DE19612194A1 - Multi-component system for changing, breaking down or bleaching lignin, lignin-containing materials or similar substances as well as methods for their use - Google Patents

Abstract

This invention concerns a multicomponent system for changing, degrading or bleaching lignin, lignin-containing materials or similar substances and processes for its use, containing a) optionally, at least one oxidation catalyst and b) at least one suitable oxidant and c) at least one mediator, characterized by the fact that the mediator is selected from the oximes of general formula (I) or (II) and their salts, ethers, or esters, where the groups X are the same or different and are O, S, or NR<1>, where R<1> means hydrogen, a hydroxy, formyl, carbamoyl or sulfono radical, an ester or salt of the sulfono radical, sulfamoyl, nitro, amino, phenyl, aryl-C1-C5-alkyl, C1-C12-alkyl, C1-C5-alkoxy, C1-C10-carbonyl, carbonyl-C1-C6-alkyl, a phospho, phosphono, or phosphonooxy radical, an ester or salt of the phosphonooxy radical where carbamoyl, sulfamoyl, amino and phenyl radicals can be unsubstituted or substituted one or several times with radical R<2> and the aryl-C1-C5alkyl, C1-C12-alkyl, C1-C5-alkoxy, C1-C10-carbonyl, carbonyl-C1-C6-alkyl radicals can be saturated or unsaturated, branched or unbranched, and can be substituted one or several times with a radical R<2>, where the radicals R<2> are the same or different and means a hydroxy, formyl or carboxy radical, an ester or salt of the carboxy radical, a carbamoyl or sulfono radical, an ester or salt of the sulfono radical, a sulfamoyl, nitro, amino, phenyl, C1-C5-alkyl or C1-C5-alcoxy radical and the radicals R<3>-R<4> are the same of different and signify a halogen or carboxy radical, an ester or salt of the carboxy radical, or they have the meanings given for R<1>, R<3> and R<4> being optionally linked to a ring [-CR<7>R<8>]n, where n = 1, 2, 3, or 4, and R<5> and R<6> have the meanings given for R<1>, and R<7> and R<8> have the meanings given for R<3> and R<4>.

Description

The present invention relates to a multi-component system for changing, breaking down or bleaching lignin, lignin containing Materials or similar substances as well as processes for its Application.

Used mainly today for pulp production Processes include the sulfate and sulfite processes. With both methods, under boiling and under pressure, cell fabric created. The sulfate process works with the addition of NaOH and Na₂S, while in the sulfite process Ca (HSO₃) ₂ + SO₂ for Application comes.

The main goal of all procedures is the removal of the lignin from the used plant material, wood or Annual plants.

The lignin that is associated with cellulose and hemicellulose Main component of the plant material (stem or stem) must be removed, otherwise it is not possible non-yellowing and mechanically heavy-duty papers to manufacture.

The wood production processes work with stone grinders (Wood sanding) or with refiners (TMP), which remove the wood after ent speaking pretreatment (chemical, thermal or chemical defibrillate thermally) by grinding.

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

For some years now, the possibilities of using Enzymes for lignin degradation researched. The mechanism of action  Such lignolytic systems is only a few years ago was cleared up when it was possible to use suitable conditions and inductor additives for the white rot fungus Phanero chaete chrysosporium to get sufficient amounts of enzyme. The previously unknown lignin peroxidases and Manganese peroxidases discovered. Since Phanerochaete chrysosporium is very effective lignin degrader, one tried its enzymes to isolate and in purified form for lignin degradation use. However, this did not work because it turned out that the enzymes mainly cause repolymerization of the lignin and do not lead to its degradation.

The same applies to other lignolytic enzyme species such as Laccases that replace the lignin with the help of oxygen decompose oxidatively from hydrogen peroxide. It could be fixed poses that there are similar processes in all cases is coming. Radicals are formed, which are themselves react with each other and thus lead to polymerization.

Today there are only processes that work with in-vivo systems beit (mushroom systems). Main focus of optimization versu are so-called biopulping and biobleaching.

Biopulping is the treatment of wood chopping cut with living mushroom systems.

There are 2 types of application forms:

• 1. Pretreatment of wood chips before refining or mah len to save energy in the production of wood fabrics (e.g. TMP or ground wood).

Another advantage is the mostly existing improvement of the mechanical properties of the fabric, a disadvantage the worse final whiteness.

• 2. Pretreatment of wood chips (Softwood / Hardwood) cellulose boiling (power process, sulfite process).

The goal here is to reduce the amount of cooking chemicals that Improve cooking capacity and "extended cooking".

Improved kappa reduction is also an advantage after cooking compared to cooking without pretreatment lung reached.

The disadvantages of these methods are clearly the long treatment periods (several weeks) and especially the unresolved Risk of contamination during treatment if one is on the uneconomical sterilization of the wood chips ver want to breed.

Biobleaching also works with in-vivo systems. Of the cooked pulp (Softwood / Hardwood) is before bleaching inoculated with fungus and treated for days to weeks. Only after This long treatment time shows a significant one Lowering the Kappa number and increasing the whiteness of the process economical for an implementation in the usual Bleaching sequences.

Another mostly with immobilized mushroom systems led application is the treatment of pulp mill tion waste water, in particular bleaching waste water for their removal coloring and reduction of AOX (reduction of chlorinated Compounds in wastewater that bleach chlorine or chlorine dioxide cause levels).

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

These enzymes are said to be mainly used against the after the cooking pro the residual lignin partially covered, reprecipitated xylan act and by its degradation the accessibility of the lignin for those used in the subsequent bleaching sequences Increase bleaching chemicals (especially chlorine dioxide). The one in the laboratory proven savings of bleaching chemicals have been made in  Large scale confirmed only to a limited extent, so that you can this enzyme type can at best be classified as a bleaching additive.

Che is used as a cofactor in addition to the lignolytic enzymes lat substances (siderophores, such as ammonium oxalate) and biotensi de on.

In the application PCT / EP87 / 00635 there is a removal system of lignin from material containing lignin cellulose under the same early bleaching described with lignolytic enzyme made from white rot fungi with the addition of reduction and oxi dation agents and phenolic compounds as mediators is working.

In DE 40 08 893C2 in addition to the Red / Ox system "Mimic Substances "that the active center (prosthetic group) of Simulate lignolytic enzymes, added. So one could significant performance improvement can be achieved.

In the application PCT / EP92 / 01086 there are additional improvements a redox cascade with the help of oxidation potential "Matched" phenolic or non-phenolic aromatics used.

With all three methods, the limitation is large for one technical use the applicability with low material density ten (up to a maximum of 4%) and for the last two registrations the danger of "leaching" of metals when using the Chelate compounds, which with downstream peroxide bleaching stages can lead to the destruction of the peroxide.

Methods are known from WO / 12619, WO 94/12620 and WO 94/12621 knows in which the activity of peroxidase by means of so-called named enhancer substances are promoted.

The enhancer substances are described in WO 94/12619 on the basis of their Characterized half-life.  

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

According to WO 94/12620, enhancer substances are organic chemicals lien, which contain at least two aromatic rings, from de NEN at least one substituted with defined radicals is.

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 detergent area. Although in the description of the Registration for usability to treat lignin referenced, but own experiments with those in the registrations Substances specifically disclosed showed that they act as mediators to increase the bleaching effect of the peroxidases in the skin lignin-containing materials had no effect!

WO 94/29510 describes a method for enzymatic de lignification, in which enzymes are used together with mediators be set. Connections with are generally used as mediators of structure NO, NOH or HRNOH.

Of the mediators disclosed in WO 94/29510, 1-hydroxy-1H-benzotriazole (HBT) provides the best results in delignification. However, HBT has several disadvantages:
It is only available at high prices and not in sufficient quantities.

It reacts under delignification conditions 1H-benzotriazole. This connection is relatively poor degradation bar and can be a considerable environmental burden in large quantities represent.

To some extent, it causes damage to enzymes.  Its delignification rate is not too high.

The present invention relates to a multi-component system for changing, breaking down or bleaching lignin, lignin containing Containing materials or similar substances

• a. optionally at least one oxidation catalyst and
• b. at least one suitable oxidizing agent and
• c. at least one mediator, characterized in that the mediator is selected from the group of oximes of the general formula I or II

and their salts, ethers, or esters, where
X is the same or different and is O, S, or NR¹ where
R¹ is hydrogen, hydroxyl, formyl, carbamoyl, sulfono, ester or salt of sulfono, sulfamoyl, nitro, amino, phenyl, aryl-C₁-C₅-alkyl, C₁-C₁₂-alkyl, C₁ -C₅-alkoxy-, C₁-C₁₀-carbonyl, carbonyl-C₁-C₆-alkyl, phospho-, phosphono-, phosphonooxy, ester or salt of the phosphonooxy,
where carbamoyl, sulfamoyl, amino and phenyl radicals are unsubstituted or can be substituted one or more times with a radical R² and the aryl-C₁-C₅-alkyl, C₁-C₁₂-alkyl, C₁-C₅-alkoxy, C₁ -C₁₀-carbonyl, carbonyl-C₁-C₆-alkyl radicals can be saturated or unsaturated, branched or unbranched and can be substituted one or more times with a radical R², where
R² is the same or different and is hydroxyl, formyl, carboxy, ester or salt of carboxy, carbamoyl, sulfono ester or salt of sulfono, sulfamoyl, nitro, amino, phenyl, C₁-C₅-alkyl , C₁-C₅ alkoxy and
the radicals R³ and R⁴ are identical or different and are halogen, carboxy, ester or salt of the carboxy radical, or have the meanings given for R¹, or are linked to form a ring [-CR⁷R⁸] _n with n equal to 2, 3 or 4 and R⁵ and R⁶ have the meanings given for R¹ and
R⁷ and R⁸ are the same or different and are halogen, Car boxyrest, ester or salt of carboxy, or have the meanings mentioned for R¹.

As mediators in the multicomponent system according to the invention Compounds with the general formula are particularly preferred I in which X is Q or S and the remaining radicals are have the meanings given above. An example of a such compound is dimethyl 2-hydroxyiminomalonate.

Isonitroso are also particularly preferred as mediators Derivatives of cyclic ureids of the general formula II. Examples of such compounds are 1-methylvioluric acid, 1,3-dimethylvioluric acid, thiovioluric acid, alloxan-4,5-dioxime.

Alloxan-5-oxime hydrate is particularly preferred as mediator (Vibluric acid) and / or its esters, ethers or salts.  

The multicomponent system according to the invention contains mediators, which are less expensive than HBT.

In addition, when using the Mediato according to the invention an increase in the rate of delignification achieved.

The multicomponent system according to the invention preferably comprises at least one oxidation catalyst.

As oxidation catalysts in the invention component system preferably used enzymes. In the sense of Er Invention, the term enzyme also includes enzymatically active pro teins or peptides or prosthetic groups of enzymes.

The enzyme in the multicomponent system according to the invention Oxidoreductases of classes 1.1.1 to 1.97 according to Internationa Enzyme Nomenclature, Committee of the International Union of Biochemistry and Molecular Biology (Enzyme Nomenclature, Academic Press, Inc., 1992, pp. 24-154) can be used.

Enzymes of the classes mentioned below are preferably used:
Class 1.1 enzymes, which comprise all dehydrogenases which act on primary, secondary alcohols and semiacetals, and which accept NAD⁺ or NADP⁺ (subclass 1.1.1), cyto-chrome (1.1.2), oxygen (O₂) ( 1.1.3), disulfides (1.1.4), quinones (1.1.5) or other acceptors (1.1.99).

The enzymes of this class are particularly preferred Class 1.1.5 with quinones as acceptors and the enzymes of the Class 1.1.3 with oxygen as the acceptor.

Cellobiose is particularly preferred in this class:
quinone-1-oxidoreductase (1.1.5.1).

Enzymes of class 1.2 are also preferred. This enzyme class (1.1.5.1) includes such enzymes that add aldehydes to the oxidize corresponding acids or oxo groups. The Ak receptors can NAD⁺, NADP⁺ (1.2.1), cytochrome (1.2.2), sow erstoff (1.2.3), sulfides (1.2.4), iron-sulfur proteins (1.2.5) or other acceptors (1.2.99).

The enzymes of group (1.2.3) are particularly preferred here with oxygen as the acceptor.

Enzymes of class 1.3 are also preferred. In this Enzymes are classed that are based on CH-CH groups of the Donors work.

The corresponding acceptors are NAD⁺, NADP⁺ (1.3.1), Cyto chrome (1.3.2), oxygen (1.3.3), quinones or related Compounds (1.3.5), iron-sulfur proteins (1.3.7) or an other acceptors (1.3.99).

Bilirubin oxidase (1.3.3.5) is particularly preferred.

Here are also the enzymes of class (1.3.3) with acid substance as acceptor and (1.3.5) with quinones etc. as acceptor particularly preferred.

Enzymes of class 1.4 which are based on CH-NH₂ groups of the donor act.

The corresponding acceptors are NAD⁺, NADP⁺ (1.4.1), Cyto chrome (1.4.2), oxygen (1.4.3), disulfide (1.4.4), iron Sulfur proteins (1.4.7) or other acceptors (1.4.99).

Enzymes of class 1.4.3 are also particularly preferred here Oxygen as an acceptor.

Also preferred are class 1.5 enzymes based on CH-NH- Groups of the donor work. The corresponding acceptors are  NAD⁺, NADP⁺ (1.5.1), oxygen (1.5.3), disulfides (1.5.4), Quinones (1.5.5) or other acceptors (1.5.99).

Enzymes with oxygen (O₂) are also particularly preferred here. (1.5.3) and with quinones (1.5.5) as acceptors.

Enzymes of class 1.6 which are based on NADH are also preferred or NADPH work.

The acceptors here are NADP⁺ (1.6.1), heme proteins (1.6.2), Disulfides (1.6.4), quinones (1.6.5), NO₂ groups (1.6.6), and a flavin (1.6.8) or some other acceptors (1.6.99).

Enzymes of class 1.6.5 are particularly preferred here Quinones as acceptors.

Enzymes of class 1.7 which are based on others are also preferred NO₂ compounds act as donors and as acceptors cyto chrome (1.7.2), oxygen (O₂) (1.7.3), iron-sulfur-pro have stones (1.7.7) or others (1.7.99).

Class 1.7.3 with oxygen is particularly preferred here as an acceptor.

Enzymes of class 1.8, which are based on Schwe Field groups act as donors and as acceptors NAD⁺, NADP⁺ (1.8.1), cytochrome (1.8.2), oxygen (O₂) (1.8.3), disulfi de (1.8.4), quinones (1.8.5), iron-sulfur proteins (1.8.7) or others (1.8.99).

Class 1.8.3 with oxygen (O₂) is particularly preferred and (1.8.5) with quinones as acceptors.

Also preferred are class 1.9 enzymes which are based on heme groups act as donors and oxygen as acceptors (O₂) (1.9.3), NO₂ compounds (1.9.6) and others (1.9.99) to have.  

Group 1.9.3 with oxygen is particularly preferred here (O₂) as an acceptor (cytochrome oxidases).

Also preferred are enzymes of class 1.12 which are based on what act as a donor.

The acceptors are NAD⁺ or NADP⁺ (1.12.1) or others (1.12.99).

Enzymes of class 1.13 and 1.14 are also preferred (Oxigenases).

Furthermore, preferred enzymes are those of class 1.15 which are based on Superoxide radicals act as acceptors.

Superoxide dismutase is particularly preferred here (1.15.1.1).

Enzymes of class 1.16 are also preferred.

NAD⁺ or NADP⁺ (1.16.1) or oxygen act as acceptors (O₂) (1.16.3).

Enzymes of class 1.16.3.1 are particularly preferred here (Ferroxidase, e.g. ceruloplasmin).

Further preferred enzymes are those belonging to the group 1.17 (effect on CH₂ groups which are oxidized to -CHOH-), 1.18 (effect on reduced ferredoxin as donor), 1.19 (Effect on reduced flavodoxin as a donor) and 1.97 (others Oxidoreductases).

The enzymes of the group are also particularly preferred 1.11. Which act on a peroxide as an acceptor. This one Subclass (1.11.1) contains the peroxidases.

The cytochrome C peroxidases are particularly preferred here (1.11.1.5), catalase (1.11.1.6), the peroxidase (1.11.1.6),  iodide peroxidase (1. 11. 1.8), glutathione peroxidase (1.11.1.9), the chloride peroxidase (1.11.1.10), the L-Ascor bat peroxidase (1.11.1.11), the phospholipid hydroperoxide Glutathione peroxidase (1.11.1.12), the manganese peroxidase (1.12.1.13), the diarylpropane peroxidase (ligninase, lignin Peroxidase) (1.11.1.14).

Enzymes of class 1.10 which are based on Biphenols and related compounds work. They catalyze the oxidation of biphenols and ascorbates. As acceptors act NAD⁺, NADP⁺ (1.10.1), Cytochrome (1.10.2), Sauer fabric (1.10.3) or other (1.10.99).

Of these, in turn, are class 1.10.3 enzymes with acid Substance (O₂) is particularly preferred as an acceptor.

Of the enzymes in this class, the enzymes are catechol oxidase (Tyrosinase) (1.10.3.1), L-ascorbate oxidase (1.10.3.3), o-A- minophenol oxidase (1.10.3.4) and laccase (benzene diol: oxigen Oxidoreductase) (1.10.3.2) is preferred, the laccases (Ben zoldiol: Oxigen Oxidoreductase) (1.10.3.2) especially before are moving.

The enzymes mentioned are commercially available or can be win according to standard procedures. As organisms for production the enzymes come from plants, animal cells, Bacteria and fungi into consideration. Basically, both naturally occurring as well as genetically modified organization be enzyme producers. Parts from einselli are also included gene or multicellular organisms conceivable as enzyme producers, especially cell cultures.

For the particularly preferred enzymes, such as those from the Grup pe 1.11.1 but above all 1.10.3 and especially for production On laccases, for example, white rot fungi such as pleu rotus, phlebia and trametes used.  

The multi-component system according to the invention comprises at least one oxidizing agent. Examples of air, oxygen, ozone, H₂O₂, organic peroxides, peracids such as peracetic acid, performic acid, persulfuric acid, persalpic acid, metachloroperoxibenzoic acid, perchloric acid, perborates, peracetates, persulfates, peroxides or oxygen-like species and their radicals can be used as oxidizing agents ^. , OOH ^· , singlet oxygen, superoxide (O₂ ^{· -} ), ozonide, dioxygenyl cation (O₂⁺), di oxirane, dioxetane or fremy radicals can be used.

Oxidizing agents are preferably used which either generated by the corresponding oxidoreductases can be z. B. dioxiranes from laccases plus carbonyls or who can chemically regenerate the mediator or di can implement directly.

The invention also relates to the use of substances which are suitable according to the invention as mediators for changing change, breakdown or bleaching of lignin, lignin-containing materia lien or similar substances.

The effectiveness of the multicomponent system 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. MgSO₄, are 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 in the effectiveness of the multicomponent system according to the invention can be achieved in that the multicomponent system in addition to the Mg ²⁺ ions also complexing agents such as. B. ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), hydroxyethylene diaminetriacetic acid (HEDTA), diethylenetriaminepentamethylene phosphonic 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.

The use of the multicomponent system according to the invention in A method for treating lignin is carried out, for example se in that the components selected in each case a) to c) according to claim 1 simultaneously or in any order sequence with an aqueous suspension of lignin-containing Ma mixes terials.

Preferably, a method using the fiction modern multi-component system in the presence of oxygen or air at normal pressure up to 10 bar and in a pH range from 2 to 11, at a temperature of 20 to 95 ° C, preferably wise 40-95 ° C, and a consistency of 0.5 to 40% carried out.

One for the use of enzymes in pulp bleaching A common and surprising finding is that when the multicomponent system according to the invention an increase in Material density a significant increase in kappa reduction enables.

For reasons of economy, one according to the invention is preferred Process with material densities of 8 to 35%, particularly preferred 9 to 15% performed.

Surprisingly, it was also found that an acid wash (pH 2 to 6, preferably 4 to 5) or Q stage (pH 2 to 6, preferably 4 to 5) before the enzyme mediator stage in man Chen pulps to a significant kappa reduction in Comparison to treatment without this special pretreatment leads. In the Q stage, the chelating agents become those Common substances (such as EDTA, DTPA) are used for the purpose. They are preferably in concentrations of 0.1% / t to 1% / t particularly preferably 0.1% / t to 0.5% / t used.  

In the process according to the invention, 0.01 to 10,000 IU enzyme used per g of lignin-containing material. Be 0.1 to 100 are particularly preferred 1 to 40 IU enzyme are added per g of lignin-containing material sets (1 U corresponds to the conversion of 1 µmol of 2,2′-azino-bis- (3-ethyl-benzothiazoline-6-sulfonic acid diammonium salt) (ABTS) / min / ml enzyme).

In the process according to the invention, preferably 0.01 mg to 100 mg of oxidizing agent per g of lignin-containing material puts. 0.01 to 50 mg of oxidation are particularly preferred medium used per g of lignin-containing material.

In the process according to the invention, preferably 0.5 to 80 mg mediator used per g of lignin-containing material. Especially 0.5 to 40 mg mediator per g ligninhal are preferred used material.

At the same time, reducing agents can be added, too together with the existing oxidizing agents for adjustment serve a certain redox potential.

Sodium bisulfite, sodium Dithionite, ascorbic acid, thio compounds, mercapto compounds gene or glutathione etc. can be used.

In the case of laccase, for example, the reaction takes place under air or Oxygen supply or oxygen or air pressure from, at the peroxidases (e.g. lignin peroxidases, manganese peroxidases) with hydrogen peroxide. For example, the Oxygen also through hydrogen peroxide + catalase and what hydrogen peroxide by glucose + glucose oxidase or other sy systems can be generated in situ.

Radical formers or radical scavengers can also be added to the system (Trapping of, for example, OH or OOH radicals) be set. These can interact within the Improve Red / Ox and radical mediators.  

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

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 ²⁺ , Ca ²⁺ , Ti ³⁺ , Cer ⁴⁺ , Al ³⁺ .

The chelates present in the solution can also as mimic substances for the enzymes, for example for the Laccases (copper complexes) or for the lignin or manganese serve oxidases (heme complexes). Among mimic substances are sol to understand substances that the prosthetic groups of (here) simulate oxidoreductases and e.g. B. Oxidation reaction can catalyze.

NaOCl can also be added to the reaction mixture. This compound can interact with hydrogen peroxide Form singlet oxygen.

Finally, it is also possible to use detergents tien to work. As such come non-ionic, anioni cal, cationic and amphoteric surfactants. The De Detergents can penetrate the enzymes and mediators in improve the fiber.

Polysacchari can also help the reaction de and / or add proteins. Here are especially as Polysaccharides glucans, mannans, dextrans, levans, pectins, Alginates or plant gums and / or your own mushrooms Poly formed or produced in the mixed culture with yeast saccharide 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. to  serve by breaking down the extensin C present in the wood, of a protein rich in hydroxyproline, better access to To achieve lignin.

Other protective colloids are amino acids, simple sugar, Oligomer sugar, PEG types of different molecular weights te, polyethylene oxides, polyethyleneimines and polydimethylsiloxa no, ask.

The method according to the invention can be used not only for the Deligni preparation (bleaching) of sulfate, sulfite, organosol, etc. Pulp and wood pulp are used, but also in the production of cellulose or wood pulp (Re Finerstoff / Holzschliff) generally for example from wood or annual plants. Defibrillation should be done by the usual cooking processes and / or mechanical processes or pressure (i.e. a very gentle treatment down to kappa numbers in the range of <50 kappa or <10% lignin content) ge be guaranteed.

In the bleaching of cellulose as well as in the production The treatment of pulps can be repeated several times either after washing and extracting the treated fabric with NaOH or without these intermediate steps. this leads to even further reduced kappa values and increased Chen increases in white. Likewise, before the enzyme / mediatorbe an O₂ level can be used or as already mentions an acid wash or Q level (chelate level) leads.

In the following, the invention will be explained in more detail by means of examples explains:  

example 1 Enzymatic bleach with violuric acid and softwood Sulfate pulp

5 g dry cellulose (Softwood O₂ delignified), consistency 30% (approx. 17 g moist) are added to the following solutions:

• A) 20 ml of tap water are mixed with 65 mg of violuric acid Monohy drat added with stirring, the pH with 0.5 mol / l H₂SO₄ solution. adjusted so that after adding the pulp and of the enzyme pH 4.5 results.
• B) 5 ml tap water with the amount of Laccase from Trame tes versicolor that an activity of 35 U (1 U = Conversion of 1 µmol ABTS / min / ml enzyme) per g pulp results.

Solutions A and B are combined and made up to 33 ml replenished.

After adding the pulp, use a batter for 2 min mixed.

The fabric is then preheated to 45 ° C given bomb and under 1-10 bar oxygen pressure for 10 incubated for up to 40 minutes.

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

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

Depending on the incubation period, the following deligni Processing rates reached:

Example 2 Enzymatic bleach with violuric acid and softwood Sulfate pulp

5 g dry cellulose (Softwood O₂ delignified), consistency 30% (approx. 17 g moist) are added to the following solutions:

• A) 20 ml of tap water are mixed with 130 mg of violuric acid Monohy drat added with stirring, the pH with 0.5 mol / l H₂SO₄ solution. adjusted so that after adding the pulp and of the enzyme pH 4.5 results.
• B) 5 ml tap water with the amount of Laccase from Trame tes versicolor that an activity of 35 U (1 U = Conversion of 1 µmol ABTS / min / ml enzyme) per g pulp results.

Solutions A and B are combined and made up to 33 ml replenished.

After adding the pulp, use a batter for 2 min mixed.

The substance is then preheated to 45 ° C given bomb and under 1-10 bar oxygen pressure for 1- Incubated for 4 hours.

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

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

Depending on the incubation period, the following deligni Processing rates reached:

The enzyme activity was used after a reak  time of 4 hours found 89%.

Comparative Example 1 Enzymatic bleach with 1-hydroxy-1-H-benzotriazole and softwood sulfate pulp

5 g dry cellulose (Softwood O₂ delignified), consistency 0% (approx. 17 g moist) are added to the following solutions:

• A) 20 ml tap water with 25 mg 1-Hydroxy-1-H-benzotriazole added with stirring, the pH with 0.5 mol / l H₂SO₄ solution. adjusted so that after adding the Pulp and the enzyme pH 4.5 results.
• B) 5 ml tap water with the amount of Laccase from Trame tes versicolor that an activity of 35 U (1 U = Conversion of 1 µmol ABTS / min / ml enzyme) per g pulp results.

Solutions A and B are combined and made up to 33 ml replenished.

After adding the pulp, use a batter for 2 min mixed.

The substance is then preheated to 45 ° C given bomb and under 1-10 bar oxygen pressure for 10 incubated for up to 40 minutes.

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

After washing the fabric again, the kappa number is determined. Depending on the incubation period, the following deligni Processing rates reached:

Comparative Example 2 Enzymatic bleach with 1-hydroxy-1-H-benzotriazole and softwood sulfate pulp

5 g dry cellulose (Softwood O₂ delignified), consistency 30% (approx. 17 g moist) are added to the following solutions:

• A) 20 ml tap water with 50 mg 1-Hydroxy-1-H-benzotriazole added with stirring, the pH with 0.5 mol / l H₂SO₄ solution. adjusted so that after adding the Pulp and the enzyme pH 4.5 results.
• B) 5 ml tap water with the amount of Laccase from Trame tes versicolor that an activity of 35 U (1 U = Conversion of 1 µmol ABTS / min / ml enzyme) per g pulp results.

Solutions A and B are combined and made up to 33 ml replenished.

After adding the pulp, use a batter for 2 min mixed.

The substance is then preheated to 45 ° C given bomb and under 1-10 bar oxygen pressure for 1-4 Incubated for hours.

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

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

Depending on the incubation period, the following deligni Processing rates reached:

The enzyme activity was used after a reak 15% recovery time of 4 hours.

Claims (11)

1. Containing a multi-component system for changing, breaking down or bleaching lignin, lignin-containing materials or similar substances

• a. optionally at least one oxidation catalyst and
• b. at least one suitable oxidizing agent and
• c. at least one mediator, characterized in that the mediator is selected from the group of oximes of the general formula I or II

and their salts, ethers, or esters, where
X is the same or different and is O, S, or NR¹ where
R¹ is hydrogen, hydroxyl, formyl, carbamoyl, sulfono, ester or salt of sulfono, sulfamoyl, nitro, amino, phenyl, aryl-C₁-C₅-alkyl, C₁-C₁₂-alkyl, C₁ -C₅-alkoxy-, C₁-C₁₀-carbonyl, carbonyl-C₁-C₆-alkyl, phospho-, phosphono-, phosphonooxy, ester or salt of the phosphonooxy,
where carbamoyl, sulfamoyl, amino and phenyl radicals are unsubstituted or can be substituted one or more times with a radical R² and the aryl-C₁-C₅-alkyl, C₁-C₁₂-alkyl, C₁-C₅-alkoxy, C₁ -C₁₀-carbonyl, carbonyl-C₁-C₆-alkyl radicals may be saturated or unsaturated, branched or unbranched and may be substituted one or more times with a radical R²
R² is the same or different and is hydroxyl, formyl, carboxy, ester or salt of carboxy, carbamoyl, sulfono ester or salt of sulfono, sulfamoyl, nitro, amino, phenyl, C₁-C₅-alkyl , C₁-C₅ alkoxy and
the radicals R³-R⁴ are identical or different and are halogen, carboxy, ester or salt of the carboxy radical, or have the meanings given for R¹, or are linked to form a ring [-CR⁷R⁸] _n with n equal to 2, 3 or 4 and
R⁵ and R⁶ have the meanings given for R¹ and
R⁷ and R⁸ are the same or different and are halogen, carboxy, ester or salt of the carboxy, or have the meanings given for R¹. 2. Multi-component system according to claim 1, characterized records that there is at least one oxidation catalyst includes. 3. Multi-component system according to claim 1 or 2, characterized ge indicates that enzyme is used as the oxidation catalyst becomes. 4. Multi-component system according to one of claims 1 to 3, characterized in that laccase is used as the enzyme. 5. Multi-component system according to one of claims 1 to 4, characterized in that the oxidizing agent is air, oxygen, ozone, H₂O₂, organic peroxides, peracids such as peracetic acid, performic acid, persulfuric acid, persalpeteric acid, metachloroperoxibenzoic acid, perchloric acid, perborates, peracetates, persulfates , Peroxides or oxygen species and their radicals such as OH ^· , OOH ^· , singlet oxygen, superoxide (O₂ ^{· -} ), ozonide, dioxygenyl cation (O₂⁺), dioxiranes, dioxetanes or fremy radicals are used. 6. Multi-component system according to one of claims 1 to 5, there characterized in that as a mediator compounds of gen my formula I, where X is O or S and the rest Residues have the meanings given above will. 7. Multi-component system according to one of claims 1 to 6, characterized in that as mediator isonitroso derivatives of cyclic ureids of the general formula II used will. 8. Multi-component system according to one of claims 1 to 7, characterized in that as mediator alloxan-5-oxime hydrate (Violuric acid) or its esters, ethers or salts used will. 9. A method for treating lignin, characterized in that that the components selected a) to c) according to Claim 1 simultaneously or in any order with egg ner aqueous suspension of the lignin-containing material mixes. 10. Use of mediators according to claim 1 for changing, Degradation or bleaching of lignin, materials containing lignin or similar substances.