Classifications

• • 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

• the present invention relates to a multi-component system for changing, breaking down or bleaching lignin or containing lignin Materials and procedures for its Application.
• 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 the sulfite process uses Ca (HSO 3 ) 2 + SO 2 .
• the main goal of all procedures is the removal of the lignin from the used plant material, wood or Annual plants.
• the lignin that is associated with cellulose and hemicellulose Main component of the plant material must be removed, otherwise it is not possible non-yellowing and mechanically heavy-duty papers to manufacture.
• the wood production processes work with stone grinders (Wood sanding) or with refiners (TMP), which the wood after appropriate Pretreatment (chemical, thermal or chemical-thermal) defibrillate by grinding.
• Wood sanding Wood sanding
• TMP refiners
• Biopulping is the treatment of wood chips with living mushroom systems.
• the goal here is to reduce the amount of cooking chemicals that Improve cooking capacity and "extended cooking".
• Improved kappa reduction is also an advantage after cooking compared to cooking without pretreatment reached.
• Biobleaching also works with in-vivo systems.
• the cooked pulp (Softwood / Hardwood) is before bleaching inoculated with the fungus and treated for days to weeks. Just after this long treatment period, a significant one becomes apparent Kappa reduction and whiteness, what the process uneconomical for an implementation in the usual Bleaching sequences.
• Chelate substances are used as a cofactor in addition to the lignolytic enzymes (Siderophores such as ammonium oxalate) and biosurfactants on.
• the enhancer substances are described in WO 94/12619 on the basis of their Characterized half-life.
• enhancer substances are organic chemicals, containing at least two aromatic rings, of which at least one substituted with defined radicals is.
• WO 94/29510 describes a method for enzymatic delignification, where enzymes are used together with mediators become. Connections with are generally used as mediators of structure NO, NOH or HRNOH.
• HBT 1-Hydroxy-1H-benzotriazole
• Examples of compounds in the multicomponent system according to the invention can be used as mediators (component c) can be 2,6-dihydroxy-3-nitrosopyridine, 2,3-dihydroxy-4-nitrosopyridine, 2,6-dihydroxy-3-nitrosopyridine-4-carboxylic acid, 2,4-dihydroxy-3-nitrosopyridine, 3-hydroxy-2-mercaptopyridine, 2-hydroxy-3-mercaptopyridine, 2,6-diamino-3-nitrosopyridine, 2,6-diamino-3-nitrosopyridine-4-carboxylic acid, 2-hydroxy-3-nitrosopyridine, 3-hydroxy-2-nitrosopyridine, 2-mercapto-3-nitrosopyridine, 3-mercapto-2-nitrosopyridine, 2-amino-3-nitrosopyridine, 3-amino-2-nitrosopyridine, 2,4-dihydroxy-3-nitrosoquinoline, 8-hydroxy-5-nitrosoquinoline, 2,3-dihydroxy-4-nitrosoquino
• Preferred mediators are 2,6-dihydroxy-3-nitrosopyridine, 2, 6-diamino-3-nitrosopyridine, 2,6-dihydroxy-3-nitrosopyridine-4-carboxylic acid, 2,4-dihydroxy-3-nitrosopyridine, 2-hydroxy-3-mercaptopyridine, 2-mercapto-3-pyridinol, 2,4-dihydroxy-3-nitrosoquinoline, 8-hydroxy-5-nitrosoquinoline, 2,3-dihydroxy-4-nitrosoquinoline as well as tautomers of these compounds.
• the multicomponent system according to the invention contains mediators, which are cheaper than those known from the prior art Mediators, in particular, are less expensive than HBT.
• Oxidation catalysts in the multi-component system according to the invention Enzymes used.
• enzyme also includes enzymatically active Proteins or peptides or prosthetic groups of enzymes.
• the enzyme in the multicomponent system according to the invention Oxidoreductases of classes 1.1.1 to 1.97 according to international standards Enzyme Nomenclature, Committee of the International Union of Biochemistry and Molecular Biology (Enzyme Nomenclature, Academic Press, Inc., 1992, pp. 24-154) can be used.
• Class 1.1 enzymes which comprise all dehydrogenases which act on primary, secondary alcohols and semiacetals and which are accepted as acceptors NAD + or NADP + (subclass 1.1.1), cytochromes (1.1.2), oxygen (O 2 ) (1.1 .3), disulfides (1.1.4), quinones (1.1.5) or other acceptors (1.1.99).
• the enzymes of this class are particularly preferred Class 1.1.5 with quinones as acceptors and the enzymes of the Class 1.1.3 with oxygen as the acceptor.
• Cellobiose is particularly preferred in this class: quinone-1-oxidoreductase (1.1.5.1).
• Enzymes of class 1.2 are also preferred. This class of enzymes includes those enzymes that oxidize aldehydes to the corresponding acids or oxo groups.
• the acceptors can be NAD + , NADP + (1.2.1), cytochrome (1.2.2), oxygen (1.2.3), sulfides (1.2.4), iron-sulfur proteins (1.2.5) or other acceptors (1.2 .99).
• the enzymes of group (1.2.3) are particularly preferred here with oxygen as the acceptor.
• Enzymes of class 1.3 are also preferred.
• enzymes are summarized that are based on CH-CH groups of the donor.
• acceptors are NAD + , NADP + (1.3.1), cytochromes (1.3.2), oxygen (1.3.3), quinones or related compounds (1.3.5), iron-sulfur proteins (1.3.7) or other acceptors (1.3.99).
• Bilirubin oxidase (1.3.3.5) is particularly preferred.
• class 1.4 enzymes which act on CH-NH 2 groups of the donor.
• acceptors are NAD + , NADP + (1.4.1), cytochrome (1.4.2), oxygen (1.4.3), disulfides (1.4.4), iron-sulfur proteins (1.4.7) or other acceptors ( 1.4.99).
• Enzymes of class 1.4.3 are also particularly preferred here Oxygen as an acceptor.
• class 1.5 enzymes which act on CH-NH groups of the donor.
• the corresponding acceptors are NAD + , NADP + (1.5.1), oxygen (1.5.3), disulfides (1.5.4), quinones (1.5.5) or other acceptors (1.5.99).
• enzymes with oxygen (O 2 ) (1.5.3) and with quinones (1.5.5) are particularly preferred as acceptors.
• Enzymes of class 1.6 which are based on NADH are also preferred or NADPH work.
• acceptors here are NADP + (1.6.1), heme proteins (1.6.2), disulfides (1.6.4), quinones (1.6.5), NO 2 groups (1.6.6), and a flavin (1.6.8 ) or some other acceptors (1.6.99).
• Enzymes of class 1.6.5 are particularly preferred here Quinones as acceptors.
• class 1.7 enzymes which act on donors of other NO 2 compounds and which accept cytochromes (1.7.2), oxygen (O 2 ) (1.7.3), iron-sulfur proteins (1.7.7) or others (1.7.99).
• Class 1.7.3 with oxygen is particularly preferred here as an acceptor.
• class 1.8 enzymes which act as donors on sulfur groups and NAD + , NADP + (1.8.1), cytochromes (1.8.2), oxygen (O 2 ) (1.8.3), disulfides (1.8. 4), quinones (1.8.5), iron-sulfur proteins (1.8.7) or others (1.8.99).
• class 1.9 enzymes which act as donors on heme groups and have oxygen (O 2 ) (1.9.3), NO 2 compounds (1.9.6) and others (1.9.99) as acceptors.
• Enzymes of class 1.12 which are based on hydrogen are also preferred act as a donor.
• the acceptors are NAD + or NADP + (1.12.1) or others (1.12.99).
• Enzymes of class 1.13 and 1.14 are also preferred (Oxigenases).
• preferred enzymes are those of class 1.15 which are based on Superoxide radicals act as acceptors.
• Enzymes of class 1.16 are also preferred.
• Enzymes of class 1.16.3.1 are particularly preferred here (Ferroxidase, e.g. ceruloplasmin).
• Further preferred enzymes are those of group 1.17 (action on CH 2 groups which are oxidized to -CHOH-), 1.18 (action on reduced ferredoxin as donor), 1.19 (action on reduced flavodoxin as donor) and 1.97 (others Oxidoreductases).
• the enzymes of group 1.11 are also particularly preferred. which act on a peroxide as an acceptor.
• This only subclass (1.11.1) contains the peroxidases.
• the cytochrome C peroxidases are particularly preferred here (1.11.1.5), catalase (1.11.1.6), the peroxidase (1.11.1.6), iodide peroxidase (1.11.1.8), glutathione peroxidase (1.11.1.9), the chloride peroxidase (1.11.1.10), the L-ascorbate peroxidase (1.11.1.11), the phospholipid hydroperoxide glutathione peroxidase (1.11.1.12), the manganese peroxidase (1.12.1.13), the diarylpropane peroxidase (ligninase, lignin peroxidase) (1.11.1.14).
• Enzymes of class 1.10 which act on biphenols and related compounds are very particularly preferred. They catalyze the oxidation of biphenols and ascorbates. NAD + , NADP + (1.10.1), cytochrome (1.10.2), oxygen (1.10.3) or others (1.10.99) act as acceptors.
• class 1.10.3 enzymes with oxygen (O 2 ) as the acceptor are particularly preferred.
• the enzymes in this class are catechol oxidase (Tyrosinase) (1.10.3.1), L-ascorbate oxidase (1.10.3.3), o-A-minophenol Oxidase (1.10.3.4) and laccase (benzene diol: oxigen Oxidoreductase) (1.10.3.2) is preferred, the laccases (benzenediol: Oxigen oxidoreductase) (1.10.3.2) is particularly preferred are.
• the enzymes mentioned are commercially available or can be win according to standard procedures.
• organisms for production the enzymes come from plants, animal cells, Bacteria and fungi into consideration. Basically, both naturally occurring as well as genetically modified organisms Be an enzyme producer. Parts of unicellular are also or multicellular organisms conceivable as enzyme producers, especially cell cultures.
• particularly preferred enzymes such as those from the group 1.11.1 but above all 1.10.3 and especially for production laccases, for example, are white rot fungi such as pleurotus, Phlebia and Trametes used.
• the multi-component system according to the invention comprises at least one oxidizing agent.
• the oxidizing agents that can be used are, for example, air, oxygen, ozone, H 2 O 2 , organic peroxides, peracids such as peracetic acid, performic acid, persulfuric acid, persitric acid, metachloroperoxibenzoic acid, perchloric acid, perborates, peracetates, persulfates, peroxides or oxygen species and their radicals such as OH, OOH, Singlet oxygen, superoxide (O 2 - ), ozonide, dioxygenyl cation (O 2 + ), dioxirane, dioxetane or fremy radicals can be used.
• Oxidizing agents are preferably used which either generated by the corresponding oxidoreductases can be e.g. Dioxiranes from laccases plus carbonyls or that can regenerate the mediator chemically or directly can implement.
• the invention also relates to the use of substances which according to the invention are suitable as mediators for changing, Degradation or bleaching of lignin or materials containing lignin.
• Mg 2+ ions can be used, for example, as a salt, such as MgSO 4 .
• concentration is in the range of 0.1-2 mg / g of lignin-containing material, preferably 0.2-0.6 mg / g.
• a further increase in the effectiveness of the multicomponent system according to the invention can be achieved in that the multicomponent system in addition to the Mg 2+ ions also complexing agents such as, for example, ethylenediaminetetraacetic acid (ED-TA), diethylenetriaminepentaacetic acid (DTPA), hydroxyethylenediamine triacetic acid (HEDTA), diethylenetriaminepentamethylenephosphonic acid ( , Nitrilotriacetic acid (NTA), polyphosphoric acid (PPA) etc. contains.
• the concentration is in the range of 0.2-5 mg / g of lignin-containing material, preferably 1-3 mg.
• a method using the method according to the invention is preferred Multi-component system in the presence of oxygen or air at normal pressure up to 10 bar and in a pH range from 2 to 11, preferably at a temperature of 20 to 95 ° C 40 - 95 ° C, and a consistency of 0.5 to 40% carried out.
• one according to the invention is preferred Process with material densities of 8 to 35%, particularly preferred 9 to 15% performed.
• the chelating agents become those Common substances (such as EDTA, DTPA) are used. They are preferably used in concentrations of 0.1% to 1% (w / w based on dry pulp), particularly preferably 0.1 % to 0.5% (w / w based on dry pulp) used.
• lignin-containing material 0.01 to 100,000 IU enzyme used per g of lignin-containing material. Especially 0.1 to 100 are particularly preferred 1 to 40 IU enzyme are used per g of lignin-containing material (1 U corresponds to the conversion of 1 ⁇ mol 2,2'-Azino-bis (3-ethyl-benzothiazoline-6-sulfonic acid diammonium salt) (ABTS) / min / ml enzyme
• oxidizing agent used per g of lignin-containing material.
• 0.01 to 50 mg of oxidizing agent are particularly preferred used per g of lignin-containing material.
• reducing agents can be added together with the existing oxidizing agents for adjustment serve a certain redox potential.
• Sodium bisulfite, sodium dithionite, Ascorbic acid, thio compounds, mercapto compounds or glutathione etc. can be used.
• the reaction takes place under air or Oxygen supply or oxygen or air pressure from, at the peroxidases (e.g. lignin peroxidases, manganese peroxidases) with hydrogen peroxide.
• peroxidases e.g. lignin peroxidases, manganese peroxidases
• oxygen also by hydrogen peroxide + catalase and hydrogen peroxide by glucose + GOD or other systems in situ to be generated.
• Radical formers or radical scavengers can also be added to the system (Trapping OH or OOH radicals, for example) added become. These can influence the interaction within the Red / Ox and improve radical mediators.
• the salts form cations in the reaction solution.
• Such ions include Fe 2+ , Fe 3+ , Mn 2+ , Mn 3+ , Mn 4+ , Cu 2+ , Ca 2+ , Ti 3+ , Cer 4+ , Al 3+ .
• the chelates present in the solution can also as mimic substances for the enzymes, for example for the Laccases (copper complexes) or for the lignin or manganese peroxidases (Heme complexes).
• mimic substances are such to understand substances that the prosthetic groups of (here) simulate oxidoreductases and e.g. Oxidation reactions can catalyze.
• NaOCl can also be added to the reaction mixture. This compound can interact with hydrogen peroxide Form singlet oxygen.
• detergents it is also possible to use detergents to work. As such come non-ionic, anionic, cationic and amphoteric surfactants.
• the detergents can penetrate the enzymes and mediators into the fiber improve.
• Polysaccharides can also be beneficial for the reaction and / or add proteins.
• Polysaccharides glucans, mannans, dextrans, levans, pectins, Alginates or plant gums and / or your own mushrooms polysaccharides formed or produced in mixed culture with yeasts and to name gelatin and albumin as proteins.
• proteases such as pepsin, bromelin, papain etc. These can include serve by breaking down the extensin C present in the wood, Hydroxyproline-rich protein, better access to lignin to reach.
• protective colloids are amino acids, simple sugar, Oligomeric sugar, PEG types of the most varied Molecular weights, polyethylene oxides, polyethyleneimines and polydimethylsiloxanes in question.
• the method according to the invention can be used not only for delignification (Bleaching) of sulfate, sulfite, organosol, etc.
• Pulp and wood pulp are used, but also in the manufacture of cellulose in general, be it from Wood or annual plants when defibrillated by the usual cooking methods (possibly connected with mechanical Process or printing) i.e. a very gentle cooking up to kappa numbers that range from about 50 to 120 kappa can lie, is guaranteed.
• the treatment can be repeated several times, either after washing and extraction of the treated material with NaOH or without these intermediate steps. This leads to kappa values which can be reduced still further and to substantial increases in whiteness.
• an O 2 stage can be used before the enzyme / mediator treatment or, as already mentioned, an acid wash or a Q stage (chelate stage) can be carried out.

Landscapes

• Life Sciences & Earth Sciences (AREA)
• Engineering & Computer Science (AREA)
• Wood Science & Technology (AREA)
• Chemical & Material Sciences (AREA)
• Biochemistry (AREA)
• Microbiology (AREA)
• Paper (AREA)
• Detergent Compositions (AREA)
• Compounds Of Unknown Constitution (AREA)
• Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)

Applications Claiming Priority (3)

Publications (2)

Family

ID=7814116

Family Applications (1)

Country Status (12)

Families Citing this family (32)

Family Cites Families (2)

• 1996
  • 1996-12-09 DE DE19651099A patent/DE19651099A1/de not_active Withdrawn
• 1997
  • 1997-12-05 JP JP10526185A patent/JP2000505844A/ja active Pending
  • 1997-12-05 CN CN97180387A patent/CN1240008A/zh active Pending
  • 1997-12-05 DE DE59702358T patent/DE59702358D1/de not_active Expired - Lifetime
  • 1997-12-05 ES ES97952038T patent/ES2150797T3/es not_active Expired - Lifetime
  • 1997-12-05 WO PCT/EP1997/006802 patent/WO1998026127A1/de active IP Right Grant
  • 1997-12-05 PT PT97952038T patent/PT943032E/pt unknown
  • 1997-12-05 AU AU55603/98A patent/AU719140B2/en not_active Ceased
  • 1997-12-05 RU RU99114460/12A patent/RU2154704C1/ru active
  • 1997-12-05 BR BR9714387-1A patent/BR9714387A/pt unknown
  • 1997-12-05 EP EP97952038A patent/EP0943032B1/de not_active Expired - Lifetime
  • 1997-12-05 CA CA002271937A patent/CA2271937A1/en not_active Abandoned
  • 1997-12-05 AT AT97952038T patent/ATE196331T1/de not_active IP Right Cessation

Also Published As

Similar Documents

Legal Events