimal treatment time is e.g. T. 2-3 hours.
• 3. The preferred mediator (here phenothiazine-10-propionic acid) has to be used in approx. 2 to approx. 14 mg per g denim, which causes considerable costs.
• 4. It must be worked in buffer systems (approx. 0.1 mol / L), since otherwise no performance can be achieved, which also makes the system considerably more expensive. This is e.g. B. not necessary in the systems according to the invention.
• 5. The coloring of the enhancer component (long-lived radical) causes a "browning" of the tissue.

The general main advantage of a laccase and / or oxidoreductase system Enzyme-enhancing compounds (enhancers, mediators etc.) when used in the Treatment of textiles (e.g. denim fabrics) described above, with a more optimal System than in the state of the art is that one looks fashion can achieve that does not allow a usual hypochlorite bleaching.

The dyes normally used in denim jeans are VAT dyes, such as Indigo or indigo derivatives, such as B. Thioindigo, but also so-called Sulfur dyes. By using such special enzymatic systems it is possible (through the high specificity of such systems) in mixed color systems such as B. Indigo and Sulfur dye to decolorize only the indigo dye, while the sulfur dye is not oxidized. This leads depending on the compound used to enhance the enzyme action to almost any desired color of the fabric (e.g. shades of gray etc.), often is desired.

An additional advantage is that the enzymatic treatment is essential runs more gently than bleaching with hypochlorite, resulting in less Fiber damage leads.

In the stone wash process, v. a. the ecological effect of importance (also alongside the lower fiber damage caused by the enzymes), if one z. B. considering that pro kg of jeans denim approx. 1 kg of stone sludge is created by this purely mechanical process. As stated in the prior art, the textile industry consists mainly of dyed fabrics (such as denim denim) have a great need for alternatives Bleaching process (for conventional hypochlorite bleaching) and / or Treatment method as an alternative to stone washing to achieve the so-called "bleached looks", not least because of the existing ones Environmental problems.

The present invention has set itself the goal of the disadvantages of the conventional processes: stone washing / bleaching after stone washing or general bleaching of dyed and / or undyed textile fabrics:
V. a. To minimize or eliminate environmental problems and fiber damage and also the disadvantages of the known oxidoreductase / enhancer systems (e.g. NO radical formation etc.) and also the oxidation systems enhanced by the lipase.

It has now been found, completely surprisingly, that the inventive enzymatic Oxidation system the performance of the above oxidoreductase mediator systems surpasses and does not have the mentioned disadvantages of the prior art.

Detailed description of the inventive enzymatic oxidation and / or Bleaching system related to the different applications I) Use in pulp bleaching

The effectiveness of the oxidation and bleaching system according to the invention when changing, breaking down or bleaching lignin, lignin-containing materials or similar substances is often further increased if Mg ²⁺ ions are present in addition to the components mentioned. The Mg ²⁺ ions can, for example, as a salt, such as. B. MgSO ₄ can be used. The concentration is in the range of 0.1-2 mg / g of lignin-containing material, preferably 0.2-0.6 mg / g.

In some cases, a further increase can be achieved in that the system in addition to the Mg ²⁺ ions also complexing agents such as. B. ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), hydroxyethylenediaminetriacetic acid (HEDTA), diethylenetriaminepentamethylenephosphonic acid (DTMPA), nitrilotriacetic acid (NTA), polyphosphoric acid (PPA) etc. The concentration is in the range of 0.2-5 mg / g of lignin-containing material, preferably 1-3 mg.

Surprisingly, it was also found that an acid wash (pH 2 to 6, preferably 2 to 5) or Q stage (pH 2 to 6, preferably 2 to 5) before or after the treatment with the inventive oxidation and bleaching process for some pulps to one Significant kappa reduction compared to treatment without this special pre or aftertreatment. In the Q stage, chelating agents are used for this purpose usual substances (such as EDTA, DTPA) are used. They are preferably in Concentrations from 0.1% / to to 1% / to, particularly preferably 0.1% / to to 0.5% / to used.

At the same time, reducing agents can be added together with the existing ones Oxidizing agents are used to set a certain redox potential.

Sodium bisulfite, sodium dithionite, ascorbic acid, Thio compounds, mercapto compounds or glutathione etc. can be used.

Radical formers or radical scavengers (interception of for example OH Oor OOH ˙ radicals) are added. They can do that Improve interaction within the Red / Ox and radical mediators.

Other metal salts can also be added to the reaction solution.

These are important in conjunction with chelating agents as radical formers or red / ox centers. The salts form cations in the reaction solution. Such ions include Fe ²⁺ , Fe ³⁺ , Mn ²⁺ , Mn ³⁺ , Mn ⁴⁺ , Cu ¹⁺ , Cu ²⁺ , Ca ²⁺ , Ti ³⁺ Cer ⁴⁺ , Al ³⁺ .

The chelates present in the solution can also act as mimic substances for certain oxidoreductases such as laccases (copper complexes) or for the lignin or Manganese peroxidases (heme complexes) are used. Such substances are included under mimic substances understand that simulate the prosthetic groups of (here) oxidoreductases and z. B. Can catalyze oxidation reactions.

Finally, it is also possible to work using detergents. As such non-ionic, anionic, cationic and amphoteric surfactants are suitable. The Detergents can penetrate the enzymes and other components into the fiber improve.

It may also be beneficial for the reaction to add polysaccharides and / or proteins. Here in particular as polysaccharides are glucans, mannans, dextrans, levans, pectins, Alginates or plant gums and as proteins gelatin and albumin. These substances mainly serve as protective colloids for the enzymes.

Other proteins that can be added are proteases such as pepsin, bromelin, papain etc. These can u. a. serve by breaking down the extensin present in the wood (hydroxyproline-rich protein) to achieve better access to lignin.

Amino acids, simple sugar, oligomer sugar, PEG- Types of different molecular weights, polyethylene oxides, polyethyleneimines and Polydimethylsiloxanes in question.

Furthermore, substances can be added to the oxidation and bleaching system according to the invention be, which increase the hydrophobicity of the reaction environment and thus swelling on the Lignin acts in the fibers and thus increases its vulnerability.

Such substances are e.g. B. glycols such as: propylene glycol, ethylene glycol, glycol ethers such as: ethylene glycol dimethyl ether etc. but also solvents such as. B Alcohols such as: methanol, ethanol, butanol, amyl alcohol, cyclohexanol, benzyl alcohol, chlorohydin, phenols such as: phenol, methyl and methoxyphenols, aldehydes such as: formaldehyde, chloral, mercaptans such as: buthyl mercaptan, benzyl mercaptan, thioglycolic acid, organic acids such as: Formic acid, acetic acid, chloroacetic acid, amines such as ammonia, hydrazine, hydrotopic solvents such as: e.g. B. conc. Solutions of sodium benzoate, others such as: benzenes, pyridines, dioxane, acetoacetic acid ethyl ester, other basic solvents such as OH ^- / H ₂ O, or OH ^- / alcohols etc.

The process according to the invention can be used not only in the delignification (bleaching) of sulfate, Sulfite, organosolv, or the like Pulp and wood pulp are used, but also at the production of cellulose in general, whether from wood or annual plants, if one Defibrillation through the usual cooking methods (possibly connected with mechanical Process or printing), d. H. a very gentle cooking up to kappa numbers that are in the range 50-120 kappa can be guaranteed.

In the bleaching of cellulose as well as in the production of cellulose, the treatment with the oxidation and bleaching system according to the invention can be carried out once or repeated several times, either before and / or after washing and extraction of the treated material with NaOH etc. or without these intermediate steps before and / or after pre- and / or post-treatment steps such as acid wash, Q-stage, alkaline leaching, bleaching stages: as peroxide bleaching, O ₂ -reinforced peroxide stages, Druckperoxidstufen, O ₂ -Delignifizierung, Cl ₂ -bleaching, ClO ₂ -bleaching, Cl ₂ / ClO ₂ bleaching, peracid bleaching stages, peracid-enhanced O ₂ bleaching / peroxide bleaching, ozone bleaching, dioxirane bleaching, reductive bleaching stages, other treatments such as: swelling stages, sulfonations, NO / NO ₂ treatments, nitrosyl-sulfuric acid treatment, enzyme treatments such as e.g. B. Treatments with hydrolases such as cellulases and / or hemicellulases (e.g. xylanase, mannanase etc.) and / or amylases and / or pectinases and / or proteinases and / or lipases and / or amidases and / or oxidoreductases such as e.g. B. laccases and / or peroxidases etc. or several combined treatments. This leads to kappa values which can be reduced still further and to substantial increases in whiteness. Likewise, an O ₂ stage can be used before the treatment with the oxidation and bleaching system according to the invention or, as already mentioned, an acid wash or Q stage (chelate stage) can also be carried out.

The invention is explained in more detail below with the aid of examples:

example 1 Enzymatic bleach with laccase / square acid / acetylacetone and softwood (Sulphate pulp)

• A) 20 ml Leitungswasser werden mit 0.1 kg Quadratsäure und 1 kg Acetylaceton pro to Zellstoff unter Rühren versetzt, der pH-Wert mit 0,5 mol/l H₂SO₄-Lsg. so eingestellt, daß nach Zugabe des Zellstoffs und des Enzyms pH 4,5 resultiert.
• B) 5 ml Leitungswasser werden mit der Menge Laccase von Trametes versicolor versetzt, daß eine Aktivität von 2 U* pro g Zellstoff resultiert.

5 g dry cellulose (Softwood O ₂ delignified), consistency 30% (approx. 17 g wet) are added to the following solutions:

• A) 20 ml of tap water are mixed with 0.1 kg of squaric acid and 1 kg of acetylacetone per ton of pulp with stirring, the pH with 0.5 mol / l H ₂ SO ₄ solution. adjusted so that pH 4.5 results after the addition of the pulp and the enzyme.
• B) 5 ml of tap water are mixed with the amount of laccase from Trametes versicolor that an activity of 2 U * per g of pulp results.

Solutions A and B are added together and made up to 33 ml. After adding the pulp, it is mixed for 2 min with a dough kneader. Then the substance is placed in a shaking water bath at 45 ° C for 1-4 hours incubated with gentle shaking.

The fabric is then washed over a nylon sieve (30 µm) and at 1 hour 70 ° C, 2% consistency and 8% NaOH extracted per g of pulp.

After washing the fabric again, the kappa number is determined.

Example 2 Enzymatic bleaching with laccase / 4-tert-butylurazole / acetylacetone and Softwood (sulfate pulp)

• A) 20 ml Leitungswasser werden mit 2 kg 4-tert.-Butylurazol und 1 kg Acetylaceton pro to Zellstoff unter Rühren versetzt, der pH-Wert mit 0,5 mol/l H₂SO₄-Lsg. so eingestellt, daß nach Zugabe des Zellstoffs und des Enzyms pH 4,5 resultiert.
• B) 5 ml Leitungswasser werden mit der Menge Laccase von Trametes versicolor versetzt, daß eine Aktivität von 2 U* pro g Zellstoff resultiert.

5 g dry cellulose (Softwood O ₂ delignified), consistency 30% (approx. 17 g wet) are added to the following solutions:

• A) 20 ml of tap water are mixed with 2 kg of 4-tert-butylurazole and 1 kg of acetylacetone per ton of pulp with stirring, the pH with 0.5 mol / l H ₂ SO ₄ solution. adjusted so that pH 4.5 results after the addition of the pulp and the enzyme.
• B) 5 ml of tap water are mixed with the amount of laccase from Trametes versicolor that an activity of 2 U * per g of pulp results.

Solutions A and B are added together and made up to 33 ml. After adding the pulp, it is mixed for 2 min with a dough kneader. Then the substance is placed in a shaking water bath at 45 ° C for 1-4 hours incubated with gentle shaking.

The fabric is then washed over a nylon sieve (30 µm) and at 1 hour 70 ° C, 2% consistency and 8% NaOH extracted per g of pulp.

After washing the fabric again, the kappa number is determined.

Example 3 Enzymatic bleaching with laccase / adipic acid dihydrazide / acetylacetone and Softwood (sulfate pulp)

• A) 20 ml Leitungswasser werden mit 2 kg Adipinsäure-Dihydrazid und 1 kg Acetylaceton pro to Zellstoff unter Rühren versetzt, der pH-Wert mit 0,5 mol/l H₂SO₄-Lsg. so eingestellt, daß nach Zugabe des Zellstoffs und des Enzyms pH 4,5 resultiert.
• B) 5 ml Leitungswasser werden mit der Menge Laccase von Trametes versicolor versetzt, daß eine Aktivität von 2 U* pro g Zellstoff resultiert.

5 g dry cellulose (Softwood O ₂ delignified), consistency 30% (approx. 17 g wet) are added to the following solutions:

• A) 20 ml of tap water are mixed with 2 kg of adipic acid dihydrazide and 1 kg of acetylacetone per ton of pulp with stirring, the pH with 0.5 mol / l H ₂ SO ₄ solution. adjusted so that pH 4.5 results after the addition of the pulp and the enzyme.
• B) 5 ml of tap water are mixed with the amount of laccase from Trametes versicolor that an activity of 2 U * per g of pulp results.

Solutions A and B are added together and made up to 33 ml. After adding the pulp, it is mixed for 2 min with a dough kneader. Then the substance is placed in a shaking water bath at 45 ° C for 1-4 hours incubated with gentle shaking.

The fabric is then washed over a nylon sieve (30 µm) and at 1 hour 70 ° C, 2% consistency and 8% NaOH extracted per g of pulp.

After washing the fabric again, the kappa number is determined.

Example 4 Enzymatic bleaching with laccase / hydantoyl-5-acetic acid / acetylacetone and Softwood (sulfate pulp)

• A) 20 ml Leitungswasser werden mit 2 kg Hydantoyl-5-essigsäure und 1 kg Acetylaceton pro to Zellstoff unter Rühren versetzt, der pH-Wert mit 0,5 mol/l H₂SO₄-Lsg. so eingestellt, daß nach Zugabe des Zellstoffs und des Enzyms pH 4,5 resultiert.
• B) 5 ml Leitungswasser werden mit der Menge Laccase von Trametes versicolor versetzt, daß eine Aktivität von 2 U* pro g Zellstoff resultiert.

5 g dry cellulose (Softwood O ₂ delignified), consistency 30% (approx. 17 g wet) are added to the following solutions:

• A) 20 ml of tap water are mixed with 2 kg of hydantoyl-5-acetic acid and 1 kg of acetylacetone per ton of pulp with stirring, the pH with 0.5 mol / l H ₂ SO ₄ solution. adjusted so that pH 4.5 results after the addition of the pulp and the enzyme.
• B) 5 ml of tap water are mixed with the amount of laccase from Trametes versicolor that an activity of 2 U * per g of pulp results.

Solutions A and B are added together and made up to 33 ml. After adding the pulp, it is mixed for 2 min with a dough kneader. Then the substance is placed in a shaking water bath at 45 ° C for 1-4 hours incubated with gentle shaking.

The fabric is then washed over a nylon sieve (30 µm) and at 1 hour 70 ° C, 2% consistency and 8% NaOH extracted per g of pulp.

After washing the fabric again, the kappa number is determined.

* 1U = conversion of 1 µmol syringaldazine / min / mg dry enzyme substance

Example 5 Enzymatic bleaching with HRP / dicyandiamide / acetylacetone and Softwood (Sulphate pulp)

• A) 20 ml Leitungswasser werden mit 2 kg Dicyandiamid, 1 kg Acetylaceton und 2 kg Peroxid pro to Zellstoff unter Rühren versetzt, der pH-Wert mit 0,5 mol/l H₂SO₄-Lsg. so eingestellt, daß nach Zugabe des Zellstoffs und des Enzyms pH 4,5 resultiert.
• B) 5 ml Leitungswasser werden mit 0.1 mg HRP pro g Zellstoff versetzt.

5 g dry cellulose (Softwood O ₂ delignified), consistency 30% (approx. 17 g wet) are added to the following solutions:

• A) 20 ml of tap water are mixed with 2 kg of dicyandiamide, 1 kg of acetylacetone and 2 kg of peroxide per ton of pulp with stirring, the pH with 0.5 mol / l H ₂ SO ₄ solution. adjusted so that pH 4.5 results after the addition of the pulp and the enzyme.
• B) 0.1 ml HRP per g pulp are added to 5 ml tap water.

Solutions A and B are added together and made up to 33 ml.

After adding the pulp, it is mixed for 2 min with a dough kneader. Then the substance is placed in a shaking water bath at 45 ° C for 1-4 hours incubated with gentle shaking.

The fabric is then washed over a nylon sieve (30 µm) and at 1 hour 70 ° C, 2% consistency and 8% NaOH extracted per g of pulp.

After washing the fabric again, the kappa number is determined.

Claims (16)

1. A method for oxidation and / or bleaching, characterized in that a) Oxidoreductases such as laccases and / or peroxidases - individually or in combination - in the presence of their respective co-substrates O ₂ , H ₂ O ₂ , organic peroxides, peracids etc. are used to activate compounds from the class of oxocarbons, from the class the urazoles and hydrazides, from the class of hydantoins, and the class of nitrile (cyan) compounds and that b) carbonyl compounds (ketones, aldehydes) can additionally be used, which can form active oxygen species such as dioxiranes, dioxetanes, peroxy compounds, etc. or other reactive compounds or transition stages such as radicals, cation radicals, anion radicals or reactive (redox-active) neutral compounds with the activated compounds. 2. Oxidation and / or bleaching system according to claim 1, characterized in that that as compounds to be activated are those from the group of oxocarbons such as α-hydroxycarbonyl compounds, α-dicarbonyl compounds, β- Hydroxycarbonyl compounds and β-dicarbonyl compounds, open chain Double bond compounds (enols) and compounds from the group of cyclic oxocarbons such as triangular acid, square acid, croconic acid, Rhodizonic acid and tetrahydroxy-p-hydroquinone and their salts and derivatives be used. 3. Oxidation and / or bleaching system according to claim 1, characterized in that that as compounds to be activated are those from the group of amides such as Hydrazides, cyclic hydrazides, urazoles and phthalhydrazides can be used. 4. Oxidation and / or bleaching system according to claim 1, characterized in that that as compounds to be activated are those from the group of imides such as Hydantoins, cyclic imides and hydantoin derivatives are used. 5. Oxidation and / or bleaching system according to claim 1, characterized in that as Compounds to be activated are those from the group of nitrile (cyan) compounds such as Cyanamide or dicyandiamide can be used. 6. Oxidation and / or bleaching system according to claim 1, characterized in that in addition carbonyl compounds, in particular non-cyclic compounds, are used. 7. Bleaching system according to claim 1, characterized in that oxidoreductases of the classes 1.1.1. up to 1.97. 8. oxidation and / or bleaching system according to claim 1, characterized in that as Oxidoreductases, laccases and peroxidases are used. 9. oxidation and / or bleaching systems according to claim 1, characterized in that as additional systems of enzymatic oxidation systems can be added simultaneously or can be used in any order in time such as: HOS system, peroxynitrite system, ferrocene / peroxide system, Organosulfonic acid / peroxide / ketone system, activated sulfite / superoxide / ketone system and oxidoreductase Mediator system. 10. Oxidation and / or bleaching systems according to claim 1, characterized in that the co-substrate is preferably air, oxygen, peroxide compounds such as: H ₂ O ₂ , organic peroxides, peracids such as peracetic acid, performic acid, persulfuric acid, persalpic acid, metachloroperoxidbenzoic acid, per compounds such as : Perborates, percarbonates, persulfates or oxygen species and their radicals such as OH radical, OOH radical, OH ⁺ radical, superoxide (O ^- ₂ ), singlet oxygen, are used. 11. Use of the oxidation and bleaching system according to claim 1 to 10 in a process for delignification and / or modification and / or bleaching of cellulose from wood and annual plants and wood pulp and deinked material, the reaction of the oxidation and bleaching systems in a pH range of pH 3 to 11, preferably pH 3 to 9, at a temperature of 20 to 95 ° C, preferably 40 to 95 ° C, at a consistency of 0.5 to 40%, preferably 4 to 15% in the presence of oxygen or air at normal pressure to slight O ₂ overpressure (up to 2 bar) and the laccase concentration, or peroxidase concentration in the range of 2-500 g pure enzyme per ton of pulp, the concentration of the compound to be activated of 1-15 kg per ton of pulp , H ₂ O ₂ in the range of 0.2 to 15 kg per ton and the carbonyl compound in the range of 0.2 to 5 kg / ton of pulp. 12. Use of the oxidation and / or bleaching system according to claim 1 to 11 in a process for delignification and / or change and / or bleaching of wood pulp and annual plants and wood pulp and deinked material, being an acid wash or Q stage before and / or after the reaction of the enzyme system is used and that the acidic wash at 60-120 ° C, at pH 2 to 5.5, for 30-90 min and 4-20% consistency is carried out and that the Q stage with 0.05-1%, preferably 0.2 to 0.5% chelating agent, at 60-100 ° C, at pH 2 to 5.5, for 30-90 min and 4-20% consistency is carried out. 13. Use of the oxidation and / or bleaching system according to claim 1 to 12 in one Process for delignification and / or modification and / or bleaching of cellulose from wood and annual plants and wood materials and deinked materials, whereby for the acid Wash and the Q level 1 hour, 60-90 ° C, pH 2 to 5 and 10% consistency are observed. 14. Use of the oxidation and bleaching system according to claim 1 to 13 in a process for delignification and / or modification and / or bleaching of cellulose from wood and annual plants and wood pulp and deinked material, be it before or after every possible treatment of the cellulose Cooking processes, bleaching stages or other pre-treatment and / or post-treatment can be used in one or more, such as alkaline leaching, alkaline extraction, washing, acid treatment, Q-stage, O ₂ -delignification stage, peroxide bleaching stage, O _2- assisted peroxide stage, pressure peroxide stage , Peracid level, peracid-supported O ₂ or peroxide level, ozone bleaching level, dioxirane level, polymetoxalate level C1 delignification level, ClO ₂ bleaching level, Cl / ClO ₂ bleaching level, reductive bleaching levels, sulfonation levels, NO / NO ₂ treatments, nitrosylsulfuric acid treatment, Source stages, enzyme treatments such as B. Treatments with hydrolases such as cellulases and / or hemicellulases (e.g. xylanase, mannanase etc.) and / or pectinases and / or proteinases and / or lipases and / or amidases and / or oxidoreductases such as e.g. B. laccases and / or peroxidases etc. or several combined treatments. 15. Use of the oxidation and / or bleaching system according to claim 1 to 14 in one process for delignification and / or modification and / or bleaching of wood pulp and Annual plants and wood pulps and deinked materials, being carried out in several stages with a wash or wash and extraction with lye between each stage or there is no washing or extraction. 16. Use of the oxidation and bleaching system according to claim 1 to 15 for use in the pulp delignification / bleaching, the use in the treatment of v. a. Pulp waste water from the paper industry and waste water from other branches of industry, for use in the Production of lignin solutions or gels, of appropriate binders / adhesives and of Wood composites, for use as an enzymatic deinking system, for use as Oxidation system in organic synthesis for use as a bleach in Detergents, for use in the baking / decolorization of textile fabrics and for use in the liquefaction of coal.