WO1998059108A2 - Systeme d'oxydation et de blanchiment comportant des agents d'oxydation produits par action enzymatique - Google Patents

Systeme d'oxydation et de blanchiment comportant des agents d'oxydation produits par action enzymatique Download PDF

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Publication number
WO1998059108A2
WO1998059108A2 PCT/DE1998/001689 DE9801689W WO9859108A2 WO 1998059108 A2 WO1998059108 A2 WO 1998059108A2 DE 9801689 W DE9801689 W DE 9801689W WO 9859108 A2 WO9859108 A2 WO 9859108A2
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Prior art keywords
acid
concentration
enzyme
component
enzyme component
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PCT/DE1998/001689
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German (de)
English (en)
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WO1998059108A3 (fr
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Hans-Peter Call
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Blume, Hildegard
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Priority to EP98936232A priority Critical patent/EP1012376A2/fr
Priority to CA002335253A priority patent/CA2335253A1/fr
Publication of WO1998059108A2 publication Critical patent/WO1998059108A2/fr
Publication of WO1998059108A3 publication Critical patent/WO1998059108A3/fr

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    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08H—DERIVATIVES OF NATURAL MACROMOLECULAR COMPOUNDS
    • C08H6/00—Macromolecular compounds derived from lignin, e.g. tannins, humic acids
    • 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
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/04—Carboxylic acids or salts thereof
    • 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
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • 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
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, 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
    • 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
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/39—Organic or inorganic per-compounds
    • C11D3/3902—Organic or inorganic per-compounds combined with specific additives
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
    • D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
    • D06L4/10—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen
    • D06L4/12—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen combined with specific additives
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
    • D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
    • D06P5/02—After-treatment
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
    • D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
    • D06P5/13—Fugitive dyeing or stripping dyes
    • D06P5/137—Fugitive dyeing or stripping dyes with other compounds
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
    • D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
    • D06P5/15—Locally discharging the dyes
    • D06P5/158—Locally discharging the dyes with other compounds
    • 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
    • D21C5/00—Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/02—Working-up waste paper
    • D21C5/025—De-inking
    • D21C5/027—Chemicals therefor
    • 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
    • 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
    • D21C9/16—Bleaching ; Apparatus therefor with per compounds
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02W—CLIMATE CHANGE MITIGATION TECHNOLOGIES RELATED TO WASTEWATER TREATMENT OR WASTE MANAGEMENT
    • Y02W30/00—Technologies for solid waste management
    • Y02W30/50—Reuse, recycling or recovery technologies
    • Y02W30/64—Paper recycling

Definitions

  • Acetone as the simplest ketone, can produce dimethyldioxirane.
  • other ketones are used instead of acetone.
  • Dioxiranes can also be produced as a pure substance before use as an oxidizing agent, but stability is problematic (WO 92/13993).
  • the aim of the present invention is to provide a very selective oxidation or bleaching system for use in cellulose bleaching or wood pulp bleaching, for use in the oxidative treatment of waste water of all kinds, for use in the production of wood composites, for use as an enzymatic deinking system , for use as an oxidative agent in organic synthesis, for use in coal liquefaction, for use as a bleaching system in detergents, for use as a bleaching agent or oxidizing agent in the textile industry (e.g. stone washing and bleaching of fabrics) , which does not have many of the disadvantages of purely chemical systems (e.g. environmental problems) or enzymatic systems (often underperformance and high costs).
  • oxidizing agent (s) responsible can be, for example, the dioxiranes formed from the ketones + the peracids formed, which then either alone for the above-mentioned applications as oxidizing agents or bleaching agents or in combination with the peracids formed.
  • an enzyme component system which contains one or more lipases, preferably from the group of triacylglycerol lipases (3.1.1.3) or one or more amidases, preferably from the Gr uppe of amidases (3.5.1.4) (system components 1), which consists of one or more fatty acids present (preferred are C 6 to C 26 , particularly preferred C 8 to C 6 fatty acids) (system component 2), and under Presence of oxidizing agents such as peroxides, preferably H 2 O 2
  • ECS enzyme component system
  • System component 3 on the formation of peracids from ketones present as a further component (system component 4) e.g. Can produce dioxiranes.
  • Binders / adhesives and wood composites IV) use as an enzymatic deinking system, V) Use as an oxidation system in organic synthesis VT) Use in coal liquefaction VH) Use as a bleach in detergents Vm) Use in bleaching / decolorization of textile fabrics.
  • 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 (HS03) 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 (Hokschliff) or with refiners (TMP), which defibrilize the wood after appropriate pretreatment (chemical, thermal or chemical-thermal). These wood materials still contain a large part of the lignin. You will v. a. used for the production of newspapers, magazines, etc.
  • Biopulping is the treatment of wood chips with living ones
  • Another advantage is the mostly existing improvement in the mechanical properties of the fabric, a disadvantage the poorer final whiteness.
  • the goal here is to reduce cooking chemicals, improve cooking capacity and "extended cooking”. As an advantage, improved kappa reduction after cooking compared to cooking without pretreatment is also achieved.
  • Biobleaching also works with in-vivo systems.
  • the boiled pulp (Softwood / Hardwood) is inoculated with the fungus before bleaching and treated for days to weeks. Only after this long treatment period is a significant one shown Lowering the kappa number and increasing the whiteness, making the process uneconomical for implementation in the usual bleaching sequences.
  • a further application is the treatment of chemical waste from sewage fabric, in particular bleaching water, to decolorize it and to reduce the AOX (reduction of chlorinated compounds in the waste water which cause chlorine or chlorine dioxide bleaching stages.
  • AOX reduction of chlorinated compounds in the waste water which cause chlorine or chlorine dioxide bleaching stages.
  • hemicellulases and xylanases are known To use mannanases as "bleach boosters".
  • the application PCT / EP87 / 00635 describes a system for removing lignin from hgnincellulose-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.
  • 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 expansion, 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) yields the best results in the expansion.
  • HBT has several disadvantages:
  • an enzyme component system (ECS) according to the invention which contains 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) (system components 1), which consists of one or more fatty acids present (preferred are C ⁇ to C 26 -, particularly preferably C 8 to C !
  • system component 2 6 - fatty acids
  • system component 3 oxidizing agents such as peroxides , preferably H 2 O 2 (system component 3) via the formation of peracids from ket as a further component onen (system component 4) can produce dioxiranes, for example.
  • 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.
  • suitable substances such as Polymerize lignins, i.e. Enlarging the corresponding molecules by means of "coupling reactions" can be used, for example, to treat humid waste water from the paper industry, such as TMP waste water (waste water from the production of thermomechanical pulp using refiners) and grinding mill waste water from wood pulping 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 (polymerized lignin) can be removed by appropriate treatments (flocculation, fuming e.g. with aluminum umbilfat / sodium aluminate, possibly with the addition of polyelectrolytes / cationic or anionic or sedimentation).
  • the wastewater then has a significantly reduced COD. It therefore causes a lower environmental impact when it is discharged, or increases the security of remaining below the permitted COD exposure limits, which, above all, in a "driving style" at the limit, which is often the FaU, is important.
  • an enzyme component system which contains 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) (system components 1), which consists of one or more fatty acids present (preferred are C 6 to C_ 6 -, particularly preferably C 8 to C ⁇ 6 - fatty acids) (system component 2), and also in the presence of oxidizing agents such as peroxides, preferably HO 2 (system component 3) via the formation of peracids from ketones present as a further component (system component 4) eg can produce dioxiranes.
  • ECS enzyme component system
  • polymerization catalysts is also provided here.
  • 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:
  • Butylphenol also particularly preferred are substances which have several hydroxyl groups, such as: Eagic acid, GaUuic acid, GaUein, GaUangin, Myo-Inositol, Morin, Nitranoic acid, Phenolphthalein, Purpurin, PurpurogaUin, Quinizarin, Chrysazin, Quercitin, Quinhydron, Chloranilklare, Carmin, Rhodizonic acid, Croconsonic acid Melhtic acid, hematoxin, 9-phenyl-2,3,7-trihydroxy-6-fluorene, 9-methyl-2,3,7-trihydroxy-6-fluorene, tetrahydroxy-p-benzoquinone, 2,2'4,4 ' -Tetra-hydroxybenzophenone, PyrogaUol Red, 1-nitrophloroglucinol, 1,4-dihydroxyanthraquinone, 5,8-dihydroxy-1,4-naphthoquinone, hexaoxo
  • the present invention aims to provide a process for the enzymatic polymerization and / or modification of lignin or lignin-containing materials, e.g. for use in the manufacture 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).
  • an enzyme component system (ECS) according to the invention which contains 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) (Systemkomponene 1), which are preferably made of one or more fatty acids present (C 6 to C_ 6 -, more preferably C 8 to C I ⁇ - fatty acids) (system component 2), and in the presence of oxidizing agents such as peroxides , preferably H 2 O 2 (system component 3) via the formation of peracids from ketones present as a further component (Sys component 4) can produce dioxiranes, for example
  • 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. ) and then the pH value is shifted below pH 7, depending on the optimal active pH range of the enzyme component system (ECS) or in the case of an alkaline active optimum of the enzyme component system, the combination of ECS and lignin and / or lignin-containing material immediately without pretreatment.
  • ECS enzyme component system
  • 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 enzyme component system and lignin and or lignin-containing material described thus serves mainly 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 binding agent, which then, combined with the wood fibers and / or wood parts to be joined (to be glued), under the action of pressure and elevated temperature solid wood composite parts such as the above-mentioned wood materials, e.g. Can harden "fiber boards" or "particle boards".
  • the main advantage lies in the reduction or saving of normally e.g.
  • Urea-formaldehyde resins used in the production of chipboard for "gluing" which, in addition to toxicological concerns, are only partially moisture-resistant or phenol-formaldehyde resins which have an unfavorable quenching behavior and long pressing times (again in addition to the toxicological question).
  • ECS enzyme component system
  • waste paper The goal is the removal of ink and other color particles from waste paper, the so-called "household collectibles", which mainly consists of newspapers and illustrated, are used as waste paper.
  • the first stage of treatment serves primarily for the mechanical / chemical removal of the
  • the fatty acid serves as a so-called collector of the color particles, in the second
  • 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.
  • the enzyme component system (ECS) according to the invention exceeds the efficiency of the other enzymatic deinking systems, in particular with oxidoreductases and in the case of lignin-containing deinking agent, by a suitable selection of the components and, above all, partially improves the advantage of the bleaching action of the purely chemical systems compensated, that is, a system can be made available that can offer the possibility of environmentally friendly deinking at neutral pH, thereby better re-bleachability, better material properties etc.
  • an enzyme component system which contains one or more lipases, preferably from the group of triacylglycerol phases (3.1.1.3) or one or more amidases, preferably from the group of amidases (3.5.1.4) (system component 1), contains which e from one or more fatty acids present (preferred are C 6 to C 26 -, particularly preferably C 8 to C i6 - fatty acids) (system component 2), and in the presence of oxidizing agents such as peroxides, preferably HO (system component 3) via the addition of Can produce peracids from ketones (system component 4) present as a further component, for example dioxiranes.
  • ECS enzyme component system
  • 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 possible structure of hard coal shows a three-dimensional network of polycyclic, aromatic ring systems with a "certain" similarity to lignin structures.
  • chelate substances siderophores such as ammonium oxalate
  • biosurfactants are assumed to be cofactors.
  • coal liquefaction systems are known as in vivo systems (with kgnin-degrading organisms, especially white rot fungi), or systems with oxidoreductases plus mediators (laccase mediator system -> WO 94/29510; WO 96/18770.
  • a enzyme component system (ECS) according to the invention is available, which has one or more lipases, preferably from the group of triacylglycerol phases (3.1.1.3) or one or more amidases, preferably from the group of amidases (3.5.1.4) (system components 1), which consists of one or more fatty acids present (preferred are C 6 to C 2 6, particularly preferably C 8 to C i6 fatty acids) (system component 2), and in the presence of oxidizing agents such as peroxides, preferably H 2 O 2 (system component 3) on the formation of peracids from ketones (system component 4) present as a further component, for example dioxirane e can produce.
  • ECS enzyme component system
  • 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.
  • TAED and SNOBS chemical bleach activators
  • WO 1/05839 describes the use of various oxidizing enzymes (oxidases and peroxidases) to prevent dye transfer.
  • peroxidases are able to add different pigments (3-hydroxyflavone and betaine by horseradish peroxidase, carotene by peroxidase) "Discolor".
  • 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 dyed substrate into a non-dyed, oxidized substance).
  • the enzyme thus compares to, for example, hypochlorite, which also contains the dye attacks on or in the tissue, have the advantage of decolorizing only the dye present in solution, with hydrogen peroxide or a corresponding precursor or in situ generated hydrogen peroxide being involved in the catalysis of the decolorization.
  • the enzyme reaction can be done, in part, 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.
  • 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.
  • metal ions such as Mn ⁇
  • halide ions such as Cl " or Br "
  • organic phenols such as p-hydroxycinnamic acid and 3,4-dichlorophenol.
  • 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 residues defined in each case.
  • AUe 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 sector.
  • the combination of these enhancer substances are limited to peroxidases.
  • the use of mixtures containing peroxidases is also known from WO 92/18687.
  • a special system consisting of oxidases and substrates suitable for this purpose and hydrogen peroxide is described in DE-OS 42 31 761.
  • DE-OS 19 18 729 relates to a further special detergent system consisting of glucose and glucose oxidase or starch,
  • Amyloglucosidase and glucose oxidase as well as an additive consisting of hydroxylamine or hydroxylamine compounds, the hydroxylamine or its derivatives serving to inhibit the frequently occurring catalase in GOD and has in no way been described as a mediator additive.
  • WO 94/29425, DE 4445088.5 and WO 97/48786 contain multi-component bleaching systems for use with wash-active substances consisting of oxidation catalysts and oxidizing agents and also aliphatic, cycloahphatic, heterocyclic or aromatic compounds containing NO, NOH or H-NR-OH.
  • a Enzyme component system (ECS) according to the invention which has one or more lipases, preferably from the group of triacylglycerol phases (3.1.1.3) or one or more amidases, preferably from the group of amidases (3.5.1.4) (system component 1), which consists of one or more fatty acids present (preferred are C 6 to C 26 -, particularly preferably C 8 to C j 6 - fatty acids) (system component 2), and in the presence of oxidizing agents such as peroxides, preferably H 2 O 2 (system component 3) via the formation of peracids from ketones (system component 4) present as a further component, for example dioxiranes.
  • VUi) Use of the enzyme component system (ECS) according to the invention is available which has one or more lipases, preferably from the group of triacylglycerol phases (3.1.1.3) or one or more amidases, preferably from the group of amidases (3.5.1.4)
  • system component 1 which consists of one
  • Enzymes are used today in increasing quantities and for various applications in the textile industry.
  • amylases plays a major role in the "desizing process"
  • RoUe which can prevent the use of strong acids, alkalis or oxidizing agents.
  • CeUulases are also used for so-called bio-pohshing 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 methods for enzymatic expansion, in which enzymes are used together with mediators.
  • mediators are general
  • Enzymes peroxidases, laccases
  • enzyme-enhancing hetero
  • oxidoreductases mainly laccases, but also peroxidases have recently been used for the treatment of mainly denim jeans.
  • 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.
  • the dyes normally used in jeans denim are VAT dyes such as indigo, or indigo derivatives such as Thioindigo, but also so-called sulfure dyes.
  • the present invention has set itself the goal of the night-time of the conventional processes: stone washing / bleaching after stone-washing or actual bleaching of dyed and / or undyed textile fabrics: above all environmental problems and fiber damage and also the night-time of the known oxidoreductase / enhancer systems (e.g. NO radicals etc.) to be minimized or remedied.
  • the known oxidoreductase / enhancer systems e.g. NO radicals etc.
  • a enzyme component system (ECS) according to the invention exceeds the performance of the above-mentioned oxidoreductase mediator systems and does not have the above-mentioned night-time effects of the prior art, ie the above object is achieved by a enzyme component system (ECS) according to the invention is available, which has one or more lipases, preferably from the group of triacylglycerol phases (3.1.1.3) or one or more amidases, preferably from the group of amidases (3.5.1.4) (system components 1), which consists of one or more fatty acids present (preferred are C ⁇ to C 26 -, particularly preferably C 8 to C i 6 - fatty acids) (system component 2), and in the presence of oxidizing agents such as peroxides, preferably H 2 O 2 (System component 3) can produce eg dioxiranes via the formation of peracids from ketones (system component 4) present as a further component.
  • system components which has one or more lipases, preferably
  • Enzymes of group 3 (hydrolases) 3.1, 3.1.1, 3.1.2, 3.1.3, 3.1.4 and 3.1.7 are preferred in accordance with the International Enzyme Nomenclature: Committee of the International Union of Biochemistry and Molecular Biology (Enzyme Nomenclature, Academic Press, Inc., 1992, pp. 306-337).
  • Enzymes which act on ester bonds are preferred (3.1), in particular those which act on carboxyl esters (3.1.1):
  • N-acetylglucosaminylphatatylinositol deacetylase 3.1.1.70 cetraxate benzyl esterase are also preferred:
  • lipases triacylglycerol lipases, triglycerol acyl hydrolases
  • organisms such as Candida antarctica, Candida rugosa, Candida hpolytica, Candida cylindracae, Candida spec, Geotrichum candidum, Humicula lanuginosa, PeniciUium robertiiufusumium, asbertiufusii, cambertq, peniculumium, asciferii, peniculium, are particularly preferred spec, Mucor javanicus, Mucor mehei, Rhizopus arrhizus, Rhizopus niveus, Rhizopus delamar, Rhizopus spec. Chromobacterium viscosum, Pseudomonas cepacia, Pseudomonas spec, from wheat germ or pancreas (pork or other queues).
  • This subclass includes enzymes that can cleave amides, amidines, and other C / N bonds. Particularly preferred are enzymes of class: 3.1.1, which act on linear amides, class: 3.5.2, which act on cych amides, class 3.5.3, which act on linear amidines, class 5.3.4, on cycüsche amidines act, class 3.5.5, which act on nitriles and class 3.5.99, which act on other compounds.
  • Class 3.5.1 enzymes which act on linear amides are particularly preferred, such as:
  • class 3.5.3 enzymes which are linear
  • Enzymes of class 3.5.4 which act on cych amidines are also particularly preferred, such as:
  • class 3.5.99 enzymes which act on other compounds, such as: 3.5.99.1 riboflavinase 3.5.99.2 thiaminase Enzymes of class 3.5.5.1 nitrilase (3.5.5.2 - 3.5.5.6, other nitrilases) are particularly preferred.
  • Enzymes of class 3.5.1 here in particular of class 3.5.1.4 amidases, are also particularly preferred.
  • Fatty acids which are used as peracid queues in the process according to the invention are, for example:
  • Nonanoic acid (pelargonic acid) decanoic acid (capric acid)
  • Nonadecanoic acid eicosanoic acid (arachic acid)
  • Tetracosanoic acid pentacosanic acids
  • Triacotanoic acid (Mehssinklare) 2) unsaturated fatty acids
  • 10-udecenoic acid 9c-dodecenoic acid (lauroleic acid) 9c-tetradecenoic acid (myristoleic acid) 9c-hexadecenoic acid (palmitoleic acid) 6c-octadecenoic acid (petroselinic acid) 6t-octodecenoic acid (petroselaidic acid) 9c-octodecenoic acid (oleic acid) 9t-octodecenoic acid (elaidic acid)
  • Tetradecanoic acid (myristic acid) and dodecanoic acid (lauric acid) are particularly preferred.
  • Peroxid (H 2 O 2 ), organic peroxides and per compounds such as: perborates, persulphates, percarbonates, perphosphates, percarbamides, perchlorates and others are preferred as oxidizing agents in the enzyme component system according to the invention.
  • Preferred organic peroxides are, for example:
  • 3-chloroperoxibenzoic acid monoperoxyphthalic acid Mg salt, di-tert-butyl peroxide, cumene hydroperoxide, lauroyl peroxide, chloroperoxybenzoic acid, dicumyl peroxide, ethymethyl ketone peroxide, benzoyl peroxide, diperoxidodecanedioic acid Na salt, etc.
  • activators such as TAED (tetraacetylethylene diamine), TAGU (tetraacetyl glycoluril) and iso-NOBS can also be used in detergents
  • H 2 O 2 -generating systems are used for the corresponding lipase effect.
  • substances such as nitrilamines or dicyandiamines, or ions from metals, such as Mo 6+ , Va 5+ and W 6 *, are used together with peroxides such as H 2 O 2 .
  • Carbonyl compounds of general formula I are particularly preferred.
  • 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 ⁇ ) and 1,3-diketones (formula m) or polyketones (polyketides) and the tautomeric enols (formula IV) are particularly preferred,
  • radicals R 3 to R 6 can each be the same or different and can represent ahphatic 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. The possibility of tautomerization or the exhaustion of a resonance hybrid is of particular importance.
  • ketones such as, in general, hydroxyketones, ⁇ , ⁇ -unsaturated ketones, oxicarboxylic acids, quinones and halogen ketones are particularly preferred. The following are particularly preferred:
  • Benzoylpropionic acid benzyhdenoacetophenone, cyclohexylphenyl ketone, deoxybenzoin, 4 ', 4'-dimethoxybenzü, l, 3-diphenyl-l, 3-propanedione, O-ethylbenzoin, ethyl-benzoylacetate, ethyl- (phenylglyoylate), 4'-hydroxypropiophen -Indanedione, 1-indanone, isopropylphenyl ketone, 6-methoxy-1,2,3,4-tetrahydro-naphthalen-1-one, methylphenylglyoxylate, phenylglyoxylonitrile, l-phenyl-l, 2-propanedione-2-oxime, propiophenone , Valerophenone, 2-acetyl- ⁇ -butyrolactone, 2-acetylpyrroL l-benzyl
  • 3-methyl-2-oxo-valeric acid 4-methyl-2-oxo-valeric acid, methyl-phenylglyoxylate, 2-oxobutyric acid, 2,3-pentanedione, 9,10-phenanthrenequinone, acetoacetanide, 2-acetyl- ⁇ -butyric acid lactone, 2-acetylcyclopentanone, AUyl acetoacetate, benzoylacetone, ter-butylacetoacetate, 1,3-cyclopentanedione, diethyl-3-oxoglutarate, dimethyl-acetylsuccinate, dimethyl-3-oxoglutarate, l, 3-diphenyl-l, 3-propanedione, ethyl acetoacetate, ethyl benzoyl acetate, ethyl butyrylacetate, ethyl 2-oxocyclohexane carboxylate, ethyl 2
  • Dimethyl succinate dimethyl terephthalate, ethylene glycol diacetate.
  • Anhydrides such as: benzoic anhydride, benzene-1, 2,4,5-tetracarboxylic acid-1, 2,4,5-dianhydride, 3,3 ', 4,4'-benzophenone tetracarboxylic acid anhydride, succinic acid anhydride, butyric acid anhydride, crotonic acid anhydride, ice cream 1,2-cyclohexanedicarboxylic anhydride, di-tert-butyl dicarbonate, dimethyl dicarbonate, dodecenyl succinic anhydride.
  • Epicon B4400 Acetic anhydride, glutaric anhydride, hexanoic anhydride, isato acid anhydride.
  • Isobutyric anhydride isovaleric anhydride, maleic anhydride, naphthalene-1,8-dicarboxylic acid anhydride, 3-nitrophthalic anhydride, 5-norborene-2,3-dicarboxylic acid anhydride, phthalic anhydride, 2.phenylbutyric anhydride, pivalic anhydride, tivalic anhydride, propionic 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 are particularly preferred - (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'-dimethoxybenzophenone, 2,2 ', 4,4' tetrahydroxybenzophenone, 2-chlorobenzophenone.
  • Figure 1 shows schematically a possible reaction cycle of components:
  • enzyme preferably lipase from, for example, Humicola lanuginosa
  • ECS enzyme component system
  • zeolite preferably 0.05 mg to 2 mg enzyme per g ZeUstoff (corresponding to about 250 to 10000 IU per g ZeUstoff) used (1 IU hydrolyzes 1 ⁇ e equivalent of fatty acid from a triglyceride in 1h at pH 7.7 and 37 ° C).
  • the expansion (bleaching) is preferably carried out by the enzyme component system according to the invention in the presence of oxygen or air at normal pressure to slight O 2 pressure and in a pH range from 2 to 11, preferably pH 3-9, at a temperature of 20 to 95 ° C, preferably 40 - 95 ° C, and a consistency of 0.5 to 40%.
  • a finding that is unusual and surprising for the use of enzymes in the bleaching of zeolites is that when the enzyme component system according to the invention is used, an increase in the consistency enables a significant increase in the kappa reduction.
  • a process according to the invention is preferably carried out at consistencies of 4 to 35%, particularly preferably 4 to 15%.
  • H 2 O 2 is preferably added as an oxidizing agent in a concentration of 0.05 to 20 mg per g of ZeUstoff (100% goods), preferably 0.05 to 10 mg per g ZeUstoff.
  • Another factor is fatty acids in one or more, preferably C 6 to C 26 , particularly preferably C 8 to C 6 , very particularly preferably tetradecanoic acid or dodecanoic acid in a concentration of 0.05 to 20 mg per g of zeolite, preferably in a concentration of 0.05 up to 10 mg per g of ZeUstoff used.
  • ketones preferably, for example, benzophenones in a concentration of 0.05 to 20 mg per g of zeolite, preferably in a concentration of 0.05 to 10 mg per g zeolite.
  • the enzyme component system according to the invention is used in a method for treating lignin, for example, by mixing the selected components at the same time or in a fixed order with an aqueous suspension of the quinine-containing material. The reaction is preferably started by adding the oxidizing agent or the enzyme.
  • the bleaching system can additionally contain phenolic compounds and / or non-phenolic compounds with one or more benzene nuclei, which in particular can serve the better "oxidation transfer” (redox cascade) and / or the trapping of radicals, which could possibly lead to polymerization of the lignin.
  • phenolic compounds and / or non-phenolic compounds with one or more benzene nuclei which in particular can serve the better "oxidation transfer" (redox cascade) and / or the trapping of radicals, which could possibly lead to polymerization of the lignin.
  • H 2 O oxidizing agent
  • oxygen possibly in addition to H 2 O 2
  • organic peroxides per compounds such as sodium perborate and / or sodium percarbonate
  • persulfates and others possibly together with activators such as TAED, nitrilamines, dicyandiamides etc.
  • Oxygen can also be generated in situ by H 2 O 2 + catalase or the like, or H 2 O 2 can be generated in situ from GOD + glucose or the like.
  • ECS enzyme component system
  • Components still contain Mg2 + ions.
  • the Mg ⁇ + ions can be used for example as a salt, such as MgSO.
  • the concentration is in the range of 0.1-2 mg / g hgnin-containing material, preferably 0.2-0.6 mg / g.
  • a further increase in the effectiveness of the enzyme component system (ECS) according to the invention can be achieved in that the system, in addition to the Mg2 + ions, also complex compounds, such as, for example, ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), hydroxyethylenediamine triacetic 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 material containing hgnin, preferably 1-3 mg.
  • an acidic wash pH 2 to 6, preferably 2 to 5) or Q stage (pH 2 to 6, preferably 2 to 5) before the ECS stage caused a considerable decrease in the kappa number in some substances Comparison to treatment without this specific pretreatment leads.
  • the substances commonly used for this purpose such as EDTN DTPA
  • they are preferably used in concentrations of 0.1% / to 1% / to, particularly preferably 0.1% / to 0.5% / to.
  • reducing agents can be added which, together with the existing oxidizing agents, serve to control a certain redox potential.
  • Sodium bisulfite, sodium dithionite, ascorbic acid, thio compounds, mercapto compounds or glutathione etc. can be used as reducing agents.
  • radical scavengers or radical scavengers can 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 Fo ⁇ + ,
  • 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 are substances that simulate the prosthetic groups of (here) oxidoreductases and can catalyze oxidation reactions, for example.
  • NaOCl can also be added to the reaction mixture. In combination with hydrogen peroxide, this compound can form singlet oxygen.
  • 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.
  • Glucans, mannans, dextrans, levans, pectins, alginates or plant gums are to be mentioned in particular as polysaccharides and gelatin and albumin as proteins. These substances mainly serve as protective cooids for the enzymes.
  • proteases such as pepsin, bromelin, papain, etc. These can include serve to achieve better access to lignin by breaking down the extensin present in the wood (hydroxyproline-rich protein).
  • Amino acids simple sugars, oligomer sugars, PEG types of the most varied molecular weights, polyethylene oxides, polyethyleneimines and polydimethylsoxanes can be considered as further protective cooids.
  • substances can be added to the enzyme component system according to the invention which increase the hydrophobicity of the reaction medium and thus act queuously on the lignin in the fibers and thus increase its vulnerability.
  • substances are e.g. Glycols such as: propylene glycol, ethylene glycol, glycol ethers such as: ethylene glycol dimethyl ether etc. but also solvents such as alcohols such as:
  • Hydrotope solvents such as: eg conc. Solutions of sodium benzoate, others such as: benzenes, pyridines, dioxane, acetoacetic acid ethyl ester, other basic solvents such as OH7H 2 O or OHV alcohols and others
  • the process according to the invention can be used not only in the expansion (bleaching) of sulfate, sulfite, organosob / -, or the like pulps and of wood pulps, but also in the manufacture of zeolites in general.
  • the treatment with the enzyme component system (ECS) according to the invention can be carried out once or repeated several times, either before and / or after washing and extracting the treated substance with NaOH etc. or without these intermediate steps but also before and / or after pre-treatment and / or post-treatment steps such as acid washing, Q levels, alkaline leaching ,.
  • Bleaching levels such as peroxide bleaching, O 2 - reinforced peroxide levels, pressure peroxide levels, O 2 expansion, Cl 2 bleach, ClO bleach. Cl / ClO bleach, peracid bleaching stages, peracid-enhanced O 2 bleach / peroxide bleach, ozone bleach.
  • Dioxirane bleaching, reductive bleaching stages, other treatments such as: QueU stages, sulfonations, NO / NO 2 treatments, nitrosyl sulfuric acid treatment, enzyme treatments such as treatments with hydrolases such as CeUulases and / or HemiceUulases (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 laccases and / or peroxidases etc. or several combined treatments.
  • hydrolases such as CeUulases and / or HemiceUulases (e.g. xylanase, mannanase etc.) and / or amylases and / or pectinases and or proteinases and / or lipases and / or amidases and or oxidoreductases such
  • An O2 stage can also be used before the ECS treatment or, as already mentioned, an acid wash or Q stage (chelate stage) can be carried out.
  • Solutions A and B are added together and made up to 33 ml.
  • the substance is then placed in a reaction vessel preheated to 45 ° C. and under
  • the fabric is then washed over a nylon sieve (30 ⁇ m) and extracted for 1 hour at 60 ° C., 2% fabric density and 8% NaOH per g of fabric.
  • the kappa number is determined.
  • the substance is then placed in a reaction vessel preheated to 45 ° C. and under
  • the fabric is then washed over a nylon sieve (30 ⁇ m) and extracted for 1 hour at 60 ° C., 2% fabric density and 8% NaOH per g of fabric.
  • the kappa number is determined.
  • A) 20 ml of tap water are mixed with 1 mg of tetradecanoic acid, 5 mg of acetone, 2.5 mg of H 2 O 2 (30% product) and 0.5 mg of nitrile amine per g of ZeUstoff, the pH value with sulfuric acid and or sodium hydroxide solution so that after addition of the ZeUstoff and the enzyme pH 7.5 results.
  • the substance is then placed in a reaction vessel preheated to 45 ° C. and under
  • the fabric is then washed over a nylon sieve (30 ⁇ m) and extracted for 1 hour at 60 ° C., 2% fabric density and 8% NaOH per g of fabric.
  • Solutions A and B are added together and made up to 33 ml.
  • the substance is then placed in a reaction vessel preheated to 45 ° C. and under
  • the kappa number is determined.
  • the substance is then placed in a reaction vessel preheated to 45 ° C. and under
  • the fabric is then washed over a nylon sieve (30 ⁇ m) and extracted for 1 hour at 60 ° C., 2% fabric density and 8% NaOH per g of fabric.
  • the kappa number is determined.
  • B) 5 ml of tap water are mixed with 200 IU amidase from Pseudomonas aeruginosa (Sigma A 6691) (1 IU conversion of 1 ⁇ mol acetamide and hydroxylamine to acetohydroxamic acid and NH 3 per minute at pH 7.2 and 37 ° C.).
  • Solutions A and B are added together and made up to 33 ml. After adding the zeolite, it is mixed with a dough kneader for 2 min.
  • the substance is then placed in a reaction vessel preheated to 45 ° C. and under
  • the fabric is then washed over a nylon sieve (30 ⁇ m) and 1 hour at 60 ° C,
  • the enzyme component system (ECS) according to the invention can be used with a low dosage of polymerization catalysts.
  • enzyme preferably lipase from Aspergülus spec
  • ECS enzyme component system
  • enzyme preferably lipase from Aspergülus spec
  • concentration of 0.05 to 50 mg per liter of waste water preferably 0.05 mg to 10 mg enzyme per liter of waste water (corresponding to approx. 250 up to 50,000 IU per liter of waste water) (1 IU hydrolyzes 1 ⁇ e equivalent of fatty acid from a triglyceride in lh at pH 7.7 and 37 ° C).
  • the treatment of the grinding mill wastewater is preferably carried out by the enzyme component system according to the invention in the presence of oxygen or air at normal pressure to slight O overpressure and in a pH range from 2 to 11, preferably pH 3-6, at a temperature of 20 to 95 ° C, preferably 40 - 95 ° C carried out.
  • HO 2 is preferably added as the oxidizing agent in a concentration of 0.05 to 200 mg per liter of waste water (100% product), preferably 0.05 to 50 mg per liter of waste water.
  • a further factor is fatty acids in one or more, preferably C 6 to C 2 6, particularly preferably C g to Cj 6 , very particularly preferably tetradecanoic acid or dodecanoic acid in a concentration of 0.05 to 200 mg per liter of waste water, preferably in a concentration of 0.05 to 50 mg per liter of wastewater.
  • ketones preferably e.g. Benzophenones are used in a concentration of 0.05 to 200 mg per liter of waste water, preferably in a concentration of 0.05 to 50 mg per liter of waste water.
  • polymerization catalysts mostly phenolic substances or polycycles with several oxidizable hydroxyl groups, such as, for example, PurpurogaUin. These substances are used in a concentration of 0.005 to 200 mg per liter of waste water, preferably in a concentration of 0.005 to 50 mg per liter of waste water.
  • Example 4 To 190 ml grinding mill waste water after the water has risen to pH 6 and
  • Enzyme solution lipase (Aspergülus spec): 1mg in 0.1 ml water.
  • the wastewater is either only filtered, filtered and with 0.2% / 0.2% or 0.5% / 0.5% aluminum sulfate solution / sodium aluminate solution, each with a 10% by weight content compared to the untreated zero value.
  • the lignin which is normally present in the grinding water without treatment in the range from 600 to 900 mg lignin per liter, is quantified at 280 ⁇ m by photometric determination.
  • the reaction is continued for Ibis for 4 hours, preferably 2 hours. Then the wastewater is either only filtered, filtered and filled with 0.2% / 0.2% or 0.5% / 0.5% aluminum sulfate solution / sodium aluminate solution, each with 10% by weight compared to the untreated NuUwert.
  • the lignin which is normally present in the grinding water without treatment in the range from 600 to 900 mg lignin per liter, is quantified at 280 ⁇ m by photometric determination. The decrease in lignin is a measure of the COD reduction and the efficiency of the system. The results are summarized in Table 2.
  • the enzyme component system (ECS) according to the invention is used with little addition of polymerization catalysts.
  • Binder / wood fiber mixture may be desired by further enzyme-catalyzed reactions.
  • the lignin removal system from grinding mill waste water described above is used as a mode system, as mentioned above.
  • enzyme preferably lipase from Humicola lanuginosa
  • ECS enzyme component system
  • enzyme preferably lipase from Humicola lanuginosa
  • concentration of 0.05 to 50 mg per liter of waste water preferably 0.05 mg to 10 mg enzyme per liter of waste water (corresponding to approx. 250 to 50,000 IU per liter of waste water) (1 IU hydrolyzes 1 ⁇ e equivalent of fatty acid from a triglyceride in lh at pH 7.7 and 37 ° C).
  • the treatment of the grinding mill wastewater is preferably carried out by the enzyme component system according to the invention in the presence of oxygen or air at normal pressure to slight O overpressure and in a pH range from 2 to 11, preferably pH 3-6, at a temperature of 20 to 95 ° C, preferably 40 - 95 ° C carried out.
  • H 2 O 2 is preferably added as an oxidizing agent in a concentration of 0.05 to 200 mg per liter of waste water (100% product), preferably 0.05 to 50 mg per liter of waste water.
  • Another factor is fatty acids in one or more, preferably C 6 to C_6, particularly preferably C 8 to C 6 , very particularly preferably tetradecanoic acid or dodecanoic acid in a concentration of 0.05 to 200 mg per liter of waste water, preferably in a concentration of 0.05 to 50 mg per liter of wastewater used.
  • Another factor used is ketones, preferably, for example, benzophenones in a concentration of 0.05 to 200 mg per liter of waste water, preferably in a concentration of 0.05 to 50 mg per liter of waste water.
  • polymerization catalysts are used, mostly phenolic substances or polycycles with several oxidizable hydroxyl groups, here preferably e.g. PurpurogaUin.
  • These substances are used in a concentration of 0.005 to 200 mg per liter of waste water, preferably in a concentration of 0.005 to 50 mg per liter of waste water.
  • Ketone solution 1 mg 2,2 ', 4,4'-tetrahydroxybenzophenone in 1 ml water.
  • Polymerization catalyst 0.1 mg purple gallin in 0.1 ml water.
  • the reaction is started by adding solution 5) (oxidizing agent -> H 2 O 2 ); 3.3 mg of H 2 O 2 (30% product) in 0.1 ml of water are added and the volume is made up to 200 ml with preheated waste water. The reaction is continued for Ibis for 4 hours, preferably 2 hours. Then the wastewater is either only filtered, filtered and with 0.2% / 0.2% or
  • enzyme preferably lipase from Humicola lanuginosa
  • ECS enzyme component system
  • enzyme preferably lipase from Humicola lanuginosa
  • concentration of 5 to 500 mg per kg lutro waste paper preferably 5 mg to 100 mg enzyme per kg lutro waste paper (corresponding to approx. 25,000 to 500,000 IU per kg of waste paper) (1 IU hydrolyzes 1 ⁇ e equivalent of fatty acid from a triglyceride in 1h at pH 7.7 and 37 ° C).
  • the treatment of the waste paper to remove the dracky color particles is preferably carried out by the enzyme component system according to the invention in the presence of oxygen or air at normal pressure to slightly elevated pressure (maximum 2 bar) and in a pH range from 7 to 11, preferably pH 7-9 , carried out at a temperature of 20 to 95 ° C, preferably 40 - 95 ° C.
  • H 2 O 2 is preferably added as the oxidizing agent in a concentration of 5 to 5000 mg per kg of waste paper (100% goods), preferably 5 to 1000 mg per kg of waste paper.
  • a further factor is fatty acids in one or more, preferably C 6 to C 26 , particularly preferably C 8 to C_ 6 , very particularly preferably tetradecanoic acid or dodecanoic acid in a concentration of 5 to 2000 mg per kg of waste paper, preferably in a concentration of 5 up to 500 mg per kg of waste paper.
  • Another factor used is ketones, preferably, for example, benzophenones in a concentration of 5 to 2000 mg per kg of waste paper, preferably in a concentration of 5 to 500 mg per kg of waste paper.
  • the compounds mentioned above are used to increase the efficiency of the process, such as phenolic substances or polycycles with several oxidizable hydroxyl groups, preferably e.g. Bisphenol A
  • reducing agents are used, preferably Na dithionite or Na bisulfite in a concentration of 0.1 to 1000 mg per kg of waste paper, preferably in a concentration of 0.1 to 200 mg per kg of waste paper.
  • collectors preferably Incopur types, e.g. Incopur RSGA in a concentration of 1 to 5000 mg per kg of waste paper, preferably from 1 to 1000 mg per kg of waste paper.
  • further enzymes such as CeUulases and / or HemiceUulases (e.g. xylanase and / or mannanases etc.) and / or pectinases and / or oxiodoreductases can be added to increase the detachment effect in some waste paper compositions.
  • system components per kg lutro waste paper are: a) 500000 IU lipase from Humicola lanuginosa per 100 ml tap water, b) 0. lg dodecanoic acid per 100 ml tap water, c) 0. lg benzophenone per 100 ml tap water, d) 0. lg Bisphenol A per 20 ml 0.1 mol NaOH, e) 0.02g Na bisulfite per 10 ml tap water, f) 0.5g Incopur RSGA per 100 ml tap water, g) lg (30% product) H 2 O 2 per 100 ml tap water ( will be admitted last)
  • the pulper is added after adding the system components a to g during the addition of the
  • Waste paper started. Then the total amount of water is 15 kg with tap water at 45 ° C.
  • the pulping process is for
  • the pulp is then transferred to a holding vessel for further reaction and incubated at about 40-45 ° C for 15 to 45 minutes.
  • the accepted material is drained off and the soles made from it determine the ISO whiteness and brightness after drying in a commercially available sheet dryer.
  • Example 7 only water is used to control the enzyme component system (ECS) according to the invention.
  • ECS enzyme component system
  • the dough kneader is started after adding system components a to g while adding the waste paper. Then the total amount of water is 1.5 kg with tap water at approx. 45 ° C. The pulping process continues for 10 minutes.
  • the pulp is then transferred to a holding vessel for further reaction and incubated at about 40-45 ° C for 15 to 45 minutes.
  • the pulper is started while the waste paper is being added. Then with approx.
  • Pulping continues for 10 minutes. The pulp is then transferred to a holding vessel for further reaction and incubated at about 40-45 ° C for 15 to 45 minutes.
  • the accepted material is drained off and the soles made from it determine the ISO whiteness and brightness after drying in a commercially available sheet dryer.
  • Laccase 800000 IU / kg waste paper + bisphenol A + Na bisulfite (0.1 or 0.02g / kg waste paper), further conditions, see WO 91/14820; WO 92/20857 V) Use as an oxidation system in organic synthesis
  • ECS enzyme component system
  • the method according to the invention has the advantage of lower costs and better performance especially compared to these methods. also in terms of costs.
  • enzyme preferably lipase from e.g. Humicola lanuginosa, in a concentration of 0.05 to 5 mg per 10 mmolar substrate, preferably 0.05 mg to 3 mg per 10 mmolar substrate (corresponding to approx. 250 to 15000 IU) (1 IU hydrolyzes 1 ⁇ Equivalent fatty acid from a triglyceride in 1 h at pH 7.7 and 37 ° C).
  • the oxidation reaction is preferably carried out by the enzyme component system according to the invention in the presence of oxygen or air at normal pressure to slight O 2 overpressure and in a pH range from 2 to 11, preferably pH 3-9, at a temperature of 20 to 95 ° C, preferably 40-95 ° C, and a substrate concentration of 5 to 100 mmolar, preferably carried out at a substrate concentration of 5 to 50 mmolar.
  • H 2 O (100% product) is preferably added as an oxidizing agent in a concentration of 0.05 to 100 mg per 10 mmolar substrate, preferably 0.05 to 30 mg per 10 mmolar substrate.
  • a further factor is fatty acids in one or more, preferably C 6 to C 26 , particularly preferably C 8 to C i6 , very particularly preferably tetradecanoic acid or dodecanoic acid in a concentration of 0.05 to 100 mg per 10 mmolar substrate, preferably in a concentration of 0.05 to 30 mg per 10 mmolar substrate used.
  • Another factor used is ketones, preferably, for example, benzophenones in a concentration of 0.05 to 100 mg per 10 mmolar substrate, preferably in a concentration of 0.05 to 30 mg per 10 mmolar substrate.
  • Example 11 (Oxidation of Benzyl Alcohols to Aldehydes) The following components are added to 50 ml of 0.1 molar acetate buffer pH 4.5 in a 250 ml reaction vessel:
  • the reaction is started by adding 12.5 mg H O (30% product) and continued for 12 to 24 hours.
  • the reaction is started by adding 12.5 mg of H 2 O 2 (30% product) and continued for 12 to 24 hours.
  • Patent applications WO 94/29510 and WO 96/18770 have also shown the precise possibility of using fungus-free systems using oxidoreductases and special mediators.
  • Network of polycychic, aromatic ring systems of brown or hard coal can be detected.
  • enzyme preferably lipase from, for example, Humicola lanuginosa
  • ECS enzyme component system
  • enzyme preferably lipase from, for example, Humicola lanuginosa
  • a concentration of 0.05 to 20 mg per gram of dry lignite preferably 0.05 mg to 10 mg enzyme per gram of coal (corresponding to approx . 250 to 50,000 IU) (1 IU hydrolyzes 1 ⁇ e equivalent of fatty acid from a triglyceride in 1 h at pH 7.7 and 37 ° C).
  • Treatment of the coal by the enzyme component system according to the invention is preferred in the presence of oxygen or air at atmospheric pressure to slight O 2 overpressure and in a pH range from 2 to 11, preferably pH 3-9, at a temperature of 20 to 95 ° C, preferably 40-95 ° C, and a consistency of 0.5 to 40%.
  • a finding that is unusual and surprising for the use of enzymes is that when the enzyme component system according to the invention is used, an increase in the consistency enables a considerable increase in performance.
  • a method according to the invention is preferred for material densities of 4 to 35%. particularly preferably 4 to 15%.
  • the oxidizing agent is preferably H 2 O 2 in a concentration of 0.05 to 100 mg per g of coal (100% goods), preferably 0.05 to 50 mg per g
  • a further factor is fatty acids in one or more, preferably C 6 to C 26 , particularly preferably C 8 to Cj 6 , very particularly preferably tetradecanoic acid or
  • Dodecanoic acid in a concentration of 0.05 to 100 mg per g of coal, preferably in one
  • ketones preferably e.g. Benzophenones in a concentration of 0.05 to 100 mg per g of coal, preferably in a concentration of 0.05 to 50 mg per g of coal.
  • Solutions A and B are added together and made up to 45 ml.
  • the substance is then placed in a reaction vessel preheated to 45 ° C. and incubated under normal pressure for 1-4 hours.
  • enzyme component system preferably lipase from e.g. Humicola lanuginosa
  • enzyme preferably lipase from e.g. Humicola lanuginosa
  • concentration of 0.05 to 20 mg per 100 ml washing solution preferably 0.05 mg to 10 mg enzyme per 100 ml washing solution (corresponding to approx.
  • the bleaching is preferably carried out by the enzyme component system according to the invention in the presence of oxygen or air at normal pressure in a pH range from 2 to 12, preferably pH 3-10, at one temperature from 20 to 95 ° C, preferably 30 - 95 ° C.
  • the oxidizing agent used is preferably H 2 O 2 in a concentration of 0.05 to 50 mg per 100 ml washing solution (100% product), preferably 0.05 to 20 mg per 100 ml washing solution.
  • a further factor is fatty acids in one or more, preferably C 6 to C 26 , particularly preferably C to C H> , very particularly preferably tetradecanoic acid or dodecanoic acid in a concentration of 0.05 to 50 mg per 100 ml of washing solution, preferably in a concentration of 0.05 to 20 mg per 100 ml washing solution.
  • ketones preferably e.g. Benzophenones in a concentration of 0.05 to 50 mg per 100 ml wash solution, preferably in a concentration of 0.05 to 20 mg per wash solution.
  • the bleaching system can contain phenolic compounds and / or non-phenolic compounds with one or more benzene cores.
  • the following are particularly preferred: air, oxygen; H 0 2 , organic peroxides, sodium perborate and / or sodium percarbonate.
  • Oxygen can also be generated in situ by H 2 O 2 + catalase or the like, or H 2 O can be generated "in situ" from GOD + glucose or the like.
  • a multicomponent bleaching system containing cation-binding metals.
  • Fe + Mn 2+ , Mn 3+ Mn 4+ , Cu + , Cu 2+ , Ti 3+ , Cer 4+ , Mg 2+ and Al 3+ are preferably used as cations.
  • the bleaching system can additionally contain polysaccharides and / or proteins.
  • Possible polysaccharides are glucans, mannans, dextrans, levans, pectins, alginates or plant gums and / or the polysaccharides which are mushroomed or produced by the fungi or mixed with yeasts.
  • Gelatin, albumin and others are proteins. applicable.
  • Simple sugar, ohgomer sugar, amino acids can also be added.
  • PEG polyethylene oxides, polyethyleneimines and polydimethylsoxanes.
  • the multi-component bleaching system according to the invention can be used in combination with detergent additives or detergent additives known per se.
  • the invention is explained in more detail using the following examples:
  • the washing solution is prepared with STW (Standard Tap Water) at 14 ° dH.
  • the wash solution is subjected to a ten-minute temperature adjustment before the start of the incubation.
  • the washing solution is prepared with STW (Standard Tap Water) at 14 ° dH.
  • the enzyme dosage is 1000 IU amidase / 100 ml
  • enzyme preferably lipase from e.g. Humicola lanuginosa, in a concentration of 0.05 to
  • the bleaching is preferably discolored by the enzyme component system according to the invention in the presence of oxygen or air at normal pressure and in a pH range from 2 to 11, preferably pH 3-9, at a temperature of 20 to 95 ° C., preferably 40 - 95 ° C, and a consistency of 0.5 to 40%.
  • a finding that is unusual and surprising for the use of enzymes is that when the enzyme component system according to the invention is used, an increase in the consistency enables a significant increase in performance.
  • a process according to the invention is preferably carried out at consistencies of 4 to 35%, particularly preferably 4 to 15%.
  • HO 2 is preferably added as the oxidizing agent in a concentration of 0.05 to 20 mg per g denim (100% goods), preferably 0.05 to 10 mg per g denim.
  • a further factor is fatty acids in one or more, preferably C 6 to C 26 , particularly preferably C 8 to Cj 6 , very particularly preferably tetradecanoic acid or dodecanoic acid in a concentration of 0.05 to 20 mg per g of denim, preferably in a concentration of 0.05 up to 10 mg per g of denim.
  • ketones preferably e.g. Benzophenones in a concentration of 0.05 to 20 mg per g denim, preferably in a concentration of 0.05 to 10 mg per g denim.
  • the pH of the solution (tap water), which comprises 50 ml after the addition of components, is pre-set to pH 6 with 0.5 n H 2 SO 4 .
  • Tetradecanoic acid 1 mg benzophenone and 2.5 mg H 2 O 2 (30% product) were added per g denim.
  • the test is carried out in a shaking water bath (200 rpm), at 45 ° C. and a reaction time of 45 min. It is then washed with tap water and the piece of tissue is air-dried. Then the brightness is determined with an Elrepho device.
  • ECS enzyme component system
  • 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.
  • CeUobiose oxigen-1-oxidoreductase (CeUobiose oxidase) 1.1.3.25, CeUobiose: quinone -1-oxidoreductase 1.1.5.1, bihrubin oxidase 1.3.3.5, cytochrome oxidase 1.9.3, oxigenases, lipoxigenases 1.13, 1.14, superoxide dismutase 1.15.11, Ferrioxidase, eg 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.
  • class 1.10.3 enzymes with oxygen (O 2 ) as the acceptor are particularly preferred.
  • the enzymes in this class are in particular the enzymes catechol oxidase (tyrosinase) (1.10.3.1), L-ascorbate oxidase (1.10.3.3).
  • the laccases benzenediol oxy oxidoreductase
  • the enzymes of group 1.1 1 are also particularly preferred
  • cytochrome-C peroxidases (1.11.1.5), catalase (1.11.1.6) and the peroxidase (1.11.1.7) are very particularly preferred here
  • Chloride peroxidase (1.11.1.10), the L-ascorbate peroxidase (1.11.1.11), the
  • Phospholipid hydroperoxide glutathione peroxidase (1.11.1.12), manganese peroxidase (1.11.1.13), diarylpropane peroxidase (ligninase, lignin peroxidase) (1.11.1.14).
  • oxidizing agent at least one suitable oxidizing agent
  • mediators selected from the group of hydroxylamines, hydroxylamine derivatives, hydroxamic acids, hydroxamic acid derivatives, the aliphatic, cycloaliphatic, heterocycous or aromatic compounds which contain at least one N-hydroxy, oxime, N-oxi , or N, N'-dioxi function and / or at least one mediator from the group of amides such as hydrazides or 1,2,4-triazolidine-3,5-dione (urazoles) and / or at least one mediator from the Group of imides like eg hydantoins and / or at least one mediator from the group of
  • At least one mediation enhancer selected from the group of carbonyr compounds, ahphatic ethers, phenol ethers or olefins (alkenes), and / or at least one mediation enhancer, selected from the group of the above-mentioned mediators of the NO, NOH-HRN-OH type and / or the amides like
  • Veratryl alcohol and / or phenol derivatives such as p-hydroxycinnamic acid, 2,4-dichlorophenoL p-hydroxybenzene sulfonate, vanillin (4-hydroxy-3-methoxy-benzaldehyde), p-hydroxybenzoic acid, 5-amino-2-hydroxy-benzoic acid (5 - Aminosalycic acid) and / or radical cation compounds according to "Wurster” (Lit .: Angewandte Chemie, 91, 1979, pp. 982-997; Che convinceder Zeit, 12, 1978, pp. 89-98; Römpp Chemie Lexikon, 9th edition, 1995) and / or radical anions, eg semiquinones, which can arise during the enzymatic oxidation of hydroquinones. * (N means nitrogen, R means residues)
  • the mediator / comediator ratio 5000: 1 to 5: 1 is particularly preferably 500: 1 to 5: 1, while the ratio when using simultaneously several mediators and comediators within this
  • enzymatic oxidation systems contain at least one oxidizing agent.
  • the oxidizing agents that can be used are, for example, air, oxygen, ozone, peroxide compounds such as H 2 O 2 , organic peroxides, peracids such as peracetic acid, performic acid, persulfuric acid, persalpic acid, metachloroperoxibenzoic acid, perchloric acid, per compounds such as perborates, percarbonates, persulfates or oxygen species and their radicals such as OH-Radücal, OOH-RadikaL OlT-RadikaL Superoxid (O " 2 ), dioxygenyl cation (O 2 + ), singlet oxygen, ozonide (O 3 " ), dioxiranes, dioxitanes or fremy radicals can be used.
  • Solutions A and B are added together and made up to 33 ml.
  • the substance is then placed in a reaction vessel preheated to 45 ° C. and incubated under normal pressure for 1-4 hours.
  • the fabric is then washed over a nylon sieve (30 ⁇ m) and 1 hour at 60 ° C,
  • the kappa number is determined.
  • System component 2 of the enzyme component system (ECS) fatty acids according to the invention which are used in the process according to the invention as peracid queues are, for example:
  • Tridecanoic acid tetradecanoic acid (myristic acid)
  • Tricosanoic acid Tetraco sanoic acid (lignoceric acid)
  • Tetradecanoic acid (myristic acid) and dodecanoic acid (lauric acid) are particularly preferred.
  • Carbonyl compounds of general formula I are particularly preferred.
  • radicals R 1 and R 2 can be the same or different and represent ahphatic 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 U) and 1,3-diketones (formula III) or polyketones (polyketides) and the tautomeric enols (formula IV) are particularly preferred,
  • radicals R 3 to R ° can again be the same or different and can represent ahphatic 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. The possibility of tautomerization or the exhaustion of a resonance hybrid is of particular importance.
  • ketones such as generally hydroxyketones, oc, ⁇ -unsaturated ketones, oxicarboxylic acids, quinones and halogen ketones are particularly preferred. The following are particularly preferred:
  • Methoxy-2-propanone glyoxylic acid. Benzyl glyoxylate, benzylacetone, benzyl methyl ketone, cyclohexyl methyl ketone. 2-decanon. Dicyclohexyl ketone. Diethyl ketone. DüsopropyUceton, 3,3-Dimethyl-2-butanone, IsobutylmethyUceton, Isopropylmethylketon, 2-Methyl-3-heptanone, 5-Methyl-3-heptanone, 6-Methyl-5-hepten-2-one.
  • 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-oxo-valeric acid, 4-methyl-2-oxo-valeric acid, methyl-phenylglyoxylate, 2-oxobutyric acid, 2,3-pentanedione, 9,10-phenanthrenequinone, acetoacetanide, 2-acetyl- ⁇ -butyric acid lactone, 2-acetylcyclopentanone, AUyl-acetoacetate, benzoylacetone, ter-butylacetoacetate,
  • Triethyl methane tricarboxylate trimethyl-l, 2,3-propane tricarboxylate, 3-acetoxy-2-cyclohexen-l-one, AUyl acetoacetate, AUyl- (cyanoacetate), benzylacetoacetate, tert-butylacetoacetate, butylcyanoacetate, chlorogenic acid hemihydrate, coumarin 3-carboxylic acid.
  • 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-l-phenyl-2-pyrazolin-5-one, l-methyl-2-pyrrohdon, methyluracu, 6-methyluracu, oxindole, phenytoin, 1 (2H) -phthalazinone, phthahmid, 2 , 5-piperazinedione.
  • Anhydrides such as: Benzoic anhydride, benzene-l, 2,4,5-tetracarboxylic acid-l, 2,4,5-dianhydride, 3,3 ', 4,4'-benzophenonetetracarboxylic acid anhydride, succinic acid anhydride, butyric acid anhydride, crotonic acid anhydride, ice-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, naphthonic anhydride, naphthonic anhydride, 1,8-naphthalenic anhydride, , 2.phenylbutyric anhydride, pivalic anhydride, propionic anhydride
  • Appendix HI Polymerization catalysts: phenolic compounds, phenol derivatives or other phenolic polycycles with a number of oxidizable hydroxyl groups:
  • Such polymerization catalysts e.g. 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-hydroxyanüin, 1,4-dimethylanthraquinone, 2,2-dihydroxybiphenyl, 4,4-dihydroxybiphenyl, 2,3-
  • substances which have several hydroxyl groups such as: Eagic acid, GaUuic acid, GaUein, GaUangin, Myo-InositoL Morin, Nitranuklare, Phenolphthalein, Purpurin, PurpurogaUin, Quinizarin, Chrysazin, Quercitin, Quinhydron, Chloranuklare, Carmin, Rhodizonic acid, Croconic acid , Hematoxüin, 9-phenyl-2,3,7-trihydroxy-6-fluorene, 9-methyl-2,3,7-trihydroxy-6-fluorene, tetrahydroxy-p-benzoquinone, 2,2'4,4'- Tetra-hydroxybenzophenone, PyrogaUol Red, 1-nitrophloroglucinoL 1,4-dihydroxyanthraquinone, 5,8-dihydroxy-1,4-naphthoquinone, hexaoxocyclohexanoctahydrate, 5,7
  • Appendix IV shows the formulas of mediators / mediation enhancers (NO, NOH and HNR-OH compounds) which can be used according to the invention as an additive to the enzyme component system (ECS) and which are used together with oxidoreductases, such as:
  • Hydroxylamines Open-chain or cyclic, aliphatic or aromatic, heterocyclic of the general formula,
  • N-hydroxymaleimide derivatives N-hydroxy-naphthalimide and optionally substituted N-hydroxy-naphthalimide derivatives,
  • N-hydroxysuccinimides and optionally substituted N-hydroxysuccinimide derivatives such as:
  • N-hydroxyphthalimide N-hydroxy-benzene-1,2,4-tricarboximide
  • N, N'-dihydroxy-pyrome] acid diimide N, N-dihydroxy-benzophenone-3,3 ', 4,4'-tetracarboxylic acid cliimide, e.g. (Formula VH):
  • N-hydroxymaleimide N-hydroxymaleimide, pyridine-2,3-dicarboxylic acid N-hydroxyknide, e.g. (Formula VUI):
  • N-hydroxy-cis-4-cyclohexene-1,2-dicarboximide e.g. (Formula IX): N-hydroxynaphthalimide sodium salt. such as. (six-membered ring according to formula A):
  • Triangular acid Triangular acid, squaric acid, croconic acid, rhodizonic acid.
  • Appendix IVa shows compounds that serve as mediation enhancers, especially as an additive together with mediators and oxidoreductases can be added to the enzyme component system (ECS) according to the invention, such as:
  • ahphatic ethers such as:
  • Olefins such as 2-alkylphenol 2-AUyl-6-methylphenol, AUylbenzol,
  • Cinnamic acid methyl ester 2,4,6-triaUyloxy-1,3,5-triazine, 1,2,4-trivinylcyclohexane, 4-AUyl-l, 2-dimethoxybenzene, 4-tert-
  • Phenol ethers such as: 2,3-dimethoxybenzyl alcohol 3,4-dimethoxybenzyl alcohol 2,4-
  • Carbonyl compounds such as:
  • Appendix 5 Possible oxidation reactions of the enzyme component system:

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Abstract

L'invention concerne un système d'oxydation et de blanchiment comportant des agents d'oxydation produits par action enzymatique, à savoir un système enzymes-composants utilisé comme système d'oxydation et de blanchiment pour la production d'agents d'oxydation spéciaux hautement sélectifs, constitué de: a) composant de système (1): au moins une hydrolase de la classe d'enzymes 3.1, 3.1.1, 3.1.2, 3.1.3, 3.1.4 ou 3.1.7 et/ou au moins une hydrolase de la classe d'enzymess 3.5, 3.5.1, 3.5.2, 3.5.3, 3.5.4, 3.5.5 ou 3.5.99; b) composant de système 2): au moins un acide gras, de préférence ayant 6 à 26 atomes de C (saturé, mono ou polyinsaturé); c) composant de système 3): au moins un agent d'oxydation précurseur destiné à réagir avec les enzymes; d) composant de système 4): au moins une cétone du groupe des composés carbonylés.
PCT/DE1998/001689 1997-06-20 1998-06-19 Systeme d'oxydation et de blanchiment comportant des agents d'oxydation produits par action enzymatique WO1998059108A2 (fr)

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WO2001092454A1 (fr) * 2000-05-31 2001-12-06 Unilever N.V. Composition et procede d'oxydation enzymatique
WO2002036724A1 (fr) * 2000-10-31 2002-05-10 Unilever N.V. Procede et composition d'oxydation
WO2002099023A2 (fr) * 2001-06-05 2002-12-12 Call, Krimhild Systemes enzymatiques de regeneration d'especes a oxygene actif destinees a reagir avec d'autres precurseurs pour permettre l'oxydation et/ou le blanchiment
WO2003048449A1 (fr) * 2001-12-03 2003-06-12 Iogen Bio-Products Corporation Etape de blanchiment comprenant l'utilisation de xylanase en association avec du peroxyde d'hydrogene, des peracides ou une combinaison de ces derniers
WO2003061550A2 (fr) * 2002-01-26 2003-07-31 Call, Krimhild Nouvelles activites catalytiques d'oxydo-reductases pour l'oxydation et/ou le blanchiment
WO2005103372A2 (fr) 2004-04-26 2005-11-03 Call, Krimhild Systemes oxydants, reducteurs, hydrolytiques et autres systemes enzymatiques destines a l'oxydation, la reduction aux fins de revetement, de couplage et de reticulation de matieres fibreuses naturelles et artificielles, de matieres plastiques ou de matieres monomeres a polymeres naturelles et artificielles
EP1066422B1 (fr) * 1998-04-03 2006-07-19 Novozymes A/S Traitement de tissu denim a l'aide d'une enzyme pectolytique
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WO2015039962A1 (fr) * 2013-09-20 2015-03-26 Novozymes A/S Blanchiment enzymatique de pulpe de papier
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WO2016096393A1 (fr) * 2014-12-15 2016-06-23 Henkel Ag & Co. Kgaa Bilirubines oxydases utilisées comme inhibiteurs de transfert de couleurs dans des produit de lavage et de nettoyage
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EP1066422B1 (fr) * 1998-04-03 2006-07-19 Novozymes A/S Traitement de tissu denim a l'aide d'une enzyme pectolytique
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WO2002036724A1 (fr) * 2000-10-31 2002-05-10 Unilever N.V. Procede et composition d'oxydation
WO2002099023A3 (fr) * 2001-06-05 2003-05-30 Call Krimhild Systemes enzymatiques de regeneration d'especes a oxygene actif destinees a reagir avec d'autres precurseurs pour permettre l'oxydation et/ou le blanchiment
WO2002099023A2 (fr) * 2001-06-05 2002-12-12 Call, Krimhild Systemes enzymatiques de regeneration d'especes a oxygene actif destinees a reagir avec d'autres precurseurs pour permettre l'oxydation et/ou le blanchiment
WO2003048449A1 (fr) * 2001-12-03 2003-06-12 Iogen Bio-Products Corporation Etape de blanchiment comprenant l'utilisation de xylanase en association avec du peroxyde d'hydrogene, des peracides ou une combinaison de ces derniers
WO2003061550A2 (fr) * 2002-01-26 2003-07-31 Call, Krimhild Nouvelles activites catalytiques d'oxydo-reductases pour l'oxydation et/ou le blanchiment
WO2003061550A3 (fr) * 2002-01-26 2004-09-10 Call Krimhild Nouvelles activites catalytiques d'oxydo-reductases pour l'oxydation et/ou le blanchiment
WO2005103372A2 (fr) 2004-04-26 2005-11-03 Call, Krimhild Systemes oxydants, reducteurs, hydrolytiques et autres systemes enzymatiques destines a l'oxydation, la reduction aux fins de revetement, de couplage et de reticulation de matieres fibreuses naturelles et artificielles, de matieres plastiques ou de matieres monomeres a polymeres naturelles et artificielles
WO2005103372A3 (fr) * 2004-04-26 2006-03-16 Call Krimhild Systemes oxydants, reducteurs, hydrolytiques et autres systemes enzymatiques destines a l'oxydation, la reduction aux fins de revetement, de couplage et de reticulation de matieres fibreuses naturelles et artificielles, de matieres plastiques ou de matieres monomeres a polymeres naturelles et artificielles
DE102009025190A1 (de) 2009-06-12 2010-12-16 Call, Krimhild Enzymatische Systeme zum Koppeln und Cross-linken von Textilien und Biomaterialien für Medizinprodukte und von anderen Stoffen und/oder Materialien
CN104662225A (zh) * 2012-06-22 2015-05-27 巴克曼实验室国际公司 在造纸过程中使用脂肪酶和氧化剂的组合控制沥青的方法及其制品
WO2015039962A1 (fr) * 2013-09-20 2015-03-26 Novozymes A/S Blanchiment enzymatique de pulpe de papier
WO2016096393A1 (fr) * 2014-12-15 2016-06-23 Henkel Ag & Co. Kgaa Bilirubines oxydases utilisées comme inhibiteurs de transfert de couleurs dans des produit de lavage et de nettoyage
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