EP1483442A2 - Nouvelles activites catalytiques d'oxydo-reductases pour l'oxydation et/ou le blanchiment - Google Patents

Nouvelles activites catalytiques d'oxydo-reductases pour l'oxydation et/ou le blanchiment

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Publication number
EP1483442A2
EP1483442A2 EP03704246A EP03704246A EP1483442A2 EP 1483442 A2 EP1483442 A2 EP 1483442A2 EP 03704246 A EP03704246 A EP 03704246A EP 03704246 A EP03704246 A EP 03704246A EP 1483442 A2 EP1483442 A2 EP 1483442A2
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EP
European Patent Office
Prior art keywords
bleaching
compounds
oxidation
acid
pulp
Prior art date
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EP03704246A
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German (de)
English (en)
Inventor
Hans-Peter Call
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Call Krimhild
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Call Krimhild
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Publication of EP1483442A2 publication Critical patent/EP1483442A2/fr
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Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38654—Preparations containing enzymes, e.g. protease or amylase containing oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D7/00—Compositions of detergents based essentially on non-surface-active compounds
    • C11D7/22—Organic compounds
    • C11D7/26—Organic compounds containing oxygen
    • C11D7/264—Aldehydes; Ketones; Acetals or ketals
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00—Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/005—Treatment of cellulose-containing material with microorganisms or enzymes
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C9/00—After-treatment of cellulose pulp, e.g. of wood pulp, or cotton linters ; Treatment of dilute or dewatered pulp or process improvement taking place after obtaining the raw cellulosic material and not provided for elsewhere
    • D21C9/10—Bleaching ; Apparatus therefor
    • D21C9/1026—Other features in bleaching processes
    • D21C9/1036—Use of compounds accelerating or improving the efficiency of the processes

Definitions

  • enzymes such as peroxidases, especially Horseradish Peroxidase (HRP) and the lignolytic enzymes belonging to lignin peroxidase and manganese peroxidase and certain oxidases such as laccase (also belonging to the lignolytic enzymes) in the presence of H 2 O 2 , organic peroxides or peracids (peroxidases) or atmospheric oxygen or O 2 (oxidases / laccases) can oxidize corresponding substrates, the substrate spectrum for these enzymes being generally very large.
  • HRP Horseradish Peroxidase
  • laccase also belonging to the lignolytic enzymes
  • these mediator compounds enable the oxidation of substrates with higher oxidation potentials, which normally could not be oxidized, and on the other hand, because they are low molecular weight and free-diffusible, they put the enzyme (laccase) / mediator system in the position not even in substrates break down freely accessible substances such as lignin in cellulose fibers. Free enzyme would not cause significant degradation here due to its too large molecular weight (in addition to the insufficient oxidizing power).
  • oxidoreductases such as laccases and / or peroxidases - individually or in combination - in the presence of their respective co-substrates O, H 2 O 2 , organic peroxides, peracids, etc.
  • Such compounds are used as oxocarbons in accordance with: Chemistry in Our Time, 16th Year 1982, No. 2, pp. 57-67 including the literature cited therein, in particular R.West et al., Oxocarbons and their Reactions, in J. Zabicky ed., "The chemistry of the Carbonyl Group", Wyley (Interscience), 1970; R.West, Oxocarbons, Academic Press, 1980 and Römpp Chemie Lexikon, Thieme
  • radicals Rl to R 8 can each independently represent one of the following atoms of the atomic groups: hydrogen, halogen, alkyl, alkyloxy, aryl, aryloxy, hydroxy, oxo, formyl, thioxo, mercapto, alkylthio, sulfeno, sulfino, sulfo , Sulfamoyl, amino, imino, amido, amidino, hydroxycarbamoyl, hydroximino, nitroso, nitro, hydrazono and being the radicals
  • R 1 and R 2 ; R 3 and R 4 ; R 5 and R 6 ; R 7 and R 8 can form a common group and where n> 1.
  • radicals R ⁇ to R * 0 each independently represent one of the following atoms or atom groups: hydrogen, halogen, alkyl, alkyloxy, aryl, aryloxy, hydroxy, oxo, formyl, thioxo, mercapto, alkylthio, sulfeno, sulfino, sulfo , Sulfamoyl, amino, imino, amido, amidino, hydroxycarbamoyl, hydroximino, nitroso, nitro, hydrazono and being the radicals
  • R ⁇ and RIO can form a common group.
  • radicals R * 1 to R * 2 can each independently represent one of the following atoms or atom groups: hydrogen, halogen, alkyl, alkyloxy, aryl, aryloxy, hydroxy, oxo, formyl, thioxo, mercapto, alkylthio, sulfeno, sulfino, Sulfo, sulfamoyl, amino, imino, amido, amidino, hydroxycarbamoyl, hydroximino, nitroso, nitro, hydrazono and m> 0.
  • Cyclic oxocarbons of the general formula IV (general empirical formula: H2C ⁇ O x , and their dianions of the general formula) are particularly preferred
  • tetrahydroxy-p-benzoquinone is particularly preferred, which are described in the literature: K.Deuchert et. al., Angewandte Chemie, 90, 1978, pp. 927-938.
  • the radicals R can be the same or different and independently represent hydrogen, alkyl, aryl or acyl groups.
  • R 4 can be hydrogen, alkyl, alkoxy, carboxy, nitro or amino.
  • the radicals R can be the same or different and independently of one another are hydrogen, alkyl, aryl or.
  • the following compounds are particularly preferred:
  • 5-Amino-5-hydroxypyrazoles, 2,3-dihydro-l, 4-phthalazinedione, phthalhydrazides, 7-nitroindazoles and 1,2-dihydropyrazine-3,6-dione are very particularly preferred.
  • the following compounds are also particularly preferred: 4-phenylurazole, 1-phenylurazole, 4-methylurazole, 4-tert-butylurazole and urazole, of which in particular: 4-tert-butylurazole and urazole.
  • hydantoins are preferred compounds of the general formula X (imides):
  • radicals R can be the same or different and, independently of one another, represent hydrogen, alkyl, aryl, acyl or amino groups.
  • radicals R can be the same or different and independently represent hydrogen, alkyl, aryl, acyl or amino groups.
  • Cyclic imides of the general formula XII are also particularly preferred:
  • Cyanamide and dicyandiamide are particularly preferred.
  • Oxidoreductases are preferably used as enzymes.
  • the term enzyme also encompasses enzymatically active proteins or peptides or prosthetic groups of enzymes.
  • the enzymes can likewise come from wild-type strains or from genetically modified host strains.
  • the particularly preferred enzymes include laccases and peroxidases, with the peroxidases partly because of their Optimal pH effects reaching far further into the alkaline environment can have considerable advantages when used for the bleaching of cellulose.
  • Oxidoreductases of classes 1.1.1. Can be used as enzymes in the oxidation bleaching system according to the invention. 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).
  • Class 1.1 enzymes particularly preferably the class 1.1.5 enzymes with quinones as acceptors and the class 1.1.3 enzymes. with oxygen as the acceptor, cellobiose: quinone-1-oxidoreductase (1.1.5.1) is particularly preferred in this class.
  • Enzymes of class 1.2 can also be used.
  • the enzymes of group (1.2.3) with oxygen as the acceptor are particularly preferred here.
  • Enzymes of class 1.3 can also be used. Here are also the enzymes of class (1.3.3) with oxygen as acceptor and (1.3.5) with quinones etc. as
  • Bilirubin oxidase (1.3.3.5) is particularly preferred.
  • Class 1.4 enzymes can also be used. Enzymes of class 1.4.3 with oxygen as the acceptor are also particularly preferred here.
  • Enzymes of class 1.5 can also be used. Enzymes with oxygen (1.5.3) and with quinones (1.5.5) are also particularly preferred here
  • Enzymes of class 1.6 can also be used. Enzymes of class 1.6.5 with quinones as acceptors are particularly preferred.
  • Enzymes of class 1.7 can also be used. Class 1.7.3 with oxygen as the acceptor is particularly preferred here.
  • Enzymes of class 1.8 can also be used.
  • Class 1.8.3 with oxygen and (1.8.5) with quinones are particularly preferred as acceptors.
  • Enzymes of class 1.9 can also be used. The is particularly preferred here
  • Enzymes of class 1.15 which are based on superoxide radicals can also be used
  • Enzymes of class 1.16 can also be used. Enzymes of class 1.16.3.1 (ferroxidase, e.g. ceruloplasmin) are particularly preferred here.
  • Flavodoxin as donor and 1.97 (other oxidoreductases).
  • the very particularly preferred enzymes include those of class 1.10. Of the enzymes in this class 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 oxy oxidoreductase) (1.10.3.2) are preferred, the laccases being particularly preferred.
  • the enzymes of group 1.11 are also particularly preferred.
  • the cytochrome C peroxidases (1.11.1.5), catalase (1.11.1.6), the peroxidase (1.11.1.6), the iodide peroxidase (1.11.1.8), the glutathione peroxidase (1.11.1.9) 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 (1.12.1.13), the diaryl propane peroxidase (ligninase, lignin peroxidase (1.12.1.14).
  • the enzymes mentioned are commercially available or can be obtained by standard processes.
  • organisms for producing the enzymes are plants, bacteria and fungi.
  • both naturally occurring and Genetically modified organisms are enzyme producers, and parts of single-cell or multicellular organisms are also conceivable as enzyme producers, especially cell cultures, in particular for the production of the preferred enzymes from group 1.11.1 and enzymes from group 1.10.3, in particular for the production of laccases and other ligninolytic enzymes (lignin peroxidases, manganese peroxidases), for example white rot fungi etc. such as pleurotus, phlebia and trametes, agaricus, lentinus, botrytis, cryphonectria, hypholoma, heterobasidion, phanerochaete and others used.
  • lignin peroxidases manganese peroxidases
  • white rot fungi etc. such as pleurotus, phlebia and trametes, agaric
  • air oxygen, peroxides such as H 2 O 2 , organic peroxides, peracids such as peracetic acid, performic acid, persulfuric acid, persitric acid, metachloroperoxibenzoic acid, per compounds such as perborates, percarbonates, persulfates or oxygen species such as OH radicals, OOH radicals can be used as co-substrates , OH + radicals, superoxide (O " 2 ) and singlet oxygen can be used.
  • radicals R 1 and R 2 can be the same or different and represent aliphatic or aromatic groups. Furthermore, the radicals R 1 and R 2 can form a ring which, in addition to carbon, can also contain heteroatoms such as nitrogen, oxygen and sulfur.
  • 1,2-diketones (formula XV) and 1,3-diketones (formula XVI) or polyketones (polyketides) and the tautomeric enols (formula XVII) are particularly preferred,
  • 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.
  • ketones are generally hydroxy ketones, ⁇ -unsaturated ketones and oxicarboxylic acids.
  • carbonyl compounds such as: acetone, methyl ethyl ketone, diethyl ketone, methyl n-butyl ketone, methyl isobutyl ketone, cyclohexanone, cyclopentanone, 2-methylcyclohexanone, 3-methylcyclohexanone, 4-methylcyclohexanone, dihydroxyacetone, diacetyl (monohydrazone), drazonyl) , Acetophenone, p-hydroxyacetophenone, l-phenylbutan-3-one, pentan-3-one, heptan-4-one, nonan-2-one, cycloheptanone, cyclooctation, cyclodecanone, cyclododecanone, cyclohexanone, 2-methylcyclohexanone, 3-methylcyclohexanone , 4-methylcyclohexanone, cyclopentanone, 2- Methylcyclopentanone
  • coal liquefaction properties were also found in the treatment of lignite or hard coal.
  • a high and selective oxidizing power when used as an "oxidizing agent" in organic synthesis a strong bleaching power when using bleach in detergents and in the general oxidative treatment (e.g. bleaching) of textile fabrics including wool, or in the case of special bleaching with Use in stone-wash processes, namely as a substitute for mechanical dye removal and / or post-bleaching in these processes, has been proven.
  • the method described in German application: DE 198 20 947.9-45 differs from the present invention mainly in the addition of suitable ketone compounds, which are generally aliphatic in the system according to the invention. No benzophenones, benzils and organic carbonyl compounds which are listed there are used, since these have been shown to be ineffective.
  • the HOS system hydrolase mediated oxidation system
  • the HOS system hydrolase mediated oxidation system
  • the HOS system consisting of lipases or similar hydrolases, peroxide
  • 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 Na2S, while in the sulfite process Ca (HS ⁇ 3) 2 + SO2 are used, or today, because of their better solubility, the sodium or ammonium salts of hydrogen sulfite.
  • the main aim of all processes is to remove the lignin from the plant material, wood or annual plants used.
  • the lignin which is the main constituent of the plant material (stem or stem) with cellulose and hemicellulose, must be removed, otherwise it will not be possible to produce non-yellowing and mechanically heavy-duty papers.
  • the wood-based production processes work with stone grinders (wood sanding) or with refiners (TMP), which defibrillate the wood after grinding (chemical, thermal or chemical-thermal).
  • Biopulping is the treatment of wood chips with living ones
  • One advantage is the mostly existing improvement in the mechanical properties of the fabric, one disadvantage is the poorer final whiteness.
  • the goal here is to reduce cooking chemicals, improve cooking capacity and "extended cooking”.
  • Biobleaching also works with in-vivo systems.
  • the boiled pulp (Softwood / Hardwood) is inoculated with the fungus before bleaching and treated for days to weeks. Only after this long treatment time does a significant decrease in kappa number and whiteness become apparent, which makes the process uneconomical for implementation in the usual bleaching sequences.
  • Another application is the treatment of pulp manufacturing wastewater, in particular bleaching plant wastewater to decolorize it and reduce the AOX (reduction of chlorinated compounds in the wastewater that cause chlorine or chlorine dioxide bleaching stages). It is also known to use hemicellulases, inter alia, xylanases, mannanases as "bleach boosters".
  • the application PCT / EP87 / 00635 describes a system for removing lignin from lignin-cellulose-containing material with simultaneous bleaching, which works with lignolytic enzymes from white rot fungi with the addition of reducing and oxidizing agents and phenolic compounds as mediators.
  • Peroxidase activity is promoted by means of so-called enhancer substances.
  • the enhancer substances are characterized in WO 94/12619 on the basis of their half-life.
  • enhancer substances are organic chemicals which contain at least two aromatic rings, at least one of which is substituted with defined radicals.
  • 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.
  • 1-hydroxy-1H-benzotriazole (HBT) provides the best results in delignification.
  • HBT has several disadvantages:
  • oxidases and peroxidases have a low substrate specificity, i.e. they can implement a wide range of substances, usually phenolic in nature. Without mediators, the oxidases, but also many peroxidases, tend to radically polymerize phenolic substances, a property that e.g. the laccase belonging to the oxidases is also attributed in nature.
  • This ability to use suitable substances such as Polymerize lignins, i.e. the corresponding molecules can be enlarged by "coupling reactions", e.g. for the treatment of lignin-containing wastewater from the paper industry, such as TMP wastewater (wastewater from the production of thermomechanical pulp using refiners) and grinding mill wastewater from wood grinding plants.
  • the enzyme effect in this application can be recognized immediately by a rapid clouding of the treated wastewater, caused by the enlarged and thus insoluble lignin molecules.
  • the target molecules can be removed by appropriate treatments (flocculation, precipitation, for example with aluminum sulfate, sodium aluminate, possibly with the addition of polyelectrolytes / cationic or anionic or sedimentation).
  • the wastewater then has a significantly reduced COD. It therefore causes an initiation lower environmental pollution, or increases the security of staying below the permitted COD exposure limits, which is important especially when driving at the limit, which is not infrequently the case.
  • laccase represents the effort for the removal of the reaction products of the enzymatic treatment by flocculation, sedimentation or precipitation or combinations of several methods which by far accounts for the major part of the costs for the overall process.
  • the processes according to the invention are systems which are significantly improved compared to the above-mentioned systems with oxidoreductases (such as laccases) as oxidation catalysts, the advantages of which are above all: in their higher oxidation power, in the use of very easily degradable system components, which increase the COD in the short term, but are easy to remove in the subsequent treatment plant steps.
  • oxidoreductases such as laccases
  • Such substances can be phenols, phenol derivatives or other phenolic polycycles with a number of oxidizable hydroxyl groups.
  • Such polymerization catalysts e.g. are preferably those as described in WO98 / 59108 and DE 101 26 988.9.
  • the object of the present invention is to provide a process for the enzymatic polymerization and / or modification of lignin or lignin-containing materials, e.g. for use in the production of wood compositions or wood composites such as "Fiber board” made of shredded wood or “particle board” made of wood shavings or pieces of wood (-> chipboard, plywood, wood composite beams).
  • the enzymatic oxidation system according to the invention shows a superior performance to the enzymatic systems for polymerizing and / or modifying lignin and / or lignin-containing materials described in the prior art.
  • lignin for example lignosulfonates and / or non-evaporated or evaporated sulfite waste liquor and / or sulfate lignin ⁇ > “Kraft lignin”, for example indulin
  • lignin-containing material for example lignin-containing material
  • the lignin and / or the lignin-containing material can either be pre-incubated at higher pH values, ie 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) C) and then the pH value is shifted below pH 7, depending on the optimum active pH range of the enzymatic oxidation system or in the case of an alkaline active optimum of the enzymatic oxidation system, the system and lignin and / or lignin-containing material can be combined immediately without pretreatment.
  • the pretreatment or the treatment at alkaline pH has the purpose of utilizing the much easier solubility of the lignin at these higher pH values, which is of great advantage for the use according to the invention, since it is then possible to work without organic solvents.
  • the combination of the enzymatic oxidation system and lignin and / or lignin-containing material described thus serves primarily the purpose of activating the substrates (polyphenylpropane) by oxidation, i.e. by radical polymerization (modification) to convert the lignin and / or the lignin-containing material into an activated and active binder, which then, combined with wood fibers and / or wood parts to be bonded (to be glued) under the action of pressure and elevated temperature to solid wood composite parts such as the above-mentioned wood materials, e.g. Can harden "fiber boards" or "particle boards".
  • the main advantage is the reduction or saving of normally e.g. Urea-formaldehyde resins used in the manufacture of particle board for "gluing" which, in addition to toxicological concerns, are also only partially resistant to moisture or phenol formaldehyde resins which show an unfavorable swelling behavior and long pressing times (again in addition to the toxicological question).
  • normally e.g. Urea-formaldehyde resins used in the manufacture of particle board for "gluing” which, in addition to toxicological concerns, are also only partially resistant to moisture or phenol formaldehyde resins which show an unfavorable swelling behavior and long pressing times (again in addition to the toxicological question).
  • Deinken as is still practiced conventionally as flotation thinking, is basically a two-step process.
  • waste paper The goal is the removal of ink and other color particles from waste paper, whereby the so-called "household collectibles", which mainly consist of newspapers and magazines, are mostly used as waste paper.
  • 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 with the simultaneous addition of 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 ).
  • bleaching chemicals such as sodium hydroxide solution, fatty acid, water glass and hydrogen peroxide ( H 2 O 2 ).
  • the fatty acid serves as a so-called collector of the color particles, in the second treatment stage, flotation, also as a foam generator.
  • the flotation is carried out after the waste paper has been opened and a certain exposure time of the chemicals mentioned has been achieved by blowing air into special flotation containers.
  • the color particles attach to the foam bubbles and are removed with them, i.e. the color is separated from the paper fibers.
  • a "driving style" in a more neutral pH environment is preferred, which necessitates the use of certain detergents instead of the fatty acid.
  • the enzymatic oxidation system according to the invention by a suitable selection of the conditions, exceeds the efficiency of the other enzymatic deinking systems in the case of lignin-containing deinking agent and, above all, the advantage of the bleaching effect of the purely chemical systems at least partially is compensated.
  • the above-mentioned addition of the special polymerization catalysts i.e. Substances, mostly phenolic in nature and in particular with several hydroxyl groups, which are also used in enzymatic wastewater treatment and general polymerization reactions such as the production of binders / adhesives from lignin or lignin-containing substances. can be used for the production of wood composites as polymerization-increasing additives, bring about a further improvement in the ink separation.
  • 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
  • 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.
  • chemical bleach activators such as TAED and SNOBS.
  • 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. It is known that peroxidases are capable of different pigments (3-hydroxyflavone and betaine by horseradish peroxidase, carotene by peroxidase ) to "decolorize".
  • the patent application mentioned 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 intended to counteract, for example, hypochlorite, which also contains the dye or attack in the tissue have the advantage of decolorizing only the dye present in solution, hydrogen peroxide or a corresponding precursor or hydrogen peroxide generated in situ being involved in the catalysis of the decolorization.
  • the enzyme reaction can in part be carried out by adding additional oxidizable enzyme substrate, for example metal ions such as Mn ++ , halide ions such as Cl " or Br " or organic phenols such as p-hydroxycinnamic acid and 3,4-dichlorophenol can be increased.
  • additional oxidizable enzyme substrate for example metal ions such as Mn ++ , halide ions such as Cl " or Br " or organic phenols such as p-hydroxycinnamic acid and 3,4-dichlorophenol can be increased.
  • additional oxidizable enzyme substrate for example metal ions such as Mn ++ , halide ions such as Cl " or Br " or organic phenols such as p-hydroxycinnamic acid and 3,4-dichlorophenol can be increased.
  • 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.
  • Peroxidase activity is promoted by means of so-called enhancer substances.
  • Such enhancer substances are characterized in WO 94/12620 on the basis of their half-life.
  • enhancer substances are organic chemicals which contain at least two aromatic rings, at least one of which is substituted by defined radicals.
  • composition in the detergent area is limited to peroxidases.
  • WO 94/29425, DE 4445088.5 and WO 97/48786 contain multicomponent bleaching systems for use with detergent substances consisting of:
  • Enzymes are used today in increasing quantities and for various applications in the textile industry.
  • amylases plays a major role in the "desizing process", which can prevent the use of strong acids, alkalis or oxidizing agents.
  • Cellulases are also used for so-called bio-polishing as well as for so-called bio-stoning, a process that is mostly used together with the conventional process of stone washing with pumice stones when treating denim jeans to remove the indigo dye.
  • WO 94/29510, WO / 96/18770, DE 196 12 194 AI and DE 44 45 088 AI describe processes for enzymatic delignification, in which enzymes are used together with mediators.
  • Compounds with the structure NO, NOH or HRNOH are generally disclosed as mediators.
  • enhancer substances are characterized in WO 94/12620 on the basis of their half-life.
  • enhancer substances are organic chemicals which contain at least two aromatic rings, at least one of which is substituted with defined radicals.
  • oxidoreductases mainly laccases, but also peroxidases have recently been used for the treatment of mainly denim jeans.
  • 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 following:
  • Laccase must be used in considerable amounts (approx. 10 IU / g denim) in order to achieve the desired result.
  • 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.
  • Buffer systems (approx. 0.1 mol / L) must be used, since otherwise no performance can be achieved, which also makes the system considerably more expensive. This is e.g. not necessary in the systems according to the invention.
  • the dyes normally used in jeans denim are VAT dyes such as indigo or indigo derivatives, e.g. Thioindigo, but also so-called Sulfur dyes.
  • An additional advantage is that the enzymatic treatment is much gentler than bleaching with hypochlorite, which leads to less fiber damage.
  • the present invention has set itself the goal of the disadvantages of the conventional processes: stone washing / bleaching after stone washing or general bleaching of dyed and / or undyed textile fabrics:
  • Mg + ions can be used, for example, as a salt, such as MgSO4.
  • the concentration is in the range of 0.1-2 mg / g ligmn restrooms material, preferably
  • a further increase can be achieved in that the system, in addition to the Mg + ions, also complexing agents such as, for example, ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), hydroxyethylenediaminetriacetic acid (HEDTA), diethylenetriaminepentamethylenephosphonic acid (DTMPA), nitrilotriacetic acid (NTA) PPA) etc. contains.
  • the concentration is in the range of 0.2-5 mg / g of lignin-containing material, preferably 1-3 mg.
  • 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 oxidation and bleaching process according to the invention with some pulps to a significant kappa reduction compared to treatment without this special prerelease.
  • Post-treatment leads.
  • the substances used for this purpose (such as EDTA, DTPA) are used as chelating agents in the Q stage. They are preferably used in concentrations of 0.1% / to 1% / to, particularly preferably 0.1% / to to 0.5% / to.
  • reducing agents can be added which, together with the oxidizing agents present, serve to set a certain redox potential.
  • Sodium bisulfite, sodium dithionite, ascorbic acid, thio compounds, mercapto compounds or glutathione etc. can be used as reducing agents.
  • radical formers or radical scavengers can also be added to the system. These can improve the interaction within the Red / Ox and radical mediators.
  • the salts form cations in the reaction solution.
  • Such ions include Fe 2+ , Fe 3+ '
  • the chelates present in the solution can also serve as mimic substances for certain oxidoreductases such as laccases (copper complexes) or for lignin or manganese peroxidases (heme complexes).
  • Mimic substances include substances that can simulate the prosthetic groups of (here) oxidoreductases and can, for example, catalyze oxidation reactions.
  • detergents Non-ionic, anionic, cationic and amphoteric surfactants are suitable as such. The detergents can improve the penetration of the enzymes and other components into the fiber.
  • Eggs can be mentioned in particular as polysaccharides glucans, mannans, dextrans, levans, pectins, jginates or vegetable gums and as proteins gelatin and albumin. These substances mainly serve as protective colloids for the enzymes.
  • proteases such as pepsin, Bromeün, Papain sw. These can include serve to achieve better access to lignin by breaking down the extensin present in the wood (protein rich in hydroxyproline).
  • protective colloids that can be used are amino acids, simple sugar, oligomer sugar, PEG types of various molecular weights, polyethylene oxides, polyethyleneimines and olydimethylsiloxanes.
  • substances can be added to the oxidation and bleaching system according to the invention, which increase the hydrophobicity of the reaction environment and thus have a swelling effect on the ignin in the fibers and thus increase its vulnerability.
  • substances are, for example, glycols such as: propylene glycol, ethylene glycol, glycol ethers such as: ethylene glycol dimethyl ether etc.
  • solvents such as alcohols such as: ethanol, ethanol, butanol, amyl alcohol, cyclohexanol, benzyl alcohol, chlorohydin, henols such as: phenol, methyl and methoxyphenols, aldehydes such as: formaldehyde, chloral, lercaptans such as: buthyl mercaptan, benzyl mercaptan, Thioglycolic acid, organic acids de: formic acid, acetic acid, chloroacetic acid, amines such as ammonia, hydrazine, hydrotope solvents such as: eg conc. Solutions of sodium benzoate, others such as: Benzenes, pyridines, dioxane, ethyl acetoacetate, other basic solvents such as OH7H 2 O, or off / alcohols etc.
  • the process according to the invention can be used not only in the delignification (bleaching) of sulfate, sulfite, organosolve, etc.
  • Cellulose and wood pulp are used, but also in the production of cellulose in general, whether from wood or annual plants, if defibrillation by the usual cooking methods (possibly connected with mechanical processes or pressure), i.e. a very gentle cooking up to kappa numbers, which can be in the range of approx. 50 - 120 kappa, is guaranteed.
  • the treatment with the oxidation and bleaching system according to the invention can be carried out once or repeated several times, either before and / or after washing and extracting the treated material with NaOH etc. or without these intermediate steps also before and / or after pre-treatment and / or post-treatment steps such as acid washing, acid treatments for the removal of hexenuronic acids, Q stages, alkaline leaching, bleaching stages: such as peroxide bleaching, O 2 - reinforced peroxide stages, pressure peroxide stages, 02 delignification, Cl 2 bleach, 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 treatments with
  • xylanase xylanase, mannanase etc.
  • amylases and / or pectinases and / or proteinases and / or lipases and / or amidases and / or oxidoreductases such as laccases and / or peroxidases etc. or several combined treatments.
  • Solutions A and B are added together and made up to 33 ml.
  • the substance is incubated at 45 ° C for 1 - 4 hours in a shaking water bath with gentle shaking.
  • the kappa number is determined.
  • the substance is incubated at 45 ° C for 1 - 4 hours in a shaking water bath with gentle shaking.
  • the kappa number is determined.
  • Solutions A and B are added together and made up to 33 ml.
  • the substance is incubated at 45 ° C for 1 - 4 hours in a shaking water bath with gentle shaking.
  • 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. Then the substance is incubated at 45 ° C for 1 - 4 hours in a shaking water bath with gentle shaking.
  • the substance is incubated at 45 ° C for 1 - 4 hours in a shaking water bath with gentle shaking.
  • the kappa number is determined.
  • 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. Then the substance is incubated at 45 ° C for 1 - 4 hours in a shaking water bath with gentle shaking.

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Wood Science & Technology (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Biochemistry (AREA)
  • Microbiology (AREA)
  • Health & Medical Sciences (AREA)
  • Emergency Medicine (AREA)
  • Paper (AREA)
  • Detergent Compositions (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

L'invention concerne un système d'oxydation et/ou de blanchiment composé : a) d'oxydo-réductases telles que des laccases et/ou des peroxydases utilisées individuellement ou en combinaison en présence de leurs cosubstrats respectifs 02, H202, de peroxydes organiques, de peracides, etc. pour l'activation de composés de la famille des oxocarbones, de la famille des urazoles et des hydrazides, de la famille des hydantoïnes et de la famille des composés (cyan) nitriles et b) de composés carbonyles supplémentaires (cétones, aldéhydes) pouvant former avec les composés activés des espèces oxygénées actives telles que des dioxyranes, des dioxétanes, des composés peroxy etc. et d'autres composés réactifs ou états de transition tels que des radicaux, des radicaux cations, des radicaux anions ou des composés neutres réactifs (redox-actifs).
EP03704246A 2002-01-26 2003-01-26 Nouvelles activites catalytiques d'oxydo-reductases pour l'oxydation et/ou le blanchiment Withdrawn EP1483442A2 (fr)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
DE10203135A DE10203135A1 (de) 2002-01-26 2002-01-26 Neue katalytische Aktivitäten von Oxidoreduktasen zur Oxidation und/oder Bleiche
DE10203135 2002-01-26
PCT/DE2003/000201 WO2003061550A2 (fr) 2002-01-26 2003-01-26 Nouvelles activites catalytiques d'oxydo-reductases pour l'oxydation et/ou le blanchiment

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EP1483442A2 true EP1483442A2 (fr) 2004-12-08

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US (1) US20060054290A1 (fr)
EP (1) EP1483442A2 (fr)
AU (1) AU2003206637A1 (fr)
CA (1) CA2514475A1 (fr)
DE (1) DE10203135A1 (fr)
WO (1) WO2003061550A2 (fr)

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FI122175B (fi) * 2003-12-23 2011-09-30 Teknologian Tutkimuskeskus Vtt Menetelmä kuitutuotteen valmistamiseksi
FI121892B (fi) * 2003-12-23 2011-05-31 Teknologian Tutkimuskeskus Vtt Menetelmä kuituyhdistelmätuotteiden valmistamiseksi
FI117439B (fi) * 2003-12-23 2006-10-13 Valtion Teknillinen Menetelmä kuitukoostumuksen valmistamiseksi
DE102004020355A1 (de) * 2004-04-26 2005-11-10 Call, Krimhild Oxidative, reduktive, hydrolytische und andere enzymatische Systeme zur Oxidation, Reduktion, zum Coaten, Koppeln und Crosslinken von natürlichen und künstlichen Faserstoffen, Kunststoffen oder anderen natürlichen und künstlichen Mono- bis Polymerstoffen
ES2282020B1 (es) * 2005-07-06 2008-10-01 Consejo Superior Investigaciones Cientificas Sistema enzima-mediador para el control de los depositos de pitch en la fabricacion de pasta y papel.
WO2008076738A2 (fr) * 2006-12-18 2008-06-26 Novozymes North America, Inc. Détoxification de matériaux prétraités contenant de la lignocellulose
WO2008117523A1 (fr) * 2007-03-23 2008-10-02 Nippon Soda Co., Ltd. Agent antiviral
ES2428132T3 (es) * 2008-05-13 2013-11-06 Arkema Inc. Activadores de peróxido de un complejo de metalocarbeno
EP2163606A1 (fr) * 2008-08-27 2010-03-17 The Procter and Gamble Company Composition de détergent comportant de l'oxydase de gluco-oligosaccharide
US20110278223A1 (en) * 2008-11-18 2011-11-17 Delozier Gregory Enzyme-Assisted Effluent Remediation
US8691340B2 (en) 2008-12-31 2014-04-08 Apinee, Inc. Preservation of wood, compositions and methods thereof
FI122278B (fi) * 2009-09-11 2011-11-15 Upm Kymmene Corp Menetelmä inkjetmustepitoisten suspensioiden siistaamiseksi
EP2386681A1 (fr) * 2010-05-14 2011-11-16 Universitat Politècnica de Catalunya Procédé de recyclage de vieux papiers, produit ainsi obtenu et ses utilisations
BR112012033774B1 (pt) * 2010-07-01 2021-08-17 Novozymes A/S Método para branqueamento de polpa, composição de branqueamento, e, uso da composição
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RU2767004C1 (ru) * 2021-03-11 2022-03-16 федеральное государственное бюджетное образовательное учреждение высшего образования "Казанский национальный исследовательский технологический университет" (ФГБОУ ВО "КНИТУ") Способ получения целлюлозы
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Publication number Publication date
DE10203135A1 (de) 2003-07-31
US20060054290A1 (en) 2006-03-16
WO2003061550A2 (fr) 2003-07-31
WO2003061550A3 (fr) 2004-09-10
CA2514475A1 (fr) 2003-07-31
AU2003206637A1 (en) 2003-09-02

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