DE10126988A1 - Systems for oxidation or bleaching, especially of pulp, comprise a component enzymatically generating peroxide, superoxide or other reactive oxygen species, and a precursor formed enzymatically, or is oxidizably reactive - Google Patents

Abstract

A system for oxidation or bleaching comprises components slowly and continuously enzymatically generating peroxide, superoxide or other reactive oxygen species (ROS), and a specified precursor which is either formed enzymatically or is an oxidizable or (A)-reactable compound. Oxidation or bleaching systems, comprising: (a) components slowly and continuously enzymatically generating peroxide, superoxide or other reactive oxygen species (ROS); and (b) a precursor which is either formed enzymatically or is an oxidizable or (a)-reactable compound comprising either: (i) compounds which enzymatically or in-situ set free NO, NO<+> or NO<-> which react with (a) to form reactive nitrogen species (RNS) (e.g. peroxynitrites or the corresponding protonated acids); (ii) dicyclopentadienyl-transition metal complexes which can activate peroxides produced by (a); or (iii) organosulfonic acids or activated sulfites which can be generated in association with (a) and ketones, e.g. dioxiranes.

Description

It is known that enzymes such as e.g. B. glucose oxidase (GOD), which can form H ₂ O ₂ from glucose, this H ₂ O ₂ for enzymes (oxidoreductases), e.g. B. certain peroxidases such as man peroxidases (MnP's) are available, with the help of which the peroxidase can oxidize corresponding substrates.

The main reason for the enzymatic generation of peroxide instead of the usually cheaper direct addition of peroxide (H ₂ O ₂ ) is the sensitivity of such enzymes to high peroxide concentrations.

In addition, these systems consist of a reactive oxygen generator Component (peroxide); but this peroxide does not directly serve as oxidants for the substrate, which would then become the actual oxidant, but the substrate is made using the peroxi this oxidizes and then usually forms the end product.

It is known from many reactions, e.g. B. certain epoxidation reactions with dioxran, which z. B. from certain peracids and acetone that is very large amounts of peracids and acetone needed to get satisfactory epoxidations that but with slow and continuous addition of the dioxirane formation components a we Significantly less quantity is required with better selectivity and performance. Therefore, it is very important for many oxidation reactions and often a mandatory advance setting for commercial applicability (e.g. also for the delignification of pulp), the active agent slowly, d. H. adapted to the corresponding reaction kinetics and kon to be fed continuously.

This task is accomplished by the enzymatic generation in situ, that is, the goal of The present invention is enzymatic systems for generating active oxygen to provide species as a system component, the most important property this system component the directed and continuous availability of the ge called reactive oxygen species.

Active oxygen species or reactive oxygen species (ROS) in general are understood to mean:
Peroxide (H ₂ O ₂ ) and peroxide compounds, the radicals: superoxide radical (O ₂ ^-. ), Hydroxyl radical (OH ^. ) Peroxyl radical (ROOH ^. ), Alkoxyl radical (RO ^. ) And hydroxyper oxyl radical (HOO ^. ), Also ozone, dioxetane, Dioxirane, singlet oxygen and peroxynitrite, which, however, also belongs to the reactive nitrogen compounds (RNS) (see below). Oxygen itself can play a role when activated by enzymes or transition metals. Furthermore, the aim of the present invention is to provide a precursor component which is converted into the actual oxidant by the continuously formed reactive oxygen species.

These precursor substances can be oxidized by the reactive oxygen species Substances, or those that react specifically with them to form an oxidant. This can be added to the oxidation system or also continuously enzymatically to be generated.

The aim of the present invention is therefore to provide an oxidation system which consists of a component for the enzymatic generation of reactive oxygen species exists and as a second component contains precursor substances, by the reaction of which actual oxidants are formed, at least one system component being enzymatic is formed.

Areas of application for these oxidation and bleaching systems are primarily intended for use in the Cellulose bleach or wood pulp bleach, the use for the oxidative treatment of Sewage of all kinds, the use in the production of wood composites, the use as an enzymatic deinking system, use as an oxidative agent in organic Synthesis, use as a bleaching system in detergents, use as a bleach or Oxidizing agents in the textile industry (e.g. stone washing and bleaching of fabrics) and the use in the liquefaction of brown coal or hard coal, as these are new Systems many of the disadvantages of purely chemical systems (e.g. significant environmental problems) or other enzymatic systems (often too low performance and high costs) exhibit. The possibility of using the systems should not be based on these applications be limited.  

It has surprisingly been found that when using these oxidation and / or bleaching systems according to the invention consisting of:

• A) enzymatic peroxide or superoxide or other reactive oxygen species (ROS) generating component that this (ROS) slowly and continuously for ver addition represents and
• B) a special precursor component which is either formed enzymatically or which is an oxidizable or reactive compound with respect to (A), the special precursor component in (B) consisting of either
  • 1. Special compounds exist which can release NO, NO ⁺ or NO ^- enzymatically or in situ, which form with (A) reactive nitrogen species (RNS) such as. B. peroxynitrites or the corresponding protonated acid form or:
  • 2. consists of dicyclopentadienyl transition metal complexes which can activate the peroxide provided by (A) or:
  • 3. consists of special organosulfonic acids or activated sulfite, which in conjunction with (A) and ketones, for. B. can generate dioxiranes

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 can be found after deinking processes.

In the oxidative treatment of waste water, such as waste water from the wood pulp manufacturing (wood pulp, refiner), from the pulp industry and dye-contaminated Sewage, e.g. B. the textile industry, could also surprisingly an oxidative Polymerization of lignin and / or lignin-like substances and / or decolorization be shown.

This oxidative polymerization of lignin and / or lignin-like substances was also able surprisingly when used in the manufacture of wood composites (binder and / or adhesive production by oxidative polymerization of the polyphenylpro present carcass) are confirmed.

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

Surprisingly, coal liquefaction properties also became apparent during the treatment of brown or hard coal found.

In addition, surprisingly, a high and selective oxidizing power was found in the Use as an "oxidizing agent" in organic synthesis, a strong bleaching power when using bleach in detergents and in general Bleaching of textile fabrics or the special bleaching when used in stone-wash Processes, namely as a substitute for mechanical color removal and / or after bleaching these processes.

Description of the system components of the enzymatic systems for the generation of active Oxygen species and their reaction with other precursors for use in Oxidations and / or bleaching SYSTEM COMPONENT A

System component (A) of the oxidation and / or bleaching system according to the invention includes:
Enzymatic peroxide or superoxide or other reactive oxygen species (ROS) generating component, which makes this (ROS) available slowly and continuously. Particularly preferred enzymes are oxidases with O ₂ as acceptor of class 1.1.3 according to the International Enzyme Nomenclature: Committee of the International Union of Biochemistry and Molecular Biology (Enzyme Nomenclature, Academic Press, Inc., 1992, pp. 55-60 ) such as B .:
Malate oxidase 1.1.3.3, glucose oxidase (GOD) 1.1.3.4, hexose oxidase 1.1.3.5, cholesterol oxidase 1.1.3.6, aryl alcohol oxidase 1.1.3.7, L-gluconolactone oxidase 1.1.3.8, galactose oxidase 1.1.3.9, pyranose Oxidase 1.1.4.10, L-sorbose oxidase 1.1.3.11, alcohol oxidase 1.1.3.12, choline oxidase 1.1.3.17, secondary alcohol oxidase 1.1.3.18, glycerin-3-phosphate oxidase 1.1.3.21, xanthine oxidase 1.1.3.22, thiamine oxidase 1.1.3.23, L-galactonolactone oxidase 1.1.3.24, cellobiose oxidase 1.1.3.25, hydroxyphytanate oxidase 1.1.3.27, N-acetylhexosamine oxidase 1.1.3.29, polyvinyl alcohol oxidase 1.1.3.30 and methanol oxidase 1.1.3.31 and particularly preferred
GOD, galactose oxidase, alcohol oxidase and cellobiose oxidase.

The corresponding substrates in particular are suitable for generating peroxide Enzyme substrates, e.g. B. glucose / GOD, galactose / galactose oxidase, ethanol / alcohol oxidase and cellobiose / cellobiose oxidase is preferred.

The substrate glucose (e.g. for the GOD) can optionally by amyloglucosidase and Starch or glucose syrup or the like can be made available.

As enzymatically superoxide (O ₂ ^-.) Generating component is preferable, the enzyme-component system (ECS) are used in PCT / DE 98/01689 (WO 98/59108) with described system, now as "hydrolase mediated oxidation system → HOS -system ",
consisting of the following components:
System component 1 of the HOS system: one or more lipases, preferably from the group of triacylglycerol lipases (3.1.1.3) or one or more amidases, preferably from the group of amidases (3.5.1.4), which consists of one or more fatty acids (preferably are C ₆ to C ₂₆ , particularly preferably C ₈ to C ₁₆ fatty acids) (= system component 2 of the HOS system), and in the presence of oxidizing agents such as peroxides, preferably H ₂ O ₂ (= system component 3 of the HOS system) About the formation of peracids from ketones present as a further component (= system component 4 of the HOS system) reactive oxygen species z. B. can produce dioxiranes.

When adding suitable one or more hydroxylated benzenes (phenols, hydroquinones) (preferably 1.4 or 2.5), which are underivatized or can be derivatized with all possible groups, as well as aromatic hydroxycarboxylic acids, polyphenols such as lignins, Depside, flavonoids, of other heterocyclic aromatics or non-aromatics, of non-aromatic cyclic hydroxylated compounds from which phenoxy radicals and / or semiquinones can be formed by oxidation, superoxide radicals can be formed by reducing the oxygen present. Such phenolic compounds are:
As system component 1 (HOS system): lipases
According to the International Enzyme Nomenclature: Committee of the International Union of Biochemistry and Molecular Biology (Enzyme Nomenclature, Academic Press, Inc., 1992, pp. 306-337), Group 3 enzymes (hydrolases) 3.1, 3.1.1, 3.1 are preferred .2, 3.1.3, 3.1.4 and 3.1.7 used such. B .:
Carboxylester hydrolases (3.1.1), thiolester hydrolases (3.1.2), phosphorus monester hydrolases (phosphatases) (3.1.3), phosphoric acid diester hydrolases (3.1.4), diphosphoric acid monoester hydrolases (3.1.7).

Enzymes from group 3.1.1.3, lipases (triacylglycerol Lipases, triglycerol acyl hydrolases).

Other enzymes are those that can split carbon / nitrogen bonds (C / N) (other than peptide bonds), used (3.5), particularly preferred: enzymes of the class 3.5.5.1 nitrilases, class 3.5.1.4 amidases and class 3.5 acylases.

Likewise particularly preferred are class 3.4 enzymes which act hydrolytically on peptide bonds: here in particular class 3.4. 11-19, which comprise the exopeptidases and particularly preferably class 3.4. 21-24 and 3.4. 99, which comprise the endopeptidases and here in particular the class of the serine proteinases such as:
Chymotrypsin (3.4.2 1.1); Trypsin (3.4.21.4); Subtilisin (3.4.21.62);
Endopeptidase K (3.4.21.64);
the class of cysteine endopeptidases is also particularly preferred, such as:
Papain (3.4.22.2), ficaine (ficin) (3.4.22.3); Bromelaine (3.4.22.32/3.4.22.33), as well
the class of aspartic endopeptidases is particularly preferred, such as:
Pepsins (3.4.23.1/3.4.23.2); Renin (3.4.23.15), aspergillopepsins (3.4.23.18/3.4.23.19),
Penicillopepsin (3.4.23.20); Rhizopus pepsin (3.4.23.21); Endothiapepsin (3.4.23.22);
Mucorpepsin (3.4.23.23); Candidapepsin (3.4.23.24), saccharopepsin (3.4.23.25);
Rhodutorulapepsin (3.4.23.26); Physaropepsin (3.4.23.26); Acrocylindropepsin (3.4.23.28),
Polyporopepsin (3.4.23.29); Pycnoporopepsin (3.4.23.30); Scytalidopepsin A / B (3.4.23.3 1 / 3.4.23.32), xanthomonapepsin (3.4.23.33);
and also particularly preferably the class of metalloendopeptidases such as:
Microbial collagenase (3.4.24.3); Gelatinase A / B (3.4.24.24/3.4.24.35); Thermolysin (3.4.24.27); Bacillolysin (3.4.24.28); Deuterolysin (3.4.24.39);
As system component 2 (HOS system), fatty acids are preferably used as the peracid source, such as:
Saturated fatty acids, unsaturated fatty acids and polyunsaturated fatty acids.

Furthermore, esters are preferably used as the peracid source, fatty acid esters and other esters such as:
Esters of mineral acids and alcohols and / or phenols, of carboxylic acids and alcohols and / or phenols such as. B. particularly preferably also the oils and / or fats and here in particular the monofatty acid esters, the difatty acid esters and the trifatty acid esters or mixtures thereof, furthermore special lipase substrates such as triacetin, tributyrin, trioctanoin, tridecanoin etc.,
inner esters of hydroxycarboxylic acids (lactones), esters of orthocarboxylic acids, thiocarboxylic acid S-ester and thiocarboxylic acid O-ester and polyester etc.

Particularly preferred oils / fats are:
Anise oil, lemon balm oil, laurel oil, castor oil, cedarwood oil, clove oil, primrose oil, corn oil, cottonseed oil, coconut oil, jojola oil, lard oil, linseed oil, macadamia nut oil, mineral oil, olive oil, orange oil, safflower oil, sunflower oil, soybean oil, wheat oil oil, liver oil oil, petroleum seed oil, petroleum seed oil, petroleum seed oil, petroleum seed oil, petroleum seed oil, peanut oil other fish oils, butterfat, cocoa butter, palm oil, milk fat, vegetable fats in general, neutral oil, avocado oil, evening primrose oil, hazelnut oil, borage peel, almond oil, rapeseed oil etc.

The following are also particularly preferred as important esters:

• a) esters of aliphatic acids such as:
  Methyl formate, Ethyl formate, Methyl acetate, Ethyl acetate, Propyl acetate, Isopropyl acetate, Butyl acetate, Isobutyl acetate, Pentyl acetate, 2-Ethylhexyl acetate, Vinyl acetate; Ethylene glycol diacetate, methoxyethyl acetate, 2-ethoxyethyl acetate, 2-butoxyethyl acetate, 2 (2-ethoxyethoxy) ethyl acetate, benzyl acetate, glyceryl acetate, methyl propionate, ethyl propionate, glyceryl tripropionate, methyl butyrate ethyl butyrate, butyl butyrate, methyl isobutyrate, ethyl isobutyrate, isobutyl isobutyrate, dimethyl adipate, bis (2-ethylhexyl) adipate, methyl stearate, butyl stearate, dodecyl stearate, hexadecyl stearate methyl acrylate, ethyl acrylate, butyl acrylate, 2-ethylhexyl acrylate, methyl methacrylate;
• b) esters of aromatic acids such as:
  Methyl benzoate, ethyl benzoate, methyl salicylate, ethyl salicylate, phenyl salicylate, dimethyl phthalate, diethyl phthalate, bis (2-ethylhexyl) phthalate, dimethyl isophthalate, dimethyl terephthalate, trimethyl trimellitate, methyl anthranilate, benzyl cinnamate.

Synthetic detergents (nonionic detergents), which can contain fatty acid residues such as:
Polyoxyethylene desorbitan esters such as preferred Tween types such. B .:
Tween 20, 21, 40, 60, 61, 65, 80, 81, 85 and polyoxyethylene bis (stearate)
and Span types such as Span 20, 40, 60, 65, 80, 85
and polyoxyethylene esters such as e.g. B. Myrj types like
Myrj 45, 52, 53, 59 etc.
or sorbitan esters such as:
Sorbitan monolaurates, monooleates, monostearates, sesquioleates, trioleates, tristearates etc.
or sucrose esters such as:
Sucrose palmitate-stearate 7, sucrose dipalmitate 11, sucrose palmitate-stearate 15
or polyoxyethylene ethers such. B. Brij types such as:
Brij 30, 35, 52, 56, 58, 72, 76, 78, 92, 97, 99, 700, 721 etc.
or polyoxyethylene ethers such as e.g. B. Triton types such as:
Triton X-100 (t-octylphenoxypolyethoxyethanol), X-15, X-35, X-45, X-102, X-114, X-155, X-165, X-207, X-305, X-405, X-705, N-42, N-57, N-60, N-101, B-1956, CG-110, XL-80N, CF-21, CF-32, CF-54, DF-12, DF- 16, WR-1339 (Tyloxapol)
or polyglycol ethers such as tergitol types such as:
Tergitol Type NP-4, NP-7, NP-9, NP-10, NP-35, NP-40, N-42, TMN-6, TMN-10, XD, XH, 15-S-5, 15- 5-7, 15-S-9, 15-S-12, 15-S-15, 15-S-30, Min Foam 1x, Min Foam 2x etc.

These substances can also be mixed with fats and / or fatty acids and / or esters are used only as a mixture or as solubilizers (emulsifiers) for these enzyme substrates.  

Detergents (surfactants / emulsifiers) may be used as solubilizers in the HOS system. used.

As groups of these connections:

• a) Nonionic surfactants
• b) Ionic surfactants:
  • 1. anionic surfactants
  • 2. cationic surfactants
• c) Amphoteric surfactants (zwitterionic) and
• d) Polymer connection surfactants

used.

Among the nonionic surfactants, particular preference is given to using compounds such as:
Fatty acid esters of alcohols, fatty acid esters of ethylene glycol, fatty acid esters of propylene glycol, fatty acid esters of glycerin (polyglycerol), fatty acid esters of sorbitol, fatty acid esters of pentaerythritol, fatty acid esters of glycerol esters, of acetic acid, lactic acid and citric acid, fatty acid esters of sucrose, fatty amides, fatty acid amides, fatty acid amides, fatty amides Polyamides
further esters such as:
Polyoxyethylene esters, polyoxyethylene ethers, polyglycol ethers, polyoxyethylene esorbitan esters, sorbitane esters, sucrose esters and further:
Alkylpolyethylene glycol ether, alkylphenol poly (ethylene glycol) ether, fatty alcohol polyglycol ether, ethylene oxide block polymers, propylene oxide block polymers, alkyldemethylamine oxides, lanolin (wool wax), beeswax, walnut, walnut substitute, lama cream HT (mixture of mono- and diglycerides of citric acid esters and edible fats) (Teg from stearic acid), methyl alcohol, emulsan (methyl glucose sequesterate), ceralan (polyglyceryl-3-beeswax), confonder (sucrose distearate), N, N-bis (3-D-gluconamidopropyl) cholamide (BIGCHAP), decanol-N- methylglucamide, n-decyl-α-D-glucopyranoside, n-decyl-β-D-glucopyranoside, n-decyl-β-D-maltopyranoside, deoxy- BIGCHAP, n-dodecyl-β-D-glucopyranoside, n-dodecyl- α-D-maltoside, n-dodecyl-β-D-maltoside, heptanoyl-N-methylglucamide, n-heptyl-β-D-glucopyranoside, N-heptyl-β-D-thioglucopyrenoside, n-hexyl-β-D- Glucopyranoside, Igepal CA-630, 1-monooleoyl-rac glycerol, nonanoyl-N-methylglucamide, n-nonyl-α-D-glucopranoside, n-nonyl -D- glucopranoside, octanoyl-N-methylglucamide, n-octyl-α-D-glucopyranoside, n-octyl-β-D-glucopyranoside, octyl-β-D-thiogalactopyranoside, octyl-β-D-thioglucopyranoside, n-tetradecyl -β-D-maltosides, n-undecyl-β-D-glucopyranosides.

Among the cationic surfactants, particular preference is given to using compounds such as:
Quaternary ammonium compounds, fatty amine salts, salts of alkylenediamines and polyamines, quaternary amidoamine compounds, alkylamine salts of ethers and esters, alkylpyridium salts, alkylimidazolium salts, alkyloxazolium salts, amine oxides such as in particular:
Alkyltrimethylammonium bromides, benzalkonium chlorides, benzethonium chlorides, bromides Benzyldimethyldodecylammonium, Benzyldiethylhexadecylammonium chlorides, benzyldimethyltetradecyl ammonium chloride, benzyltrimethylammonium methoxide, Cetyldimethylethylammonium bromides, cetylpyridinium, decamethonium bromide, dimethyldioctadecylammonium bromide, methylbenzethonium chloride, methyltrioctylammonium chloride, N, N ', N'-Polyoxyethylene (10) - N-tallow-1,3-diaminopropane, cetylpyridium chloride, cethyltrimethylammonium bromide;
Among the anionic surfactants, particular preference is given to using compounds such as soaps, alkylbenzenesulfonates, alkanesulfonates, α-olefin sulfonates, α-sulfo fatty acids, methyl esters, fatty alcohol sulfates, fatty acid sulfonates, fatty acid ester sulfonates, alkyl sulfates, fatty alcohol ether sulfates,
Oxo alcohol ether sulfates such as in particular:
Aerosol 22, Aerosol-OT, salts of alginic acid, salts of caprylic acid, salts of cholic acid, salts of pectic acid, 1-decanesulfonic acid, dehydrocholic acid, deoxycholic acid, dioctyl sulfosuccinate, 1-dodecanesulfonic acid, glycocholic acid, glycodeoxychanesulfonic acid, 1-heptonic acid, 1-heptonic acid N-lauryl sarcosine, lauryl sulfate (dodecyl sulfate), 1-nonanesulfonic acid, 1-octanesulfonic acid, 1-pentanesulfonic acid, taurocholic acid, taurodeoxycholic acid, ox gall, zonyl FSA, hyamine 1622, 2389, 3500, dimethylbenzenesulfonic acid, triisopropylnaphthalenesulfonic acid, GR-7M, QS-15, QS-30, QS-44, XQS-20, W-30, X-151, X-200, X-301;
Among the zwitterionic surfactants, particular preference is given to using compounds such as alkylbetaines, alkylsulfobetaines,
such as in particular:
CHAPS, CHAPSO; N-decyl-N, N-dimethyl-3-ammonio-1-propanesulfonate, N-dodecyl-N, N-dimethyl-3-ammonio-1-propanesulfonate, N-hexadecyl-N, N-dimethyl-3-ammonio-1- propanesulfonate, N-octadecyl-N, N-dimethyl-3-ammonio-1-propanesulfonate N-octyl-N, N-dimethyl-3-ammonio-1-propanesulfonate, phosphatidylcholine, N-tetradecyl-N, N-dimethyl-3 -ammonio-1-propanesulfonate;
Among the polymer compound surfactants, compounds such as:
Polyethylene glycols (PEG) and polypropylene glycols and their monomers:
Ethylene glycol, propylene glycol, polyacrylic acids, polyvinyl alcohols, polyethylenimines, polyethylenoxides, polydimethylsiloxanes, polyvinylpyrrolidones, generally polysaccharides such as: vegetable gums, xantans, pectins, starch and their derivatives, amylopectins, cellulose and their derivatives, glucans, mannans, arabanes, arabucins, alginines , Mannans and their derivatives and mixed polysaccharides, cyclodextrins, lignins, ligninsulfonic acids, proteins such as gelatin, etc.

As system component 3 (HOS system) (oxidizing agent: peroxides or per compounds), preference is given to compounds such as:
Peroxide (H ₂ O ₂ ), organic peroxides and per compounds, such as:
Perborates, persulphates, percarbonates, perphosphates, percarbamides, perchlorates etc. are used.

Compounds such as:
3-chloroperoxybenzoic acid, monoperoxyphthalic acid Mg salt, di-tert-butyl peroxide, cumene hydroperoxide, lauroyl peroxide, dicumyl peroxide, ethymethyl ketone peroxide, benzoyl peroxide, diperoxidodecanedioic acid Na salt and others.

Combinations of bleach activators also used in detergents can also be used such as TAED (tetraacetylethylenediamine), TAGU (tetraacetylglycoluril) and iso-NOBS (Sodium p-iso-nonanoyloxybenzenesulfonate) u. a. be used.  

System component 4 (HOS system) (ketones) are particularly preferred Carbonyl compounds of the general formula I used.

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 II) and 1,3-diketones (formula III) or polyketones (polyketides) and the tautomeric enols (formula IV) 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.

In addition to general carbonyl compounds, ketones such as general are particularly preferred Hydroxyketones, α, β-unsaturated ketones, oxicarboxylic acids, quinones and halogen ketones.

The following are particularly preferred:
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, methyl isityl oxyacetone, methyl isophenyloxy acetone, mesophenyl oxyacone, mesophenyl oxyacetone, mesophenyl oxyacone, mesophenyl ketone, methyl isophenyl ketone, meso-2 3-pentanedione, 2,3-hexanedione, phenylacetone, propiophenone, benzophenone, benzoin, benzil, 4,4'-dimethoxybenzil, 4'-methoxyacetophenone, 3'-methoxyacetophenone, O-ethylbenzoin, (2-methoxyphenyl) - acetone, (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-1-one, 2,6,6-trimethyl-2-cyclohexen-1,4-dione, 2-acetylbenzoic acid, 1-acetylnaphthalene, 2-acetylnaphthalene, 3'-aminoacetophenone, 4'-aminoacetophenone, 4'-cyclohexylaceto phenone, 3 ', 4'-diacetoxyacetophenone, diacetylbenzene, 2', 4'-dihydroxy '- dihydroxyacetophenone, 2', 6'-dihydroxyacetophenone, 3,4-dimethoxyacetophenone, 2'-hydroxyacetophenone, 4'-hydroxyacetophenone, 3'-methoxyacetophenone, 4'-methoxyacetophenone, 2'-methylacetophenone, 4'-methylacetophenone -Nitroacetophenone, 3'-nitroacetophenone, 4'-nitroacetophenone, 4'-phenylacetophenone, 3 ', 4', 5'-trimethoxyacetophenone, 4'-aminopropiophenone, benzoylacetone, benzoylpropionic acid, benzylidene acetophenone, Cyclohexylphenyl ketone, deoxybenzoin, 4 ', 4'-dimethoxybenzil, 1,3-diphenyl-1,3-propanedione, O-ethylbenzoin, ethyl benzoylacetate, ethyl (phenylglyoylate), 4'-hydroxypropiophenone, 1,3-indanedione, 1 -Indanon, isopropylphenyl ketone, 6-methoxy-1,2,3,4-tetrahydro-naphthalin-1-one, methyl-phenylglyoxylate, phenylglyoxylonitrile, 1-phenyl-1,2-propanedione-2-oxime, propiophenone, valerophenone, 2 -Acetyl-γ-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-indolylmethyl 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) - (-) - camphorquin on, (1S) - (+) - camphorquinone, 3,5-di-tert-butyl-o-benzoquinone, 1,2-dihydroxycyclobutene-3,4-dione, ethyl- (2-amino-4-thiazolyl) - glyoxylate, ethyl (phenylglyoxylate), ethyl pyruvate, 2,3-hexanedione, 3,4-hexanedione, 3-methyl-2-oxo-butyric acid, 3-methyl-2-oxovaleric acid, 4-methyl-2-oxo-valeric acid, Methylphenylglyoxylate, 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-butyryl acetate, ethyl-2-oxocyclohexane carboxylate, ethyl-2- phenylacetoacetate, methyl acetoacetate, 2-methyl-1,3-cyclohexanedione, 2-methyl-1,3-cyclopentanedione, methyl isobutyrylacetate, methyl 3-oxopentanoate, methylpivaloyl acetate, 3-oxoglutaric acid, tetrahydrofuran-2,4-dione, 2, 2,6,6-tetramethyl-3,5-heptanedione, 3-benzoylpropio Acid, 1,4-cyclohexanedione, dimethyl acetyl succinate, 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 malonate, diethyl butyl malonate, diethyl ethoxymethyl diethyl ethyl diethyl malate, diethyl ethoxymethyl Diethyl maleinate, diethyl malonate, diethyl methyl malonate, diethyl oxalate, diethyl 3-oxoglutarate, diethyl phenylmalonate, diethyl phthalate, diethyl pimelate, diethyl sebacate, diethyl suberate, diethyl succinate, diisobutyl phthalate, dimeth yl acetylene dicarboxylate, dimethyl 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, monoethyl fomate, 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, coumarin -Carboxylic acid, diethyl ethoxycarbonylmethanephosphonate, 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 almondate, ethyl 2-methyl lactate, ethyl 4-nitrocinnamate, ethyl oxamate, ethyl 2-ethyl 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, Bernst , 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, diethylacetamidomalonate, 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, ε-caprolactone, dihydrocoumarin, 4-hydroxycoumarin, 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-fluorenylmethyl succinimidyl 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 -dioxide, 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 diimidazole, N, N-dimethyl urea, N-ethyl urea, N Formyl urea, urea, n-methyl urea, N-phenyl urea, 4-phenylsemicarbazide, tetramethyl urea, 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, naphthalenic anhydride, naphthalenic anhydride , 2ndphenylbutyric anhydride, pivalic anhydride, propionic anhydride, cis-1,2,3,6-tetrahydrophthalic anhydride, valeric anhydride.

Benzophenones such as:
benzophenone; 4-aminobenzophenone, 2-amino-5-chlorobenzophenone, benzophenone-2-carboxylic acid, (S) - (-) - 2- (N-benzopropyl) -aminobenzophenone, 4,4'-bis (dimethylamino) - benzophenone, 4 , 4'-bis (diethylamino) benzophenone, 3,4-dimethoxybenzophenone, 4,4'-dihydroxybenzophenone, 2,4-dihydroxybenzophenone, 4-hydroxybenzophenone, 2-hydroxy-4-methoxybenzophenone, 4-methoxybenzophenone, 4,4 '-Dimethoxybenzo-phenone, 2,2', 4,4'-tetrahydroxybenzophenone, 2-chlorobenzophenone.

In addition to the H ₂ O ₂ and superoxide-generating enzyme systems mentioned, other enzymes from class 1 (oxidoreductases) according to the International Enzyme Nomenclature: Committee of the International Union of Biochemistry and Molecular Biology (Enzyme Nomenclature, Academic Press, Inc., 1992) are also preferred , Pp. 24 to 154) for this purpose, particularly preferably enzymes of the classes:
Cellobiose :. quinone-1-oxidoreductase 1.1.5.1, bilirubin oxidase 1.3.3.5, cytochrome oxidase 1.9.3, oxigenases, lipoxygenases, cytochrome P 450 enzymes, 1.13, 1.14, superoxide dismutase 1.15.11, ferrioxidase, e.g. B. ceruloplasmin 1.16.3.1 and particularly preferably class 1.10 enzymes which act on biphenols and related compounds. They catalyze the oxidation of biphenols and ascorbates. NAD ⁺ , NADP ⁺ (1.10.1), cytochrome (1.10.2), oxygen (1.10.3) or others (1.10.99) act as acceptors. Of these in turn, class 1.10.3 enzymes with oxygen (O ₂ ) as the acceptor are particularly preferred.

Of the enzymes in this class, the enzymes in particular are 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) preferred, the laccases (benzenediol: Oxigen Oxidoreductase) (1.10.3.2.) Are particularly preferred.

Enzymes from group 1.11., Which correspond to a Peroxide act as an acceptor. This only subclass (1.11.1) contains the Peroxidases. The cytochrome C are very particularly preferred here Peroxidases (1.11.1.5), Catalase (1.11.1.6), the peroxidase (1.11.1.7) 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 (1.11.1.13) and the diarylpropane peroxidase (ligninase, lignin peroxidase) (1.11.1.14).

SYSTEM COMPONENT B I: generation of peroxynitrite etc.

System component (B) of the oxidation and / or bleaching systems according to the invention consists of a special precursor component which is either formed enzymatically or an oxidizable or reactive compound with respect to system component (A), the special precursor component in (B) consisting of:

• A) there are special compounds which can release enzymatically or in situ NO, NO ⁺ or NO ^- which form with (A) reactive nitrogen species (RNS) such as B. peroxynitrite or the corresponding much more active acid form.

It is known from the literature that peroxynitrite can be formed from NO + superoxide, NO ⁺ + H ₂ O ₂ and from NO ^- + O ₂ .

Peroxynitrite is relatively stable in alkaline at pH values <11, while (pK _a value: 6.8), depending on the pH value, increasingly forms the protonated acid, which has a very high oxidation potential (2.1V), but also in Dependence on pH only has a half-life of seconds, whereby radicals are formed when oxidizable substances are present; Thiols and many other biomolecules are oxidized or the decomposition into nitrate or nitric acid predominates.

The acid, which can be present in the activated transconfiguration, reacts very quickly with metal complexes with heterolic decomposition (NO ₂ ⁺ and OH ^- ), which implies a strong nitriding ability, which is mostly undesirable.

The following substances are preferred as precursor substances for generating NO, NO ⁺ or NO ^- for reaction with component (A) → reactive oxygen species (ROS) for the production of peroxynitrite:
O-nitro and O-nitroso compounds such as:
organic nitrates such as:
Glycerol trinitrate, isosorbide-5-mononitrate, isobutyl nitrate, isopentyl nitrate, ethyl nitrite; Isobutyl nitrite, amyl nitrite (isopentyl nitrite),
S-nitro and S-nitroso compounds such as thionitrates and thionitrites (S-nitrosothiols) such as:
S-nitroso-N-acetyl-D, L-penicillamine, S-nitrosoglutathione, N-acetyl-S-nitrosopenicillaminyl-S-nitrosopenicillamine, S-nitrosocysteine,
N-nitroso compounds such as:
N-hydroxy-N-nitrosamines; N-nitrosamides, nitrosoguanidines, N-nitrosohydrazines and N-nitrosimines such as:
N-nitrosodimethylamine, N-methyl-N-nitrosourea, 1-methyl-3-nitrosoguanidine, streptozocin, N-nitroso-N-phenylhydroxylamine (copper ron).

Diazenium diolates (NONOates) such as:
Sper / NO, DEA / NO, DETA / NO (NOC-18), MAMA / NO (NOC-19), PAPA / NO (NOC-15), NOC-5, NOC-7, NOC-12, CNO-4 and CNO-5.

Likewise preferred are C-nitro and nitroso compounds such as:
4-nitrophenol, 3-nitropropionic acid, 2-methyl-2-nitrosopropane, phenyl-Nt-butyl nitrone.

Oximes such as:
NOR-3 and NOR-4 and heterocyclic NO donors like Sydnonimine like:
Molsidomine, 3-morpholinosydnonimine, N-morpholino-N-nitrosaminoacetonitrile / γ-cyclodextrin complex.

Oxadiazoles (furoxanes), oxatriazoles and oxatriazolimines such as:
4-phenyl-3-furoxane carbonitrile, GEA 3162, GEA 5024, GEA 5583 and
Nitroxyl-generating compounds such as:
Benzosulfohydroxamic acid (Piloty's acid), sodium trioxotrinitrate (Angeli's salt), sodium nitroxyl, diazetidine di-N-oxide, cyanamide, hydroxylamine, N-hydroxyguanidine, N-hydroxy-L-arginine.

Inorganic NO donors such as:
Sodium nitrite, nitrosysl hydrogen sulfate, peroxynitrite, nitrosyl tetrafluoroborate, nitrosyl chloride, and sodium azide.

Transition metal nitrosyls such as are also preferred
Sodium nitroprusside, dinitrosyl iron-cysteine complex, pentachloronitrosyl ruthenium nitrosyl complexes of iron / sulfur clusters, and pentacyanonitrosyl complexes of molybdate, manganate and tungstate.

The use of sodium nitrite and HNO ₃ to generate NO ₂ or the direct use of NO ₂ in the pretreating delignification and bleaching of pulp is known. This application is aimed at activating the pulp, protecting the cellulose (preventing the loss in strength of the pulp) and increasing the delignification in the subsequent bleaching steps, such as mainly the O ₂ delignification stage or the peroxide stage, which is a pretreatment.

This treatment is almost always used in combination with an O ₂ level.

Even an even stronger nitration than occurs in the pretreatment mentioned, with z. B. nitrosyl bisulfate, serves this pretreatment.

In no way was the combination of reactive oxygen species (ROS) and  reactive nitrogen species (RNS) to form peroxynitrite etc. or carried out so that the present inventive method does not affect in any way becomes.

It is also generally known that one of the usual chemical generations of peroxynitrite can take place via the reaction of nitrite (e.g. sodium nitrite) in acid with H ₂ O ₂ →
Formation of NO and especially NO ⁺

The procedure is to specify acidified peroxide, then nitrite and immediately With excess NaOH, the acid formed into the alkali stable anion → Peroxynitrite (see above) is transferred.

It has now surprisingly been proven that, in contrast to chemically generated peroxynitrite and its use, e.g. B. in the delignification of pulp under (A) I alkaline conditions (the peroxynitrite anion also has a relatively high oxidation power), ie the alkaline use in generation directly in the pulp, or (B) II when used directly in the pulp where sodium nitrite and H ₂ O _{2 are brought together} at pH 3 and the formation of peroxynitrite is somewhat slower than under "in situ"conditions; in a generation in which H ₂ O ₂ , e.g. B. with glucose oxidase (GOD) and glucose) is formed, ie continuously and slowly released in the presence of sodium nitrite and pH 4-4.5 (C) III a significantly higher delignification could be achieved and nitration / nitrosation could be almost completely prevented , Table 1 shows the corresponding results:

Table 1

This is, for the first time, completely surprisingly proven that the active protonated form of peroxynitrite or other reactive nitrogen species (RNS) from NO, NO ⁺ and continuous formation of reactants such as e.g. B. H ₂ O ₂ are able to break down lignin with very good performance.

It was also found completely surprisingly that if the HOS system described above (without ketones) + suitable hydroquinones or phenols such as, in particular, 1,4-dihydroxyphenols or 2.5 dihydroxyphenols (→ probable formation of superoxide) and suitable peroxynitrite precursors- Connections such as B. sodium nitrite (NO, NO ⁺ - formation) gives an even better delignification can be achieved.

Table 2 shows the results.  

Table 2

It was also found completely surprisingly that when combining NO, NO ⁺ or NO ^- generating enzyme systems such as catalase / H ₂ O ₂ / sodium azide or catalase / H ₂ O ₂ / hydroxylamine (or instead of catalase peroxidase) - where Na- azide and hydroxylamine are strong inhibitors for both enzymes - with component (A) z. B. GOD / glucose or HOS (without ketone) + hydroquinone and / or phenol, ie with simultaneous continuous release of (ROS) = peroxide or superoxide, a good lignin degradation performance can also be achieved.

The delignification values here are in the range of 22-25%.

An enzyme system known in the literature as a superoxide generating system:
Xanthine oxidase + xanthine or acetaldehyde in combination with SNAP = S-nitroso-N-acetylpenicillamine brought only a slight delignification, even at high concentrations of the components.

In addition, xanthine oxidase is far too expensive for large-scale use.  

In general, in addition to the enzymes mentioned:
Hydrolases, especially lipases in the HOS system,
Catalases and peroxidases as releasing enzymes for NO, NO ⁺ or NO ^- from the above-mentioned precursory compounds also preferably other enzymes from class 1 (oxidoreductases) according to the International Enzyme Nomenclature: Committee of the International Union of Biochemistry and Molecular Biology (Enzyme Nomenclature, Academic Press, Inc., 1992, pp. 24 to 154) applied such as:
Cellobiose: quinone-1-oxidoreductase 1.1.5.1, bilirubin oxidase 1.3.3.5, cytochrome oxidase 1.9.3, oxigenases, lipoxygenases, cytochrome P 450 enzymes, 1.13, 1.14, superoxide dismutase 1.15.11, ferrioxidase, e.g. B. Ceruloplasmin 1.16.3.1
and particularly preferably class 1.10 enzymes which act on biphenols and related compounds. They catalyze the oxidation of biphenols and ascorbates. NAD ⁺ , NADP ⁺ (1.10.1), cytochrome (1.10.2), oxygen (1.10.3) or others (1.10.99) act as acceptors. Of these in turn, class 1.10.3 enzymes with oxygen (O ₂ ) as the acceptor are particularly preferred.

Of the enzymes in this class, the enzymes in particular are 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) preferred, the laccases (benzenediol: Oxigen Oxidoreductase) (1.10.3.2.) Are particularly preferred.

Enzymes from group 1.11., Which correspond to a Peroxide act as an acceptor. This only subclass (1.11.1) contains the Peroxidases. The cytochrome C peroxidases are very particularly preferred here (1.11.1.5), 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 (1.11.1.13) and the diarylpropane peroxidase (ligninase, Lignin peroxidase) (1.11.1.14).

system Activation of reactive oxygen species (ROS) provided by system component (A), here mainly → H ₂ O ₂ by (B) / II dicyclopentadienyl transition metal complexes

Dicyclopentadienyl complexes of metals → metallocenes and in particular Dicyclopentadienyl complexes of iron → Ferrocenes are in the literature as catalysts described for a variety of reactions with increasing interest in the last few Years. In addition to the originally used sandwich complexes, there are also more and more Half-sandwich complexes and multi-sandwich complexes are used.

There are no references for the present applications according to the invention.

However, it is known from the literature that other transition metal complexes e.g. B. such of iron, manganese, copper, molybdenum, vanadium, tungsten etc., however, completely various ligands such as heme, phenanthroline, pyridine, siderophores etc. can be used also together with peroxide around z. B. bleach in detergents or pulp delignification and / or bleach. Most of the time, even after activation of the peroxide formed metal peroxo complexes the actual oxidant.

Although the oxidative destruction of the complex cannot be ruled out under certain conditions for ferrocene and some derivatives, and transition metal impurities (especially Fe ²⁺ ) in the commercially available compounds are not unlikely, Fenton chemistry could not proceed from this on reaction with peroxide be excluded.

These Fenton reactions or the peroxo complexes that are present in too high a concentration previously led z. B. always significant in the treatment of pulp Loss of strength (usually measured by the high loss of cellulose viscosity), what these methods besides the mostly considerable costs for these complexes for you Make industrial use unusable.

The task of avoiding these disadvantages was solved by the fact that ferrocene in particular or certain ferrocene complexes together with component (A) of the invention Oxidation and / or bleaching processes, d. H. GOD + slow and slow glucose continuous generation of peroxide e.g. B. in the delignification and / or bleaching of Pulp were used.

It has surprisingly been found that significant delignification in at the same time very good preservation of the strength occurred.

Furthermore, it was surprisingly found that mediators of the NO, NOH or HRNOH type, normally used in the well-known laccase mediator system  find, could be oxidized what z. T. by color changes, which also the formation of NO Show radicals, can be optically tracked. The corresponding delignification was even better with better maintenance of strength. This fact make this system additionally also more interesting commercially, since no laccase is required (the corresponding mediator connections are listed in Appendix I).

This result is all the more surprising since the oxidation potentials of those used Connections are in the range of 0.4 to 0.6 V and would therefore not be able to to oxidize the mediators mentioned. As already mentioned above, the peroxo- Probably complexes the active oxidant.

Furthermore, it was surprisingly found that the addition of small amounts of sulfite, sulfate or persulfate led to a significantly improved performance (comparable to that of the mediators mentioned above) while maintaining the strength. A generation of sulfite, sulfate or persulfate radicals is also suspected here. Since, as already mentioned above, the applications of ferrocene + H ₂ O ₂ according to the invention are unknown and, surprisingly, e.g. B. with pulp delignification and / or bleaching at an optimized temperature (= max. 60 ° C), pH <pH 4, consistency and residence time a good performance with relatively good strength is possible, in this case also without component (A) be worked.

As dicyclopentadienyl complexes of transition metals, all those in the standard work should: Gmelin's Handbook of Inorganic Chemistry Part 1-14: Iron-organic compounds, Springer Verlag, 1974 etc. listed ferrocene compounds and derivatives become.

Likewise, in the standard work:
Ferrocenes (Homogeneous Catalysis, Organic Synthesis, Materials Science), VCH, 1995 listed ferrocenes, their descendants and mixed metallocenes,
like those in the standard work:
Metallocenes I and II, Wiley-VCH, 1998 compounds are used.

In particular and preferably, the following should be used:
Ferrocene, cyclopentadienyl iron dicarbonyl dimer, 1,1'-ferrocene dicarboxylic acid, 1,1'-bis (diphenylphosphino) ferrocene, a-methyl-ferrocenyl-methanol, benzoylferrocene, ferrocenium tetrafluoroborate, 1,2-diferrocenylethane, decamethylferrocene, 1,1 ' -Dimethylferrocene, ferrocene aldehyde, ferrocenium hexalluorophosphate, butyrylferrocene, (dimethylaminomethyl) ferrocene, ferroceneacetonitrile, ferrocene boronic acid, trans-4 (2- (1-ferrocenyl) vinyl) -1-methylpyridium iodide.

Metallocenes such as:
Methylcyclopentadienylmolybdenum tricarbonyl dimer, bis-cyclopentadienyl-cobalt, zirconocene chloride hydride, bis-cyclopentadienyl-vanadium, cyclopentadienyl tungsten tricarbonyl dimer, bis (cyclopentadienyl) nickel, (methylcyclopentadienyl) manganese tricarbonylyl, magentene tricarbonylyl, magentene tricarbonylyl, magentene tricarbonylyl, magnesia trenocarbonyl, magnes ,

system Reactive oxygen species (ROS) provided here by system component (A), here above all → H ₂ O ₂ , can be reacted with component (B) / (III), which consists of special organosulfonic acids or activated sulfite, and added ketones, e.g. B. Dioxiranes are generated

It is known that certain organosulfonic and sulfonimidic acids react by reaction with peroxide in the slightly alkaline range perorganosulfonic acids or sulfonimidine peracids can form. When adding ketones z. B. acetone can the corresponding dioxiranes be formed.

The corresponding active precursor substances are sulfonyl azoles and the most active ones Connections z. E.g. N-p-toluenesulfonylimidazole, toluenesufonamide, 1. (2- Mesitylenesulfonyl) -3-nitro-1,2,4-triazole, 1- (P-tosyl) -3,4,4-trimethylimidazolidine, and 1- (2-mesitylenesulfonyl) -1H-1,2,4-triazole.

The connections are e.g. T. relatively expensive and after reaction to the corresponding sulfonic acid inactive and not recyclable.

Therefore, they are not suitable for large-scale use.

There is also no application in the literature corresponding to the present one Oxidation and / or bleaching processes according to the invention.

The task at hand is to provide a more affordable and feasible alternative was solved by reacting component (A) enzymatically GOD and glucose was provided continuously and slowly, which is peroxide with the corresponding precursors in component (B), the corresponding organosulfone  acids, continuously z. B. forms perorganosulfonic acids, which with added ketones can continuously form dioxiranes.

This is a requirement that only small amounts of substance have to be added, an economical use in z. B. the area: pulp delignification and / or However, bleaching is only possible in other large-scale applications (see above).

It has now been found, completely surprisingly, that with continuous supply of H ₂ O ₂ by means of, for. B. GOD / glucose to the organosulfonic acids + addition of ketones, even with a very small amount of sulfonic acid (<2 kg per ton), a very good delignification performance with very good strength properties could be obtained. The main advantage for the pulp industry is that there are no large amounts of acetone (up to 50 kg per ton and more) and peroxosulfuric acid (up to 25 kg / ton and more), which are mostly formed in situ using concentrated sulfuric acid and peroxide must be applied in order to obtain significant delignification by the dioxirane formed. This is also attacked by persulfuric acid and can be destroyed.

The following organosulfonic acids are preferably used:
Phthalatesulfathiazole, cyclohaxanesulfamic acid sodium salt, 2-indanyl-p-toluenesulfonate, sulfathiazole sodium salt, 6-ethoxy-2-benzothiazolesulfonamide, 2-nitrobenzenesulfonamide, 4-toluenesulfonyl- (4-nitroanilide), sulfisomidyl, p- Sulfaguanidine, saccharin, acesulfame K, sulfamic acid, Np-toluenesulfonylimidazole, N- (2-nitrophenylthio) saccharin, diazald, sulfamethazine, sulfisoxazole, sulfacetamide, sulfamethoxazole, (-) - N- (phenylsulfonyl) glutamic acid, N'-sulfane Salt, benzenesulfonic acid amide, 4- (phenylsulfonyl) -2-azetidinone, sulfadiazine, sulfamethazine, 1,1'-sulfonyldiimidazole, sulfaphenazole, 4-acetamidobenzenesulfonic acid, N-cyclohexyl-P-toluenesufonamide, ethyl O-mesitylsulfonyxes (2-acetohydroxylamate) ) -3- nitro-1,2,4-triazole, 1- (P-tosyl) -3,4,4-trimethylimidazolidine, 8- (tosylamino) quinolines, 1- (phenylsulfonyl) 1H-benzotriazole, hydroxybenzenesulfonamide, Ammonium sulfamate, N1-acetylsulfonamide sodium salt, 2,4,6-trimethylbenzenesulfonyl hydrazide, 1- (2-mesitylenesulfonyl) -1H-1,2,4-triazole, 1-tosylimidazole, sulfur trioxide, pyridine complex, methanesulfonic anhydride, taurine, 1,4-butanesultone.

It is known from the literature that SO ₅ ^2- ions, i.e. peroxomonosulfuric acid anions (anions), can be generated in alkaline under Cu ²⁺ catalysis and excess O ₂ and slow addition of sulfite, which is activated by the copper Caro's acid), which, for. B. as delignification and / or bleaching agents in the cellulose bleaching Ver use. Generation via this route would save the dangerous and expensive formation of the anion via - as already mentioned above - peroxide and sulfuric acid or the even more expensive addition of the triple salt oxone.

It has so far only been possible to obtain relatively small amounts of SO ₅ ^2- using the method described (excess O ₂ , alkaline pH, Cu catalysis, slow metering in of sulfite) by means of vigorous stirring.

The object of providing a much better method for generating SO ₅ ^2- was achieved by continuously providing superoxide using system component (A) which was activated with the sulfite (SO.) Activated by the enzyme action of system component (B) ₃ ^2-. ) SO ₅ ^2- Generate ions that can form dioxirane with added ketone.

It has now been found, completely surprisingly, that by means of the HOS system (without ketone) + hydroquinone addition or phenol addition, superoxide is (probably) generated continuously (system component (A)) and by means of suitable enzymes such as e.g. B. Peroxidase or laccase + sulfite (system component (B)) (probably) activated sulfite (SO ₃ ^2-. ) Is generated, which can react after reaction to SO ₅ ^2- ions and by existing ketone to dioxirane.

It has also been found completely surprising that delignification and / or bleaching of pulp in comparison with the performance with normal HOS system (without ketone) HOS system (without ketone) + hydroquinone or phenol + sulfite and addition of peroxidase (HRP) and compared to systems where one component has been omitted complete system had a much better performance.

The enzymes used for the activation of sulfite are preferably those from class 1 (oxidoreductases) according to the International Enzyme Nomenclature: Committee of the International Union of Biochemistry and Molecular Biology (Enzyme Nomenclature, Academic Press, Inc., 1992, p. 24 to 154) as preferred:
Cellobiose: quinone-1-oxidoreductase 1.1.5.1, bilirubin oxidase 1.3.3.5, cytochrome oxidase 1.9.3, oxigenases, lipoxygenases, cytochrome P 450 enzymes, 1.13, 1.14, superoxide dismutase 1.15.11, ferrioxidase, e.g. B. ceruloplasmin 1.16.3.1 and particularly preferably class 1.10 enzymes which act on biphenols and related compounds. They catalyze the oxidation of biphenols and ascorbates. NAD ⁺ , NADP ⁺ (1.10.1), cytochrome (1.10.2), oxygen (1.10.3) or others (1.10.99) act as acceptors. Of these in turn, class 1.10.3 enzymes with oxygen (O ₂ ) as the acceptor are particularly preferred.

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) preferred, the laccases (benzene diol: oxigen oxidoreductase) (1.10.3.2.) are particularly preferred.

Enzymes from group 1.11., Which correspond to a Peroxide act as an acceptor. This only subclass (1.11.1) contains the Peroxidases. The cytochrome C are very particularly preferred here Peroxidases (1.11.1.5), Catalase (1.11.1.6), the peroxidase (1.11.1.7) 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 (1.11.1.13) and the diarylpropane peroxidase (ligninase, lignin peroxidase) (1.11.1.14).  

Description of the various uses of the enzymatic according to the invention Oxidation and bleaching systems

• A) use in pulp / wood pulp bleaching,
• B) Use:
  • a) in the treatment of pulp wastewater from the paper industry and
  • b) waste water from other branches of industry,
• C) Use in the production of lignin solutions or gels, from corresponding Binders / adhesives and 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 bleaching systems according to the invention in the Pulp / pulp bleaching

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 to remove 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 appropriate 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 a 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. Because they become radicals educated; 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.

There are 2 types of application forms:

• 1. Pretreatment of wood chips before refining or grinding to save energy in the manufacture of wood materials (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".

Improved kappa reduction after cooking are also compared as advantages 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 uneconomical 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. A significant reduction in kappa numbers is only evident after this long treatment period and whiteness, which makes 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, in particular bleaching effluent for the same Decolorization and reduction of 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 confirmed to a limited extent on a large scale, so that this enzyme type is at best 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 reduction and oxi dationsmittel and phenolic compounds works 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 aroma "matched" in the oxidation potential ten used.

The limitation for large-scale use is applicable to all three processes with low consistency (up to a maximum of 4%) and with the last two registrations additionally the risk of "leaching out" of metals when using the chelate compounds, the V. a. in the case of downstream peroxide bleaching stages can lead to the destruction of the peroxide.

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, of which at least one with defined residues substi is acted upon.

All three applications concern "dye transfer inhibition" and the use of the respective Enhancer substances together with peroxidases as 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 lignin-containing materials!

WO 94/29510 and WO 96/18770 describe a method for enzymatic delignification, in which enzymes are used together with mediators. Compounds with the structure NO, NOH or HRNOH are generally disclosed as mediators. Of the mediators listed in WO 94/29510 and WO 96/18770, 1-hydroxy-1H-benzotriazole (HBT) provides the best results in delignification. However, BRT has several disadvantages:

• - It is only available at relatively high prices and not in sufficient quantities.
• - reacts under delignification conditions to 1H-benzotriazole and colored others Products.
• - This compound is relatively poorly degradable and can be found in larger quantities Represent environmental pollution.
• - 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 meet the stated requirements Do not have disadvantages or to a lesser extent.

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

IIa) The use of the enzymatic ogidation and bleaching systems according to the invention for the enzymatic treatment of special waste water (paper industrial waste water e.g. from groundwood or refiner systems), or IIb) 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 using refiners) as well as grinding waste water from wood grinding plants be used.

The water-soluble lignin compounds (polyphenol propane bodies) are mainly responsible for the high COD (chemical acid material requirement = high load with organic material) and can be used with conventional Technology cannot be removed. In the sewage 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 faults. The enzyme effect in this application is immediately through a rapid clouding of the be recognized waste water, 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 expense of 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 systems with a special combination of components an efficiency that is superior to the enzymatic systems described above can be achieved, d. H. the inventive methods are compared to the above mentioned systems with oxidoreductases (such as laccases) as oxidation catalysts represent significantly improved systems, the advantages of which are: 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.

Also 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, the contaminated partial streams are treated before mixing with other wastewater in order to achieve optimal To achieve efficiency.

Here too, it was surprisingly found that the use of the inventive Enzymatic oxidation systems work 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:
Alizarin, 5-amino-2-hydroxybenzoic acid, 3-aminophenol, pyrocatechol, 2,2-bis (4-hydroxyphenyl) propane, bis (4-hydroxyphenyl) methane, quinalizarin, 4-chloro-1-naphthol, Coniferyl alcohol, 2,4-diaminophenol dihydrochloride, 3,5-dichloro-4-hydroxyaniline, 1,4-dihydroxyanthraquinone, 2,2-dihydroxybiphenyl, 4,4-dihydroxybiphenyl, 2,3-dihydroxynaphthalene, 2,6-diisopropylphenol, 3, 5-dimethoxy-4-hydroxybenzhydrazine, 2,5-di-tert-butyl-hydroquinone, 2,6-di-tert-butyl-4-methylphenol, 4-hydroxybiphenyl, 2-hydroxydiphenyl-methane, 2- (2nd -Hydroxyphenyl) -benzothiazole, 5-indanol, 2-isopropoxyphenol, 4-isopropyl-3-methylphenol, 5-isopropyl-2-methylphenol, 4-isopropylphenol, lauryl gallate, 2-naphthol, 4-nonylphenol, 3- (pentadecyl) - phenol, 2-propylphenol, 4-propylphenol, purpurin, pyrogallol, 4- (1,1,3,3-tetra-methylbutyl) phenyl, 1,2,4-trihydroxybenzene, 2,4,6-trimethylphenol, 2, 3,5-trimethylphenol, 2,3,6-trimethylphenol, 3,4,5-trimethylphenol, 6,7-dihydroxy-4-methylcoumarin, 2- (2-hydroxyethoxy) benzaldehyde , 1-Naphthol, Nordihydroguaiaretsäure, octyl gallate, silibinin, 3,4,6-trihydroxybenzoic acid octyl ester, 2,4,6-tri-tert-butylphenol, 2,4-di-tert-butylphenol, 2,6-dichlorophenolindophenol , Ethoxyquin, 1-aminoanthraquinone, 2-amino-5-chlorobenzophenone, 4-aminodiphenyl-amine, 7-amino-4-hydroxy-2-naphthalenesulfonic acid, 2- (4-aminophenyl) -6-methylbenzothiazole, benzanthrone, trioctyl trimellitate, trans -Chalcon, bis (4-aminophenyl) amine sulfate, 2,2'-ethylidenebis (4,6-di-tert-butylphenol), 2,2-bis (2,6-dibromo) 4- (2-hydroxy-ethoxyphenyl) propane, bis (3,5-di-tert-butyl-4-hydroxyphenyl) methane, 2,2-bis (3,5-dichloro-4-hydroxyphenyl) -propane, Bismarck Brown Y, 1-bromonaphthalene, 4-butylaniline, 2-tert-butyl-5-methylphenol, 1-chloroanthraquinone, 2-chloroanthraquinone, triallyl-1,3,5-benzenetricarboxylate, 1,1-tris- (hydroxymethyl) propane trimethacrylate, pentaerythrityl triacrylate, 1,2,4-trivinylcyclohexane, trans, cis-cycloododeca-1,5,9-triene, pentaerythritol tetrabenzoate, 4,4'-methylenebis (2,6- di-tert .-Butylphenol), 4,4'-isopropylidene bis (2,6-dichlorophenol), 4,4'-isopropylidene bis (2,6-dibromophenol), 4,4'-isopropylidene bis (2- (2nd , 6-dibromo-phenoxy) ethanol, 2,2'-ethylidenebis-4,6-di-tert-butylphenol), 3-tert-butyl-4-hydroxy-5-methyl-phenyl, 5-tert-butyl-4 -hydroxy-2-methyl-phenyl, syringaldazine, 4,4'-dimethoxy-triphenylmethane, di-sec-butylphenol.

Substances which have several hydroxyl groups, such as:
Ellagic acid, gallic acid, galllein, gallangin, myo-inositol, morin, nitranilic acid, phenolphthalein, purpurin, purpurogallin, quinizarin, chrysazine, quercitin, quinhydron, chloranilic acid, carmine, rhodizonic acid, croconic acid, mellitic acid, hematoxilin, 9-phenyl-2,3-phenin 7-trihydroxy-6-fluorene, 9-methyl-2,3,7-trihydroxy-6-fluorene, tetrahydroxy-p-benzoquinone, 2,2'4,4'-tetrahydroxybenzophenone, pyrogallol red, 1-nitrophloroglucinol, 1, 4- dihydroxyanthraquinone, 5,8-dihydroxy-1,4-naphthoquinone, hexaoxocyclohexanoctahydrate, 5,7-dihydroxyflavanone, 3 ', 4'-dihydroxy-flavan 44871 00070 552 001000280000000200012000285914476000040 0002010126988 0000.5oxalis tris (2-hydroxyethyl) isocyanuric acid, quinalizarin, 2,4,5-trihydroxybenzamine.

III) Use of the enzymatic oxidation and bleaching systems according to the invention the production of lignin solutions or gels, of appropriate 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 preparation of these enzymes and that low yields even with genetically modified systems.

It has now been found, completely surprisingly, that the inventive ones are also here enzymatic oxidation systems superior performance to those in the prior art described enzymatic systems for the polymerization and / or modification of lignin and / or show lignin-containing materials.

The enzymatic oxidation systems according to the invention are treated 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 systems or in the case of an alkaline active optimum of the enzymatic oxidation systems the system and lignin and / or lignin-containing material can be put together immediately done without pretreatment. Pretreatment or treatment at alkaline pH The purpose of this is 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 enzymatic oxidation systems and lignin and / or Material containing lignin 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 e.g. B. at the Particle board production for "gluing" used urea-formaldehyde resins, which in addition to toxicological concerns, they are only partially resistant to moisture or Phenol formaldehyde resins that have an unfavorable swelling behavior and long pressing times (too again in addition 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 systems 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 inventive enzymatic oxidation and bleaching systems as enzymatic deinking system

Under Deinken, as is still practiced conventionally as flotation thinking today is basically a two-stage 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 fiber 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 level, 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 chemicals mentioned by blowing air into special flotation containers accepted. The color particles attach themselves to the foam bubbles and become with them carried 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 effect of the laccase of Shift Trametes versicolor, which is normally in the pH range of approx. PH 4-5, to 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 sodium hydroxide 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 enzyma according to the invention oxidation systems by appropriate selection of conditions the efficiency of the other enzymatic deinking systems v. a. with oxidoreductases and with lignin  Deinkstoff surpass and v. a. the advantage of 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 additives to increase polymerization can find a further improvement in ink separation.

V) Use of the inventive enzymatic oxidation and bleaching systems as Oxidation system in organic synthesis

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

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 connections via epoxying
• c) Production of arene oxides
• d) production of phenols
• e) Preparation 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 found, completely surprisingly, that with the help of the invention moderate enzymatic oxidation systems a variety of oxidation reactions from the can perform exemplary enumeration shown above.  

VI) Use of the inventive enzymatic oxidation and bleaching systems as 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 more 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 so far been available for detergent bleaching.

WO 1/05839 describes the use of various oxidizing enzymes (oxidases and Peroxidases) to prevent dye transfer. Peroxidases are better known able to measure different pigments (3-hydroxyflavone and betaine by 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 in situ generated hydrogen peroxide being involved in the catalysis of the dyeing. 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. Here, the formation of short-lived radicals or other oxidized states of the added substrate is postulated, which are responsible for the bleaching or other modification of the colored substance.

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, of which at least one with 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-compos nente bleaching systems for use with wash-active substances consisting of Oxidation catalysts and oxidizing agents as well as aliphatic, cycloaliphatic, heterocyclic or aromatic NO, NOH or H-NR-OH-containing compounds.

A disadvantage of all known "enzymatically enhanced" detergent bleaching systems is that the cleaning and bleaching effect is still unsatisfactory or the Mediator substances have to be added in large quantities and are therefore environmentally harmful and economic problems can arise.

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

VII) Use of the inventive enzymatic oxidation and bleaching systems 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, alkalis 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 carried out together with the konventio process of stone washing with pumice stones when treating denim Denim is 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 media gates 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 (Peroxi dasen, laccases) and enzyme-enhancing (hetero) aromatic compounds such as Nitroso compounds work, described.

However, as in the patents WO 94/12619, WO 94/12620 and WO 94/12621 only the insert 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 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 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 range or pulp pale 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 fabrics such as cotton, viscose, rayon, (rayon) ramie, Linen, Tencelm, silk or mixtures of these fabrics or mixtures of these fabrics with synthetic fibers such as. 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 for bleaching 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 be.
On the other hand, the system can be used together with cellulase in stone washing instead of the usual mechanical treatment using pumice stones, which is said to improve the performance of "cellulase-only treatment".

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

• - Laccase must be used in considerable quantities (approx. 10 IU / g denim) in order to achieve the desired result.
  • 1. The optimal treatment time is e.g. T. 2-3 hours.
  • 2. The preferred mediator (here phenothiazine-10-propionic acid) must be used in about 2 to about 14 mg per g of denim, which causes considerable costs.
  • 3. It has to 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.
  • 4. 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 enzyme effect-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 jeans denim 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 enzyme activity-enhancing compound used 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 is more gentle than bleaching with hypochlorite, which means 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 mainly consists of dyed fabrics (such as denim denim) have a great need for alternatives Bleaching process (for conventional hypochlorite bleaching) and / or treatment  process as an alternative to stone washing to achieve the so-called "bleached looks ", not least because of the environmental problems that also exist here.

The present invention has now 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 systems the performance of the oxidoreductase mediator systems mentioned above surpass and do not have the mentioned disadvantages of the prior art.  

A more detailed description of the inventive enzymatic oxidation and / or Bleaching systems related to the different applications I) Use in pulp bleaching

The effectiveness of the oxidation and bleaching systems 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 systems 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 processes for some pulps into one considerable 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 and thiover can be used as reducing agents bonds, mercapto compounds or glutathione etc. are used.  

In addition, radical formers or radical scavengers (trapping of, for example, OH ^. Or OOH ^. Radicals) can be added to the systems. These can improve the 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 nonionic, 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 systems according to the invention be, which increase the hydrophobicity of the reaction environment and thus swelling on the Lignin act in the fibers and thus increase 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 and others

The methods according to the invention can be used not only in the delignification (bleaching) of Sulfate, sulfite, organosolve, or the like Pulp and wood pulp are used, but also in the production of cellulose in general, be it from wood or annual plants, if defibrillation by the usual cooking methods (possibly connected with mecha process or printing), d. H. a very gentle cooking up to kappa numbers, which in the Range of approximately 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 systems according to the invention can be carried out once or repeated several times, either before and / or after washing and extracting the treated material with NaOH etc. or without these intermediate steps but also before and / or after pre-treatment and / or post-treatment steps such as acid wash, Q-steps, alkaline leaching, bleaching steps: such as peroxide bleaching, O ₂ -reinforced peroxide steps, pressure peroxide steps, O ₂ - delignification, Cl ₂ bleaching, ClO ₂ - Bleach, Cl ₂ / ClO ₂ bleach, 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 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 even further and to considerable whiteness increases. Likewise, an O ₂ stage can be used before the treatment with the oxidation and bleaching systems 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 peroxynitrite Enzymatic bleaching of Softwood O ₂ delignified (sulfate pulp)

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 3 kg / to nitrite, 6 kg / to glucose and 2.4 kg / to H ₂ O ₂ (30% product) with stirring, the pH is adjusted with sulfuric acid and / or sodium hydroxide solution, that after adding the pulp and the enzyme pH 4.5 results.
• B) 5 ml of tap water are mixed with 5 g / to substance GOD (crude / Asperg. Niger) added.

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

After the pulp has been added, it is mixed for 2 min with a dough kneader.

The substance is then placed in a reaction vessel preheated to 50 ° C. and under Normal pressure incubated for 1-4 hours.

Then the fabric is washed over a nylon sieve (30 µm) and 1.5 hours at 70 ° C, 2% consistency and 8% NaOH extracted per g of pulp.

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

A delignification of 33% could be achieved.

Example 2 Ferrocene / GOD / Glucose treatment Enzymatic bleaching of Softwood O ₂ delignified (sulfate pulp)

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 with 125 g / to ferrocene and 5 kg / to glucose with stirring added, the pH adjusted with sulfuric acid and / or sodium hydroxide so that after Addition of the pulp and the enzyme pH 4.2 results.
• B) 5 ml of tap water are mixed with 5 g / to GOD (crude / Asperg. Niger).

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

After the pulp has been added, it is mixed for 2 min with a dough kneader.

The substance is then placed in a reaction vessel preheated to 55 ° C. and under Normal pressure incubated for 1-4 hours.

The fabric is then washed over a nylon sieve (30 µm) and 1 hour at 60 ° C, 2% Density and 8% NaOH extracted per g of pulp.

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

The delignification was 34%.

Example 3 Ferrocene + H ₂ O ₂ Enzymatic bleaching of Softwood O ₂ delignified (sulfate pulp)

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

• A) 25 ml of tap water are mixed with 125 g / to ferrocene and 5 kg / to H ₂ O ₂ (30% product) with stirring, the pH is adjusted with sulfuric acid and / or sodium hydroxide so that after adding the pulp pH 4.2 results.

It is made up to 33 ml.

After the pulp has been added, it is mixed for 2 min with a dough kneader.

The substance is then placed in a reaction vessel preheated to 55 ° C. and under Normal pressure incubated for 1-4 hours.

The fabric is then washed over a nylon sieve (30 µm) and 1 hour at 60 ° C, 2% Density and 8% NaOH extracted per g of pulp.

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

The delignification was 28%.  

Example 4 Delignification with organosulfonic acids / GOD / glucose / acetone Enzymatic bleaching of Softwood O ₂ delignified (sulfate pulp)

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

• A) 20 ml tap water with 2 kg / to diazald, 5 kg / to glucose and 5 kg / to acetone added with stirring, the pH adjusted with sulfuric acid and / or sodium hydroxide solution, that after adding the pulp and the enzyme pH 7 results.
• B) 5 ml of tap water are mixed with 5 g / to GOD (crude / Asperg. Niger).

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

After the pulp has been added, it is mixed for 2 min with a dough kneader.

The substance is then placed in a reaction vessel preheated to 45 ° C. and under Normal pressure incubated for 1-4 hours.

The fabric is then washed over a nylon sieve (30 µm) and 1 hour at 60 ° C, 2% Density and 8% NaOH extracted per g of pulp.

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

The delignification was 32%.

Example 5 Treatment with activated sulfite / HOS system / HRP Enzymatic bleaching of Softwood O ₂ delignified (sulfate pulp)

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 stirring, 5 kg / to sulfite, 1.2 kg / to fatty acid Na oleate, 5 kg / to acetone and 1.2 kg / to H ₂ O ₂ (30% product), the pH adjusted with sulfuric acid and / or caustic soda so that pH 5 results after adding the pulp and the enzyme.
• B) 5 ml of tap water are mixed with 20 g / to lipase (crude / Asperg. Niger) and 5 g / to HRP added.

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

After the pulp has been added, it is mixed for 2 min with a dough kneader.

The substance is then placed in a reaction vessel preheated to 45 ° C. and under  Normal pressure incubated for 1-4 hours.

The fabric is then washed over a nylon sieve (30 µm) and 1 hour at 60 ° C, 2% Density and 8% NaOH extracted per g of pulp.

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

The delignification was 30%.

Addition of other factors to the inventive oxidation and bleaching systems

For all of the applications mentioned, the oxidation and bleaching systems according to the invention can be added to the components of the enzymatic oxidation systems with compounds which enhance enzyme activity, which are known from the applications DE 198 21 263.1 and DE 198 20 947.9 or PCT / DE 98/01313, comprising:

• a) at least one oxidation catalyst, particularly preferably enzymes such as oxidoreductases of classes 1.1.1. 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, pp. 24-154), particularly preferred:
  Cellobiose: oxigen-1-oxidoreductase (cellobiose oxidase) 1.1.3.25, cellobiose: quinone-1-oxidoreductase 1.1.5.1, bilirubin oxidase 1.3.3.5, cytochrome oxidase 1.9.3, oxigenases, lipoxigenases 1.13, 1.14, superoxide dismutase 1.15.11, ferrioxidase, z. B. ceruloplasmin 1.16.3.1, and particularly preferably class 1.10 enzymes which act on biphenols and related compounds. They catalyze the oxidation of biphenols and ascorbates. NAD ⁺ , NADP ⁺ (1.10.1), cytochrome (1.10.2), oxygen (1.10.3) or others (1.10.99) act as acceptors. Of these in turn, class 1.10.3 enzymes with oxygen (O ₂ ) as the acceptor are particularly preferred.
  Of the enzymes in this class are in particular the enzymes catechol oxidase (tyrosinase) (1.10.3.1), L-ascorbate oxidase (1.10.3.3) .O-aminophenol oxidase (1.10.3.4) and laccase (benzenediol: oxigen oxidoreductase) (1.10. 3.2) is preferred, the laccases (benzene diol: oxigen oxidoreductase) (1.10.3.2.) Being particularly preferred. The enzymes of group 1.11 are also particularly preferred. which act on a peroxide as an acceptor. This only subclass (1.11.1) contains the peroxidases. The cytochrome C peroxidases (1.11.1.5), catalase (1.11.1.6), the peroxidase (1.11.1.7), the iodide peroxidase (1.11.1.8) and the glutathione peroxidase (1.11.1.9) are very particularly preferred here. 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 (1.11.1.13), the diarylpropane peroxidase (ligninase , Lignin peroxidase) (1.11.1.14).
• b) at least one suitable oxidizing agent,
• c) at least one mediator selected from the group of hydroxylamines, hydroxylamine derivatives, hydroxamic acids, hydroxamic acid derivatives, aliphatic, cycloaliphatic, heterocyclic or aromatic compounds which contain at least one N-hydroxy, oxime, N-oxi, or N, N'- Contain dioxi function and / or at least one mediator from the group of amides such. B. hydrazides or 1,2,4-triazolidine-3,5-diones (urazoles) and / or at least one mediator from the group of imides such as. B. Hydantoins
  and / or at least one mediator from the group of oxocarbons.

These enzymatic oxidation systems according to the invention contain at least one oxidizing agent. Examples of oxidizing agents are air, oxygen, ozone, peroxide compounds such as H ₂ O ₂ , organic peroxides, peracids such as peracetic acid, performic acid, persulfuric acid, persalpic acid, metachloroperoxobenzoic acid, perchloric 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 ), dioxygenyl cation (O ₂ ⁺ ), singlet oxygen, ozonide (O ₃ ^- ), dioxirane, dioxitane or fremy radicals.

The following is an example of the enzymatic pulp bleaching the possible performance improvement for some types of pulp through the combination the inventive oxidation and bleaching systems and those described above enzymatic oxidation systems with compounds that enhance enzyme activity shown:

Example 6 Nitrite / HOS system / laccase Enzymatic bleaching of softwood (sulfate pulp)

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 5 kg / to nitrite, 1.2 kg / to H ₂ O ₂ (30% product), 1.2 kg / to Na-oleate and 1 kg / to violuric acid, the pH value with 0.5 mol / l H ₂ SO ₄ solution adjusted so that pH 4.5 results after addition of the cellulose and the enzyme.
• B) 5 ml of tap water are mixed with 5 g / to lipase (crude / Asperg. Niger), 5 g / to laccase (crude / Trametes) offset.

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

After the pulp has been added, it is mixed for 2 min with a dough kneader.

The substance is then placed in a reaction vessel preheated to 50 ° C. and under Normal pressure incubated for 1-4 hours.

The fabric is then washed over a nylon sieve (30 µm) and 1 hour at 60 ° C, 2% Density and 8% NaOH extracted per g of pulp.

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

The delignification was 43%.

Appendix I

Appendix I shows the compounds of the invention as an addition to the Mediators / (NO-, NOH- and HNR-OH compounds) and other compounds together with oxidoreductases be applied such. B .:  

Hydroxylamines. (Open-chain or cyclic, aliphatic or aromatic, heterocyclic) such as compounds, ie derivatives of 1-hydroxybenzotriazole and tautomeric benzotriazole-1-oxide, and their esters and salts, preferably the following compound:
1-Hydoxybenzotriazol.

Furthermore preferred compounds (cyclic N-hydroxy compounds) such as:
N-hydroxy-phthalimides and optionally substituted N-hydroxy-phthalimide derivatives,
N-hydroxymaleimides and optionally substituted N-hydroxymaleimide derivatives,
N-hydroxy-naphthalimide and optionally substituted N-hydroxy-naphthalimide derivatives,
N-hydroxysuccinimides and optionally substituted N-hydroxysuccinimide derivatives,
such as B .:
N-hydroxyphthalimide, N-hydroxy-benzene-1,2,4-tricarboximide,
N, N'-dihydroxy pyromellitic diimide,
N, N'-dihydroxy-benzophenone-3,3 ', 4,4'-tetracarbonsaurediimid,
N-hydroxymaleimide, pyridine-2,3-dicarboxylic acid N-hydroxyimide,
N-1-hydroxy succinimide, N-1-hydroxy tartarimide,
N-hydroxy-5-norbornene-2,3-dicarboximide,
exo-N-hydroxy-7-oxabicyclo [2.2.1] hept-5-ene-2,3-dicarboximide,
N-hydroxy-cis-cyclohexane-1,2-dicarboximide,
N-hydroxy-cis-4-cyclohexene-1,2-dicarboximide,
N-hydroxynaphthalimide sodium salt and
N-hydroxyglutarimide.

Oximes such as:
1-methylvioluric acid, 1,3 dimethylvioluric acid, thiovioluric acid, alloxan-4,5-dioxime.
Alloxan-5-oxime hydrate (violuric acid) and / or its esters or salts.

Compounds from the class of N-aryl-N-hydroxy amides are also preferred and compounds such as nitroxyl radicals / nitroxides.

Hydrazides, cyclic hydrazides, urazoles and phthalhydrazides, imides, cyclic imides, derivatives of hydantoin and oxocarbons such as:
Square acid, croconic acid and rhodizonic acid.

Claims (28)

1. Oxidation and / or bleaching systems consisting of:

• A) enzymatic peroxide or superoxide or other reactive oxygen species (ROS) generating component, which makes this (ROS) slowly and continuously available and
• B) a special precursor component that is either formed enzymatically or is an oxidizable or reactive compound with respect to (A), the special precursor component in (B) consisting of either:
  • 1. Special compounds exist which can release NO, NO ⁺ or NO ^- enzymatically or in situ, which form with (A) reactive nitrogen species (RNS) such as. B. peroxynitrites or the corresponding protonated acid form or:
  • 2. consists of dicyclopentadienyl transition metal complexes which can activate the peroxide provided by (A) or:
  • 3. consists of special organosulfonic acids or activated sulfite, which in connection with (A) and ketones z. B. can generate dioxiranes

2. Oxygen species-generating enzymatic component (A) according to claim 1, characterized in that the enzyme oxidases with O ₂ as acceptor of class 1.1.3 such as: malate oxidase 1.1.3.3, glucose oxidase (GOD) 1.1.3.4, hexose oxidase 1.1 .3.5, cholesterol oxidase 1.1.3.6, aryl alcohol oxidase 1.1.3.7, L-gluconolactone oxidase 1.1.3.8, galactose oxidase 1.1.3.9, pyranose oxidase 1.1.4.10, L-sorbose oxidase 1.1.3.11, alcohol oxidase 1.1.3.12 , Choline oxidase 1.1.3.17, secondary alcohol oxidase 1.1.3.18, glycerol-3-phosphate oxidase 1.1.3.21, xanthine oxidase 1.1.3.22, thiamine oxidase 1.1.3.23, L-galactonolactone oxidase 1.1.3.24, cellobiose oxidase 1.1.3.25, Hydroxyphytanate oxidase 1.1.3.27, N-acetylhexosamine oxidase 1.1.3.29, polyvinyl alcohol oxidase 1.1.3.30 and methanol oxidase 1.1.3.31. 3. oxygen species-generating enzymatic component (A) according to claim 1 and 2, characterized in that the enzyme system for the generation of peroxide GOD / glucose is.   4. oxygen species-generating enzymatic component (A) according to claim 1, characterized characterized as providing superoxide as a generating system the hydrolase (especially lipase) is mediated oxidation system (HOS system). 5. oxygen species-generating enzymatic component (A) according to claim 1 and 4, characterized in that the generating system provides superoxide, the HOS system, from fatty acids (saturated, unsaturated, polyunsaturated) or fats or other esters, consists of peroxide and ketones. 6. oxygen species-generating enzymatic component (A) according to claim 1, 4 and 5, characterized in that the generating system provides superoxide, the HOS system, as an additive for the formation of superoxide phenols and / or hydroquinones contains and no ketones. 7. The oxygen species-generating enzymatic component (A) according to claim 1 and 4, characterized in that the generating system provides superoxide, the HOS system, enzymes from class 3 (hydrolases) 3.1, 3.1.1, 3.1.2, 3.1.3, 3.1.4 and 3.1.7 contains such as:
Carboxylester hydrolases (3.1.1), thiolester hydrolases (3.1.2), phosphorus monester hydrolases (phosphatases) (3.1.3), phosphoric acid diester hydrolases (3.1.4), diphosphoric acid monoester hydrolases (3.1.7) and va 3.1.1.3, lipases (triacylglycerol lipases, triglycerol acyl hydrolases), 3.5.1.4 amidases, 3.5 acylases and 3.4 proteases. 8. Precurser component (B), which is either formed enzymatically or is an oxidizable or reactive in relation to (A) according to claim 1, characterized in that it consists of special compounds such as:
organic nitrates / nitrites, NONOates, C-nitoso compounds, oximes, sidnonimines and related compounds, oxadiazoles, sulfohydroxamic acids, hydroxylamines, inorganic NO donors such as Na azides, Na nitrites, nitrosyl hydrogen sulfates, etc., which are enzymatic or in situ NO, Can release NO ⁺ or NO ^- , which with component (A) reactive nitrogen species (RNS) form such. B. peroxynitrite or the corresponding protonated acid form. 9. Precurser component (B), which is either formed enzymatically or an oxidizable or in relation to (A) represents a reactive compound according to claim 1, characterized records that it consists of cyclopentadienyl transition metal complexes, which by Component (A) can activate provided peroxide. 10. Precurser component (B), which is either formed enzymatically or an oxidizable or in relation to (A) represents a reactive compound according to claims 1 and 9, characterized thereby records that the for the activation by the cyclopentadienyl transition metal Kom plexing provided by component (A) peroxide by GOD / glucose ready is provided. 11. Precurser component (B), which is either formed enzymatically or an oxidizable or with respect to (A) represents a reactive compound according to claims 1, 9 and 10, thereby characterized in that they act as cyclopentadienyl transition metal complexes or ferrocene Contains ferrocene derivatives. 12. Precurser component (B), which is either formed enzymatically or an oxidizable or with respect to (A) represents a reactive compound according to claims 1, 9, 10 and 11, thereby characterized in that they act as cyclopentadienyl transition metal complexes or ferrocene Ferrocene derivatives and additionally laccase mediators of NO-, NOH- or NRNOH- Type contains. 13. Precurser component (B), which is either formed enzymatically or an oxidizable or with respect to (A) is a reactive compound according to claim 1, 9 to 12, thereby characterized in that they act as cyclopentadienyl transition metal complexes or ferrocene Ferrocene derivatives and additionally contains sulfite, sulfate, or persulfate anions. 14. Precurser component (B), which is either formed enzymatically or an oxidizable or in relation to (A) represents a reactive compound according to claim 1, characterized records that it consists of special organosulfonic acids or activated sulfite, which in Connection with (A) and ketones e.g. B. can generate dioxiranes   15. Precurser component (B), which is either formed enzymatically or is an oxidizable or reactive in relation to (A) according to claim 1 and 14, characterized in that the special organosulfonic acids are compounds such as:
Phthalatesulfathiazole, cyclohaxanesulfamic acid sodium salt, 2-indanyl-p-toluenesulfonate, sulfathiazole sodium salt, 6-ethoxy-2-benzothiazolesulfonamide, 2-nitrobenzenesulfonamide, 4-toluenesulfonyl- (4-nitroanilide), sulfisomidyl, p- Sulfaguanidine, saccharin, acesulfame K, sulfamic acid, Np-toluenesulfonylimidazole, N- (2-nitrophenylthio) saccharin, diazald, sulfamethazine, sulfisoxazole, sulfacetamide, sulfamethoxazole, (-) - N- (phenylsulfonyl) - glutamic acid Na, Salt, benzenesulfonic acid amide, 4- (phenylsulfonyl) -2-azetidinone, sulfadiazine, sulfamethazine, 1,1'-sulfonyldiimidazole, sulfaphenazole, 4-acetami dobenzenesulfonic acid, N-cyclohexyl-P-toluenesufonamide, ethyl O-mesitylsulfonyxl (acetohydroxamethyl) 2-mesitylenesulfonyl) -3-nitro-1,2,4-triazole, 1- (P-tosyl) -3,4,4-trimethylimidazolidine, 8- (tosylamino) quinolines, 1- (phenylsulfonyl) 1H-benzotriazole , Hydroxybenzenesulfonamide, ammonium sulfamate, N1-acetylsulfonamide Na salt, 2,4,6-trimethylbenzenesulfonyl hydrazi d, 1- (2-mesitylenesulfonyl) -1H-1,2,4-triazole, 1-tosylimidazole, sulfur trioxide pyridine complex, methanesulfonic anhydride, taurine, 1,4-butanesultone. 16. Precurser component (B), which is either formed enzymatically or an oxidizable or in relation to (A) represents a reactive compound according to claim 1, characterized records that the activated sulfite, which in connection with (A) and ketones z. B. Dioxiranes can be activated by the reaction with peroxidase or laccase. 17. Precurser component (B), which is either formed enzymatically or an oxidizable or with respect to (A) represents a reactive compound according to claims 1 and 16, thereby characterized in that the sulfite activated by peroxidase or laccase in association with provided by (A) superoxide, can form peroxomonosulfate anions with Can generate ketones dioxiranes. 18. Precurser component (B), which is either formed enzymatically or an oxidizable or with respect to (A) represents a reactive compound according to claims 1, 16 and 17, thereby characterized in that the superoxide provided by (A), which with  activated sulfite peroxomonosulfate can form anions through the HOS system + phenols is formed. 19. Oxidation and bleaching systems according to claim 1, characterized in that enzymatic oxidation systems with compounds which enhance enzyme activity can be added as additional systems, comprising:

• a) at least one suitable oxidation catalyst
• b) at least one suitable oxidizing agent,
• c) at least one mediator selected from the group of hydroxylamines, hydroxylamine derivatives, hydroxamic acids, hydroxamic acid derivatives, aliphatic, cycloaliphatic, heterocyclic or aromatic compounds which contain at least one N-hydroxy, oxime, N-oxi, or N, N'- Contain dioxi function and / or at least one mediator from the group of amides such. B. hydrazides or 1,2,4-triazolidine-3,5-diones (urazoles) and / or at least one mediator from the group of imides such as. B. Hydantoins
  and / or at least one mediator from the group of oxocarbons.

20. Oxidation and bleaching systems according to claim 1 and 19, characterized in that enzymes such as oxidoreductases of classes 1.1.1. As oxidation catalysts. up to 1.97 are used, preferably:
Cellobiose: oxigen-1-oxidoreductase (Cellobiose oxidase) (1.1.3.25), Cellobiose: quinone-1-oxidoreductase (1.1.5.1), bilirubin oxidase (1.3.3.5), cytochrome oxidase (1.9.3), oxigenases, lipoxygenases (1.13, 1.14), superoxide dismutase (1.15.11), ferrioxidase, e.g. B. ceruloplasmin (1.16.3.1),
1.10, such as 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),
1.11., Such as cytochrome C peroxidase (1.11.1.5), catalase (1.11.1.6), peroxidase (1.11.1.7) iodide peroxidase (1.11.1.8), glutathione peroxidase (1.11.1.9), chloride peroxidase (1.11. 1.10), L-ascorbate peroxidase (1.11.1.11), phospholipid hydroperoxide glutathione peroxidase (1.11.1.12), manganese peroxidase (1.11.1.13), diarylpropane peroxidase (ligninase, lignin peroxidase) (1.11.1.14). 21. Oxidation and bleaching system according to claim 1, 19 and 20, characterized in that Enzymes such as laccases and / or peroxidases are preferably used as oxidation catalysts become. 22. Oxidation and bleaching systems according to claim 1, 19 to 21, characterized in that as additional oxidizing agents, preferably air, oxygen, ozone, peroxide compounds such as:
H ₂ O ₂ , organic peroxides, peracids such as peracetic acid, formic acid, persulfuric acid, persalpic acid, metachloroperoxidbenzoic acid, perchloric 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 ), dioxygenyl cation (O ₂ ⁺ ), singlet oxygen ozonide (O ₃ ^- ), dioxirane, dioxitane or fremy radical can be used. 23. Use of the oxidation and bleaching systems according to claim 1 to 22, 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 from 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 Normal pressure to a slight O ₂ overpressure (up to 2 bar) and the GOD concentration, the lipase, laccase and peroxidase concentration in the range of 2-50 g (crude) per ton of pulp, the fatty acids or fat in a range from 0.5 to 5 kg per ton of pulp, glucose in the range of 1-15 kg per ton of pulp, H ₂ O ₂ in the range of 0.2 to 15 kg per ton and phenols in the range of 0.2 to 5 kg / ton of pulp, ferrocene in Range from 0.1 to 2 kg, Organosu Ifonic acids in the range from 0.5 to 5 kg, sulfite in the range from 0.5 to 10 kg, sulfates, persulfates, NO, NOH and HRNOH compounds in the range from 0.5 to 5 kg, NO precursors in the range from 0.5 to 5 kg per Ton of pulp can be used. 24. Use of the oxidation and bleaching systems according to claim 1 to 23, in a process for delignification and / or change and / or bleaching  of wood pulp and annual plants and wood pulp and deinked material, wherein before and / or after the reaction of the enzyme component system, an acid wash or Q stage 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 to be led. 25. Use of the oxidation and bleaching systems according to claim 1 to 24, 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. 26. Use of the oxidation and bleaching systems according to claim 1 to 25, in a process for delignification and / or modification and / or bleaching of cellulose from wood and annual plants and wood pulp and deinked material, it being before or after every possible treatment of the cellulose one or more cooking processes, bleaching stages or other pre- and / or post-treatments can be used, 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 level, peracid level, peracid-supported O ₂ or peroxide level, ozone bleaching level, dioxirane level, polymetoxalate level, Cl 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. 27. Use of the oxidation and bleaching systems according to claim 1 to 26, in a process for Delignification and / or alteration and / or bleaching of wood pulp and annuals plants and wood pulps and deinked materials, it being carried out in several stages, whereby between each stage a wash or a wash and an extraction with lye or neither Laundry extraction is still taking place.   28. Use of the oxidation and bleaching systems according to claim 1 to 27, for use in pulp delignification bleach, the use in the treatment of v. a. wood 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 corresponding 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 laundry medium, for use in the baking / decolorization of textile fabrics and for use in the liquefaction of coal.