CN104342425A - Fiber oxidase composition for improving whiteness of paper and papermaking method and application thereof - Google Patents

Fiber oxidase composition for improving whiteness of paper and papermaking method and application thereof Download PDF

Info

Publication number
CN104342425A
CN104342425A CN201410366880.4A CN201410366880A CN104342425A CN 104342425 A CN104342425 A CN 104342425A CN 201410366880 A CN201410366880 A CN 201410366880A CN 104342425 A CN104342425 A CN 104342425A
Authority
CN
China
Prior art keywords
fiber
fiber oxidation
oxidation enzyme
enzyme
paper
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Granted
Application number
CN201410366880.4A
Other languages
Chinese (zh)
Other versions
CN104342425B (en
Inventor
王祥槐
谢焱
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Rui Xing Biotechnology (guangzhou) Co Ltd
Original Assignee
Rui Xing Biotechnology (guangzhou) Co Ltd
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Rui Xing Biotechnology (guangzhou) Co Ltd filed Critical Rui Xing Biotechnology (guangzhou) Co Ltd
Priority to CN201410366880.4A priority Critical patent/CN104342425B/en
Publication of CN104342425A publication Critical patent/CN104342425A/en
Priority to PCT/CN2015/084456 priority patent/WO2016015571A1/en
Application granted granted Critical
Publication of CN104342425B publication Critical patent/CN104342425B/en
Active legal-status Critical Current
Anticipated expiration legal-status Critical

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004Oxidoreductases (1.)
    • C12N9/0055Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10)
    • C12N9/0057Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10) with oxygen as acceptor (1.10.3)
    • C12N9/0061Laccase (1.10.3.2)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004Oxidoreductases (1.)
    • C12N9/0006Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004Oxidoreductases (1.)
    • C12N9/0065Oxidoreductases (1.) acting on hydrogen peroxide as acceptor (1.11)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/16Hydrolases (3) acting on ester bonds (3.1)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/16Hydrolases (3) acting on ester bonds (3.1)
    • C12N9/18Carboxylic ester hydrolases (3.1.1)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405Glucanases
    • C12N9/2408Glucanases acting on alpha -1,4-glucosidic bonds
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405Glucanases
    • C12N9/2408Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411Amylases
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405Glucanases
    • C12N9/2434Glucanases acting on beta-1,4-glucosidic bonds
    • C12N9/2437Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405Glucanases
    • C12N9/2434Glucanases acting on beta-1,4-glucosidic bonds
    • C12N9/2445Beta-glucosidase (3.2.1.21)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2477Hemicellulases not provided in a preceding group
    • C12N9/248Xylanases
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/88Lyases (4.)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y101/00Oxidoreductases acting on the CH-OH group of donors (1.1)
    • C12Y101/01Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
    • C12Y101/01001Alcohol dehydrogenase (1.1.1.1)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y101/00Oxidoreductases acting on the CH-OH group of donors (1.1)
    • C12Y101/03Oxidoreductases acting on the CH-OH group of donors (1.1) with a oxygen as acceptor (1.1.3)
    • C12Y101/03004Glucose oxidase (1.1.3.4)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y101/00Oxidoreductases acting on the CH-OH group of donors (1.1)
    • C12Y101/99Oxidoreductases acting on the CH-OH group of donors (1.1) with other acceptors (1.1.99)
    • C12Y101/99018Cellobiose oxidase (1.1.99.18)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y110/00Oxidoreductases acting on diphenols and related substances as donors (1.10)
    • C12Y110/03Oxidoreductases acting on diphenols and related substances as donors (1.10) with an oxygen as acceptor (1.10.3)
    • C12Y110/03002Laccase (1.10.3.2)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y111/00Oxidoreductases acting on a peroxide as acceptor (1.11)
    • C12Y111/01Peroxidases (1.11.1)
    • C12Y111/01006Catalase (1.11.1.6)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y111/00Oxidoreductases acting on a peroxide as acceptor (1.11)
    • C12Y111/01Peroxidases (1.11.1)
    • C12Y111/01014Lignin peroxidase (1.11.1.14)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y302/00Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01004Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y302/00Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01021Beta-glucosidase (3.2.1.21)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y302/00Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01091Cellulose 1,4-beta-cellobiosidase (3.2.1.91)
    • DTEXTILES; PAPER
    • D21PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21HPULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
    • D21H17/00Non-fibrous material added to the pulp, characterised by its constitution; Paper-impregnating material characterised by its constitution
    • D21H17/005Microorganisms or enzymes
    • DTEXTILES; PAPER
    • D21PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21HPULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
    • D21H21/00Non-fibrous material added to the pulp, characterised by its function, form or properties; Paper-impregnating or coating material, characterised by its function, form or properties
    • D21H21/06Paper forming aids
    • D21H21/10Retention agents or drainage improvers
    • DTEXTILES; PAPER
    • D21PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21HPULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
    • D21H21/00Non-fibrous material added to the pulp, characterised by its function, form or properties; Paper-impregnating or coating material, characterised by its function, form or properties
    • D21H21/14Non-fibrous material added to the pulp, characterised by its function, form or properties; Paper-impregnating or coating material, characterised by its function, form or properties characterised by function or properties in or on the paper
    • D21H21/30Luminescent or fluorescent substances, e.g. for optical bleaching

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Organic Chemistry (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Engineering & Computer Science (AREA)
  • Genetics & Genomics (AREA)
  • Wood Science & Technology (AREA)
  • Zoology (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • General Engineering & Computer Science (AREA)
  • Microbiology (AREA)
  • Molecular Biology (AREA)
  • Biotechnology (AREA)
  • Biomedical Technology (AREA)
  • Medicinal Chemistry (AREA)
  • Paper (AREA)

Abstract

The invention discloses a fiber oxidase composition for improving whiteness of paper and a papermaking method and an application thereof. The fiber oxidase composition is mainly prepared from the following components: a bio-enzyme component and an auxiliary component, wherein the bio-enzyme component has an oxidizing function for fibers and particularly refers to the fiber oxidase which changes the fiber surface property by virtue of redox reaction; the auxiliary component has a function of increasing the catalytic activity of the fiber oxidase and particularly refers to a reaction substrate of the fiber oxidase. The invention further provides a method of the composition for making paper. The composition is used for treating paper pulp, so that the whiteness of the obtained paper can be remarkably improved.

Description

For improving the fiber oxidation enzyme composition of Paper White Degree and papermaking process and application
Technical field
The present invention relates to biological enzyme and use biological enzyme to improve the technical field of fibrous physics chemical property, particularly, relating to a kind of fiber oxidation enzyme composition for improving Paper White Degree and papermaking process and application.
Background technology
China paper industry keeps high growth rate in continuous 10 years between 2000-2010, to the turnout of China's paper in 2011 and cardboard and consumption all more than 100,000,000 tons, all ranks first in the world.The constitutive material mainly fiber of Paper or cardboard, because slurrying, papermaking need a large amount of raw materials, and environment is had a certain impact, current countries in the world paper industry is all produced in compression slurrying, to ensure the forest reserves, add that the construction of base of internal sources woods is slow, limited for material, but not wood pulp development is subject to the delayed impact of cleaner production new technology development, the constraint of resource, the energy and environment that China paper industry development faces highlights day by day.
And waste paper is as the recycling secondary stock resource of one, recovery papermaking both can protect forest resources and alleviate the great demand pressure of paper industry development to natural resources to a certain extent, can reduce again the consumption of water and the energy, reduce environmental pollution.The recycling dynamics of China to waste paper resources is also strengthening year by year, according to Chinese papermaking association statistics, during within 2002, national paper pulp consumes, paper waste ratio only accounts for 47%, within 2011, paper waste consumes 5,660 ten thousand tons, the ratio accounting for national paper pulp consumption rises to 62%, and therefore, the research of deinking receives increasing concern as the committed step of Waste Paper Handling.
Traditional Chemical Deinking adds the chemical reagent such as sodium hydroxide, water glass, hydrogen peroxide, sequestrant and tensio-active agent, various chemokines impels ink to be come off from fiber by saponification in the basic conditions, then utilizes the method for flotation or washing to be removed by ink.Deinking agent is mainly used in destroying ink to the adhesive power of fiber in waste paper recycling, makes ink peel off from fiber and be scattered in water.Chemical Deinking method, owing to adopting comparatively multi-chemistry, not only can cause contaminate environment, and is not suitable for the wastepaper of Laser Printing and duplicating.With the Mixed Office WasteMOW that Laser Printing and xerox are representative, because top sizing degree is high, ink is melted on fiber, relies on mechanical stirring and phase mutual friction to be difficult to ink detachment by means of only conventional flotation and washing.The introducing of biological enzyme can suitably interrupt the connection between ink and fiber and make it to depart from fiber surface, improves the whiteness of paper waste, improves the physicals of paper simultaneously.
In the past few decades, a lot of enzyme (such as cellulase/hemicellulose, lipase, laccase) reclaims in industry at deinking and is studied the substitutability of chemical method.The deinking mechanism of various enzyme is different and wait further research, comparatively admits at present: the noncrystalline domain part of cellulase/hemicellulase hydrolyzes fiber surface, ink was died down with interfibrous connection, thus be conducive to separation; Lipase by the oil based vehicles degraded in ink, makes the carbon black in ink and pigment shed from paper, depart from targetedly.Lignin-degrading enzymes, as laccase, optionally can remove the xylogen of paper surface, thus promotes removing of ink.To be that multiple highly effective biological zyme preferably with strong points is composite form in enzymatic deinking agent, with enzyme activition special assistant with the use of, for the deinking of newspaper, Mixed Office WasteMOW, books, magazine etc.
Compared with traditional chemical deinking, enzymatic deinking has a series of outstanding advantage: 1. enzymatic deinking mild condition, and chemicals usage is few, and fiber loss is little, keeps good fiber properties; 2. significantly reduce COD of sewage and BOD, alleviate treatment pressure of sewage; 3. improve paper pulp yield and improve paper strength; 4. cleaner production, saves the energy, reduces material consumption; 5. use simple, mate with existing most of deinking process.At present, enzymatic deinking agent has been applied to paper-making deinking field; But adopt the action effect of biological enzyme of the prior art to be only limited to and improve ink point dissociating from fiber surface.
Summary of the invention
Based on this, an object of the present invention is for providing a kind of fiber oxidation enzyme composition for improving Paper White Degree.
The concrete technical scheme solved the problems of the technologies described above is as follows:
For improving a fiber oxidation enzyme composition for Paper White Degree, comprise following composition:
I) fiber is had to the biological enzyme component of oxidative function, described biological enzyme component is the fiber oxidation enzyme being changed property of fiber surface by redox reaction; With
Ii) fiber oxidation enzyme is had to the auxiliary component increasing catalytic activity, described auxiliary component is the reaction substrate of fiber oxidation enzyme;
The weight ratio of described biological enzyme component and auxiliary component is 1:1-100.
Wherein in some embodiments, described fiber oxidation Mei Shi gang molecular weight is at 20-50KDa, the glycan oxygenase with the dependent small molecules metalloenzyme of copper, and the reaction substrate of described fiber oxidation enzyme is oxygen, air or oxygen release compound; Described oxygen release compound is superoxide or ozone.
Wherein in some embodiments, described superoxide is at least one in hydrogen peroxide, sodium peroxide, calcium peroxide or Potassium peroxide.
Wherein in some embodiments, the weight ratio of described biological enzyme component and auxiliary component is 1:1-75.
Wherein in some embodiments, the weight ratio of described biological enzyme component and auxiliary component is 1:20-75.
Wherein in some embodiments, the weight ratio of described biological enzyme component and auxiliary component is 1:30-70.
Wherein in some embodiments, described fiber oxidation enzyme composition also comprises protein fiber oxidation enzyme to promoter action, and the described protein having a promoter action to fiber oxidation enzyme is have the biological enzyme of catalytic activity or the cellulose binding protein of catalytically inactive.
Wherein in some embodiments, described in have the biological enzyme of catalytic activity to be oxydo-reductase, be selected from one or more in cellobiose dehydrogenase, laccase, notatin, Catalase, alcohol dehydrogenase or xylogen peroxidase; Or described in have the biological enzyme of catalytic activity to be the hydratase of non-cellulose lytic enzyme, be selected from one or more in amylase, zytase, polygalacturonase or esterase.
Wherein in some embodiments, in described fiber oxidation enzyme composition, the weight ratio of fiber oxidation enzyme and protein fiber oxidation enzyme to promoter action is 1:(0.5-3).
Wherein in some embodiments, the protein of described catalytically inactive is Fiberonectin and/or filament expansion albumen.
Another object of the present invention is for providing a kind of fiber oxidation enzyme composition or fiber oxidation enzyme in paper technology as the application improving the SYNTHETIC OPTICAL WHITNER of Paper White Degree, deinking agent or whitening agent.
Another object of the present invention, for providing a kind of papermaking process, mainly comprises the following steps:
A) moisture cellulosic papermaking slurry material is formed,
B) the above-mentioned fiber oxidation enzyme composition for improving Paper White Degree joined in paper making pulp react,
C) by step b) in the paper making pulp that obtains serve net, form page by filtrate by fibre solid component thus,
D) by page through squeeze section and dryer section, final production goes out paper product.
Wherein in some embodiments, step b) described in fiber oxidation enzyme dosage in fiber oxidation enzyme composition be dry finish 0.01-10 kilogram per ton, the consumption of auxiliary component is dry finish 0.05-10 kilogram per ton.
Wherein in some embodiments, step b) described in fiber oxidation enzyme dosage in fiber oxidation enzyme composition be dry finish 0.05-10 kilogram per ton, the consumption of auxiliary component is dry finish 0.1-10 kilogram per ton.
Wherein in some embodiments, step b) described in fiber oxidation enzyme dosage in fiber oxidation enzyme composition be dry finish 0.1-1 kilogram per ton.
Wherein in some embodiments, step b) described in fiber oxidation enzyme dosage in fiber oxidation enzyme composition be dry finish 0.1-0.5 kilogram per ton.
Wherein in some embodiments, the reaction times of described fiber oxidation enzyme composition and paper making pulp is 5-600 minute, pH is 3-10, and temperature is 20-80 DEG C.
Wherein in some embodiments, the reaction times of described fiber oxidation enzyme composition and paper making pulp is 20-300 minute, and reaction pH is 5-10, and temperature of reaction is 30-65 DEG C.
Wherein in some embodiments, the reaction times of described fiber oxidation enzyme composition and paper making pulp is 60-120 minute, and reaction pH is 8-10, and temperature of reaction is 50-65 DEG C.
A kind of fiber oxidation enzyme composition and papermaking process for improving Paper White Degree of the present invention and application has the following advantages and beneficial effect:
The present invention is through a large amount of experiment of contriver and research, show that fiber oxidation enzyme and composition thereof significantly can improve Paper White Degree, and determine best composition and the proportioning thereof of fiber oxidation enzyme composition, in the process of process old paper stock, add this fiber oxidation enzyme composition or fiber oxidation enzyme, the connecting key near fiber surface or ink ion can be changed, promote the swollen of fiber, the connection between fiber and ink is caused to weaken, again by suitable mechanical treatment, ink particle is made more intactly to depart from from fiber surface further, effective elimination is got final product again through washing or flotation.Simultaneously, fiber oxidation enzyme or its composition can also the decomposition of Catalytic lignin, due to the chromophoric group in lignin structure, it is the main source of slurrying color, and the decomposition of xylogen, fiber oxidation enzyme can destroy chromophoric group, thus significantly improves the whiteness of paper pulp, also significantly can reduce deinking agent used in prior art and the consumption for increasing the material that Paper White Degree adds.
Embodiment
Cellulolytic enzyme: " cellulolytic enzyme " in the present invention refers to all biological enzymes being carried out degraded cellulose by hydrolysis reaction, usually the terms such as cellulolytic enzyme and cellulase, fiber hydrolase and cellulase is used alternatingly at present.3 classes can be divided into according to the modes of action different during cellulose degraded substrate:
(1) endo cellulase is referred to as again endoglucanase (Endoglucanase, EG; EC 3.2.1.4);
(2) exocellulase is referred to as again cellobiohydrolase (Cellobiohydrolase, CBH; EC3.2.1.91);
(3) beta-glucosidase (β-glucosidase, BGL; EC 3.2.1.21).
A () endo cellulase is (also known as endoglucanase, endo-1,4-β-D-glucanase, EC 3.2.1.4), this fermentoid mainly acts on the noncrystalline domain of Mierocrystalline cellulose inside, random hydrolysis β-1,4-glycosidic link, by the brachymemma of long chain cellulose molecule, produce the small molecules Mierocrystalline cellulose of a large amount of non reducing end, its molecular size range is about 23-146KD;
B () exocellulase is (also known as exoglucanase, exo-1,4-β-D-glucanase, EC 3.2.1.91), this fermentoid acts on Mierocrystalline cellulose linear molecule end, hydrolysis β-1,4-D-14 glycosidic link, cuts next cellobiose molecule successively, therefore is also called cellobiohydrolase (cellobiohydrolase, CBH), molecular weight is about 38-118KD.
C () cellobiase (also known as beta-glucosidase, β-Isosorbide-5-Nitrae-glucosidase, EC 3.2.1.21), is called for short BG.The cellodextrin of cellobiose or solubility is generally hydrolyzed into glucose molecule by this fermentoid, and its molecular weight is about 76KD.
The enzymic activity (CMCase) of cellulase: in the present invention, the enzymic activity of cellulolytic enzyme refers to that cellulose degradation to be become the enzymic activity of the dextran in the ability of glucose, cellobiose and disaccharides at them by cellulose components.The activity of cellulase is generally determined with the reduction of the soltion viscosity of carboxymethyl cellulose.
Cellulose binding protein matter (cellulose binding protein, CBP): " cellulose binding protein matter " in the present invention refer to cellulose surface, there is special avidity, can be adsorbed on consumingly cellulose surface but itself does not have the protein of catalytic hydrolysis reaction activity to Mierocrystalline cellulose.In the literature, cellulose binding domain (Cellulose Binding Domain, CBD) is also called, cellulose binding module (Cellulose Binding Module, CBM), cellulose-binding domain, Mierocrystalline cellulose affinity structural domain.
Filament expansion albumen (Swollenin or Expansin): " filament expansion albumen " in the present invention refers to a kind of protein/polypeptide compound that the fibrous texture expansion of the natural substrate such as crystalline cellulose and hemicellulose can be made loose, the catalysis that this proteinoid is not degraded to Mierocrystalline cellulose, but the hydrolysis ability of cellulase to Microcrystalline Cellulose can be improved." filament expansion albumen " is also referred to as the filament expansion factor, English title Swollenin and Expansin, be a class plant cell wall expansion albumen, it has the non-hydrolytic activated protein in cellulase typical structure territory composition (containing cellulose binding structural domain (CBD)).The fiber expansin coming from plant mainly contains two classes, respectively called after α-expansin and β-expansin.Two types of fibers expansin has higher homology on structure and function: α-expansin molecular weight is about 25kDa, aminoacid sequence high conservative, and homology reaches 70% ~ 90%; β-expansin molecular weight is about 29kDa, but aminoacid sequence changes greatly.
Fiber oxidation enzyme (Cellulose Oxidative Enzymes): " fiber oxidation enzyme " in the present invention refers to glycan oxygenase (polysaccharide monooxygenase, PMO), described " glycan oxygenase " refers to that gang's molecular weight is in 20-50KDa, small molecules metalloenzyme (metalloenzyme) containing copper (II), the oxidizing reaction of oxygenation or dehydrogenation can be carried out with fiber surface, thus change the biological enzyme of fiber surface chemical property.Other title of glycan oxygenase comprises poly-glucose oxygenase or claims poly-glucose monooxygenase (polysaccharide monooxygenase, PMO), cracking performance glycan oxygenase (lytic polysaccharide monooxygenase, LPMO), and glucosides hydratase 61 race (glycosyl hydrolase 61, GH61).
The difference of fiber oxidation enzyme and cellulolytic enzyme is: cellulolytic enzyme is by being hydrolyzed reacting β-Isosorbide-5-Nitrae-D-14 glycosidic link, making cellulose degradation; And fiber oxidation enzyme is by carrying out redox reaction to Mierocrystalline cellulose, reacts the key mapping changed and be not limited to β-Isosorbide-5-Nitrae-D-14 glycosidic link.Although PMO was just found as far back as 1974, due to by CMCase (namely testing the activity methods of endo cellulase) analytical procedure, find that PMO is to β-1, the hydrolysis reaction of 4-D-14 glycosidic link is very faint, so people do not carry out more deep research understanding to the effect of this enzyme and its reaction mechanism, CAZy (Carbohydrate Active Enzymes, be called for short CAZy, http://www.cazy.org/) they are divided into Glycosyl Hydrolases 61 race (GH61).But, current research surface, PMO is actual is that a kind of copper-dependency list oxygen adds synthase (Copper-dependent monooxygenases, EC 1.14.17.x), it is acted on fiber by oxidizing reaction, and by hydrolysis reaction, fiber is acted on unlike common cellulolytic enzyme, therefore PMO is oxydase but not lytic enzyme.Classical cellulolytic enzyme has many enzyme races, on the contrary, PMO only has Liang Ge family, i.e. carbohydrate binding module family 33 (CBM33, Tan Shui binding domain family 33) and glycosyl hydrolase (GH61, glycoside hydrolase Families 61).PMO arranges and is divided into AA9 class and AA10 class biological enzyme by CAZy recently again.The former main source is fungi (fungus), and the latter mainly comes from bacterium, virus and some fungi.
PMO is present in the microorganism of a lot of lignin fiber degraded, can purify according to this and express, or carry out recombinant expressed by modern protein engineering techniques to zymoprotein.Such as, US Patent No. Pat.7,273,738, U.S. Patent application USA2009/099079, the U.S. Patent application USA2013/0052698 row sequences disclosing a series of new GH61 enzyme.US Patent No. 8,298,795 and U.S. Patent application USA2012/0083019 disclose from fungal host strain Myceliophthora thermophila (also known as Chrysosporium lucknowense) obtain restructuring GH61 albumen (recombinant GH61 proteins) and this GH61 of conbined usage and and cellulase (cellulase) compositions-treated lignocellulose material increase biorefining efficiency, improve the technology of alcohol output.So far, about the application of PMO is all at biorefining (biorefinery), the report that PMO applies in pulping and paper-making is not also had.
End in February, 2013, the database of CAZy have collected 249 kinds of PMO (i.e. GH61) Argine Monohydrochloride row order sequenced data, and major part belongs to ascus and belongs to bacterial strain (ascomycetous) and basidiomycetes (basidiomycetous).And show at the Search Results of NCBI/JGIBlast, have the genic system of 761 cover GH61 at present.Along with research is goed deep into, the data can predicting PMO can continue to increase sharply.
Fiber oxidation enzyme composition: " fiber oxidation enzyme composition " in the present invention refers to that said composition contains the following two kinds component, a component is glycan oxygenase (polysaccharide monooxygenase), with another one component be can keep or increase to dimension oxidase activity subsidiary, wherein this subsidiary can be one or more compounds of following compound, (1) the reaction substrate oxygen of fiber oxidation enzyme or oxygen release compound (oxygen precursors), (2) scavenging agent (radical scavengers) of reaction product, (3) fiber oxidation enzyme is had to the protein of promoter action.
" reaction substrate of fiber oxidation enzyme " of the present invention refers to except fiber, and glycan oxydase reacts necessary electron acceptor(EA)--oxygen; This reaction substrate can provide in the following way: oxygen, air or oxygen release compound, oxygen release compound in the present invention refers to superoxide or ozone, and wherein superoxide comprises hydrogen peroxide, sodium peroxide, calcium peroxide, Potassium peroxide.
" to fiber oxidation enzyme have the protein of promoter action " of the present invention refers to biological enzyme, cellulose binding protein and the filament expansion albumen that can increase glycan oxydase reaction activity; Wherein the biological enzyme of promoter action is had to refer to other class lytic enzyme (comprising amylase, polygalacturonase, lipase, esterase and zytase) except cellulolytic enzyme and oxydo-reductase (comprising cellobiose dehydrogenase, notatin, laccase and xylogen peroxidase) to glycan oxydase.
Cellulose oxidation enzyme composition involved in the present invention can be add respectively in paper-making process with the product of its single enzyme component, also two components can be added respectively different positions or be mixed into a formula for a product and add in paper-making process and agree to position, to reach best effect.
" kg/T " of the present invention refers to kilogram number added materials in oven dry stock per ton.
Described in following embodiment, raw material is conventional commercial product.
Below with reference to specific embodiment, the present invention will be further described.
Embodiment 1 fiber oxidation enzyme and compositions-treated ONP paper pulp thereof
One, experiment purpose
Fiber oxidation enzyme and composition thereof is evaluated on the impact of Paper White Degree by comparative analysis.
Two, experimental technique
(1) test materials prepares
Recovery old newspaper (ONP) and outdated magazine (OMG) waste paper mix according to the ratio of 80%:20%.200 grams of mixed waste papers and 1300 grams of plain boiled waters (are added CaCl 2regulate hardness to 400 PPM; Temperature 70 C), be placed in the hydrapulpter of 10 liters, then add caustic soda, pulping 7.5 minutes; After pulping, then add 2700 grams of plain boiled waters, join 5% slurry.
The GH61 that fiber oxidation enzyme (PMO) is provided by Dyadic company of the U.S., this enzyme is produced from bacterial strain Myceliophthora thermophila, its amino acid row sequence in US Patent No. 8,298,795 and U.S. Patent application USA2012/0083019 have detailed statement.
The commerical prod that notatin (Glucose Oxidase, GOX) is Genencor company of display drivers of DuPont group.
(2) papermaking
A, cellulase treatment condition: get above-mentioned 600 grams, the slurry prepared, put into 1000ml mixing agitator, control the temperature of slurry at 60 DEG C with radiator valve;
B, experimental group and control group are set,
Described control group is: add caustic soda 1-10kg/T in the slurry, water glass 15-30kg/T, hydrogen peroxide 10-20kg/T, deinking agent 0.5-3kg/T; (note: all consumptions are oven dry stock, in like manner following).
Described experiment component is 3 groups, wherein,
Experimental group 1 is: add fiber oxidation enzyme (PMO) 150-300g/T (oven dry stock) in the slurry, deinking agent 0.5kg/T, add caustic soda 2kg/T, water glass 15kg/T, hydrogen peroxide 10kg/T;
Experimental group 2 is: add notatin 250-500g/T in the slurry, and deinking agent 1kg/T adds caustic soda 2kg/T, water glass 15kg/T, hydrogen peroxide 10kg/T;
Experimental group 3 is: add fiber oxidation enzyme and notatin combined treatment in the slurry, and PMO 150-300g/T, GOX 250-500g/T, deinking agent 0.5kg/T, add caustic soda 1-2kg/T, water glass 15kg/T, hydrogen peroxide 10kg/T;
Above-mentioned reaction conditions is: temperature is 60 DEG C, and the reaction times is 90 minutes, and reaction pH is 8-10, and constant speed stirs.
C, deinking test: get and will join Denver's formula flotation machine of 3 liters with spreading mass, add plain boiled water (50 DEG C, 400 PPM hardness) diluted slurry is to about 1%, be uniformly mixed 3 minutes, then pressurized air valve and adjust flux is opened to the even tiny bubble of formation and stable foam layer, scraped by foam, flotation time is 4 minutes, obtains Deinking Pulp.
D, handsheet prepare and ionization meter: by the above-mentioned Deinking Pulp prepared, add tap water be diluted to 1.0% slurry dense, mixing, measuring tempeature and slurry concentration, by TAPPI method, accurately preparation 10-12 opens the handsheet of 6.5 grammes per square metres.After oven dry, handsheet to be placed in the controlling box of constant temperature and constant humidity degree 24 hours, then measures its whiteness by TAPPI measuring method.
Three, experimental result
Result see table 1, as can be seen from Table 1: conventional deinking raw material, PMO and GOX separately or conbined usage process old paper stock on the impact of deinking efficiency.Reduce 80% at amount of caustic soda, water glass reduces 50% and under hydrogen peroxide reduces by the condition of 50%, and after fiber oxidation enzyme and compositions-treated thereof, the whiteness of paper just had remarkable increase before flotation, and comparison improves 2-4%ISO than the whiteness of condition; After flotation, whiteness increase is more remarkable, and comparison improves 3-4%ISO than condition.Add separately GOX process, the whiteness of paper increases comparison and slightly improves than condition, but not remarkable.When fiber oxidation enzyme and notatin conbined usage, most pronounced effects, the whiteness of its paper reaches more than 54%ISO.
Table 1 fiber oxidation enzyme and the impact of notatin conbined usage process reclaimed waste paper slurry on paper physical index
The above embodiment only have expressed several embodiment of the present invention, and it describes comparatively concrete and detailed, but therefore can not be interpreted as the restriction to the scope of the claims of the present invention.It should be pointed out that for the person of ordinary skill of the art, without departing from the inventive concept of the premise, can also make some distortion and improvement, these all belong to protection scope of the present invention.Therefore, the protection domain of patent of the present invention should be as the criterion with claims.

Claims (10)

1. for improving a fiber oxidation enzyme composition for Paper White Degree, it is characterized in that, comprising following composition:
I) fiber is had to the biological enzyme component of oxidative function, described biological enzyme component is the fiber oxidation enzyme being changed property of fiber surface by redox reaction; With
Ii) fiber oxidation enzyme is had to the auxiliary component increasing catalytic activity, described auxiliary component is the reaction substrate of fiber oxidation enzyme;
The weight ratio of described biological enzyme component and auxiliary component is 1:1-100.
2. the fiber oxidation enzyme composition for improving Paper White Degree according to claim 1, it is characterized in that, described fiber oxidation Mei Shi gang molecular weight is at 20-50KDa, the glycan oxygenase with the dependent small molecules metalloenzyme of copper, and the reaction substrate of described fiber oxidation enzyme is oxygen, air or oxygen release compound; Described oxygen release compound is superoxide or ozone.
3. the fiber oxidation enzyme composition for improving Paper White Degree according to claim 2, is characterized in that, described superoxide is at least one in hydrogen peroxide, sodium peroxide, calcium peroxide or Potassium peroxide.
4. the fiber oxidation enzyme composition for improving Paper White Degree according to claim 1, is characterized in that, the weight ratio of described biological enzyme component and auxiliary component is 1:30-70.
5. the fiber oxidation enzyme composition for improving Paper White Degree according to any one of claim 1-4, it is characterized in that, described fiber oxidation enzyme composition also comprises protein fiber oxidation enzyme to promoter action, the described protein having a promoter action to fiber oxidation enzyme is have the biological enzyme of catalytic activity or the cellulose binding protein of catalytically inactive, and in described fiber oxidation enzyme composition, the weight ratio of fiber oxidation enzyme and protein fiber oxidation enzyme to promoter action is 1:(0.5-3).
6. the fiber oxidation enzyme composition for improving Paper White Degree according to claim 5, it is characterized in that, the described biological enzyme having catalytic activity is oxydo-reductase, is selected from one or more in cellobiose dehydrogenase, laccase, notatin, Catalase, alcohol dehydrogenase or xylogen peroxidase; Or described in have the biological enzyme of catalytic activity to be the hydratase of non-cellulose lytic enzyme, be selected from one or more in amylase, zytase, polygalacturonase or esterase.
7. the fiber oxidation enzyme composition for improving Paper White Degree according to claim 5, is characterized in that, the protein of described catalytically inactive is Fiberonectin and/or filament expansion albumen.
8. fiber oxidation enzyme or the fiber oxidation enzyme composition as described in any one of claim 1-7 in paper technology as the application improving the SYNTHETIC OPTICAL WHITNER of Paper White Degree, deinking agent or whitening agent.
9. a papermaking process, is characterized in that, mainly comprises the following steps:
A) moisture cellulosic papermaking slurry material is formed,
B) the fiber oxidation enzyme composition being improved Paper White Degree being used for described in any one of claim 1-7 joins in paper making pulp and reacts,
C) by step b) in the paper making pulp that obtains serve net, form page by filtrate by fibre solid component thus,
D) by page through squeeze section and dryer section, final production goes out paper product.
10. papermaking process according to claim 9, is characterized in that, step b) described in fiber oxidation enzyme dosage in fiber oxidation enzyme composition be dry finish 0.01-10 kilogram per ton, the consumption of auxiliary component is dry finish 0.05-10 kilogram per ton; And/or
The time of described fiber oxidation enzyme composition and paper making pulp reaction is 5-600 minute, pH is 3-10, and temperature is 20-80 DEG C.
CN201410366880.4A 2013-07-29 2014-07-29 For improving fiber oxidation enzymatic compositions and papermaking process and the application of Paper White Degree Active CN104342425B (en)

Priority Applications (2)

Application Number Priority Date Filing Date Title
CN201410366880.4A CN104342425B (en) 2013-07-29 2014-07-29 For improving fiber oxidation enzymatic compositions and papermaking process and the application of Paper White Degree
PCT/CN2015/084456 WO2016015571A1 (en) 2014-07-29 2015-07-20 Fiber oxidase composition used for improving whiteness of paper, papermaking method, and applications of the composition

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
CN2013103238534 2013-07-29
CN201310323853.4 2013-07-29
CN201310323853 2013-07-29
CN201410366880.4A CN104342425B (en) 2013-07-29 2014-07-29 For improving fiber oxidation enzymatic compositions and papermaking process and the application of Paper White Degree

Publications (2)

Publication Number Publication Date
CN104342425A true CN104342425A (en) 2015-02-11
CN104342425B CN104342425B (en) 2017-11-28

Family

ID=51959822

Family Applications (3)

Application Number Title Priority Date Filing Date
CN201410366880.4A Active CN104342425B (en) 2013-07-29 2014-07-29 For improving fiber oxidation enzymatic compositions and papermaking process and the application of Paper White Degree
CN201410366879.1A Active CN104342424B (en) 2013-07-29 2014-07-29 For changing and improving fiber oxidation enzymatic compositions and papermaking process and the application of fibre property
CN201410368089.7A Active CN104178474B (en) 2013-07-29 2014-07-29 For changing the fiber oxidation enzymatic compositions with improvement fibre property and papermaking process and application

Family Applications After (2)

Application Number Title Priority Date Filing Date
CN201410366879.1A Active CN104342424B (en) 2013-07-29 2014-07-29 For changing and improving fiber oxidation enzymatic compositions and papermaking process and the application of fibre property
CN201410368089.7A Active CN104178474B (en) 2013-07-29 2014-07-29 For changing the fiber oxidation enzymatic compositions with improvement fibre property and papermaking process and application

Country Status (1)

Country Link
CN (3) CN104342425B (en)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2016015571A1 (en) * 2014-07-29 2016-02-04 瑞辰星生物技术(广州)有限公司 Fiber oxidase composition used for improving whiteness of paper, papermaking method, and applications of the composition

Families Citing this family (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2016015570A1 (en) * 2014-07-29 2016-02-04 瑞辰星生物技术(广州)有限公司 Fiber oxidase composition used for altering and improving whiteness of paper, papermaking method, and applications of the composition
WO2016015569A1 (en) * 2014-07-29 2016-02-04 瑞辰星生物技术(广州)有限公司 Fiber oxidase composition used for altering and improving whiteness of paper, papermaking method, and applications of the composition
CN106269818A (en) * 2016-11-11 2017-01-04 无限极(中国)有限公司 The processing method of a kind of Chinese medicine dreg and application
BR112019010355B1 (en) * 2016-11-24 2024-03-05 Dsm Ip Assets B.V. ENZYME COMPOSITION
CN107419578B (en) * 2017-06-21 2020-02-07 昆明理工大学 Method for improving pulping effect of oxygen-alkali method by cellulase pretreatment
CN108755216B (en) * 2018-05-07 2021-04-13 希杰尤特尔(山东)生物科技有限公司 Method for improving the fiber strength of hardwood pulp by using compound enzymes
CN109730350A (en) * 2019-03-05 2019-05-10 湖北中烟工业有限责任公司 Method for improving the quality of paper-making reconstituted tobacco leaves by using Fe-CA/H2O2 imitation enzyme system
CN119434022A (en) * 2024-10-21 2025-02-14 中冶纸业银河有限公司 A method for making paper surface superhydrophobic based on polyphenols modified by bio-enzymes

Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN102086611A (en) * 2010-11-30 2011-06-08 王祥槐 Composition for changing and improving property of fiber surface and paper making method
WO2012068236A2 (en) * 2010-11-16 2012-05-24 Dyadic International (Usa) Inc. Novel fungal oxidoreductases
WO2012093149A2 (en) * 2011-01-06 2012-07-12 Dsm Ip Assets B.V. Novel cell wall deconstruction enzymes and uses thereof
WO2012130950A1 (en) * 2011-04-01 2012-10-04 Dsm Ip Assets B.V. Novel cell wall deconstruction enzymes of talaromyces thermophilus and uses thereof

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CA2736661A1 (en) * 2007-09-07 2009-03-12 Dyadic International, Inc. Novel fungal enzymes
HUE033334T2 (en) * 2010-08-20 2017-11-28 Codexis Inc Use of glycoside hydrolase-61 proteins in cellulose processing
CA2847879C (en) * 2011-09-09 2020-06-23 Novozymes A/S Improving properties of paper materials
WO2013090430A1 (en) * 2011-12-12 2013-06-20 Regents Of The University Of Minnesota Lignin degrading methods

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2012068236A2 (en) * 2010-11-16 2012-05-24 Dyadic International (Usa) Inc. Novel fungal oxidoreductases
CN102086611A (en) * 2010-11-30 2011-06-08 王祥槐 Composition for changing and improving property of fiber surface and paper making method
WO2012093149A2 (en) * 2011-01-06 2012-07-12 Dsm Ip Assets B.V. Novel cell wall deconstruction enzymes and uses thereof
WO2012130950A1 (en) * 2011-04-01 2012-10-04 Dsm Ip Assets B.V. Novel cell wall deconstruction enzymes of talaromyces thermophilus and uses thereof

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2016015571A1 (en) * 2014-07-29 2016-02-04 瑞辰星生物技术(广州)有限公司 Fiber oxidase composition used for improving whiteness of paper, papermaking method, and applications of the composition

Also Published As

Publication number Publication date
CN104342425B (en) 2017-11-28
CN104342424B (en) 2017-12-01
CN104178474B (en) 2018-05-18
CN104342424A (en) 2015-02-11
CN104178474A (en) 2014-12-03

Similar Documents

Publication Publication Date Title
CN104342425B (en) For improving fiber oxidation enzymatic compositions and papermaking process and the application of Paper White Degree
Pérez et al. Biodegradation and biological treatments of cellulose, hemicellulose and lignin: an overview
Umikalsom et al. The treatment of oil palm empty fruit bunch fibre for subsequent use as substrate for cellulase production by Chaetomium globosum Kunze
Palonen Role of lignin in the enzymatic hydrolysis of lignocellulose
Ibarra et al. Enzymatic deinking of secondary fibers: cellulases/hemicellulases versus laccase-mediator system
Marques et al. Characterisation and application of glycanases secreted by Aspergillus terreus CCMI 498 and Trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
Maity et al. Xylanase isozymes from the newly isolated Bacillus sp. CKBx1D and optimization of its deinking potentiality
Madlala et al. Xylanase-induced reduction of chlorine dioxide consumption during elemental chlorine-free bleaching of different pulp types
Chapla et al. Assessment of a thermostable xylanase from Paenibacillus sp. ASCD2 for application in prebleaching of eucalyptus kraft pulp
Garg et al. Bleach-boosting effect of crude xylanase from Bacillus stearothermophilus SDX on wheat straw pulp
Nathan et al. Low Molecular Weight Xylanase from Trichoderma viride VKF3 for Bio-bleaching of Newspaper Pulp.
Das et al. Cellulase activity of a novel bacterial strain Arthrobacter woluwensis TDS9: its application on bioconversion of paper mill sludge
Tuli et al. Current status and future scope of microbial cellulases
Dhiman et al. ‘Single lay out’and ‘mixed lay out’enzymatic processes for bio-bleaching of kraft pulp
Hamisan et al. Delignification of Oil Palm Empty Fruit Bunch using Chemical and
CN102108644B (en) Pollution-free production process of plant fiber pulp
Lee et al. Evaluation of enzymatic deinking of non-impact ink laser-printed paper using crude enzyme from Penicillium rolfsii c3-2 (1) IBRL
CN106436417B (en) Composition and papermaking method for controlling deposition of organic pollutants in pulp and paper production
JP4730933B2 (en) Cellulase deinking method for waste paper without paper strength reduction and its evaluation method
Chen Biological fundamentals for the biotechnology of lignocellulose
Kumar et al. Microbial enzymes in paper and pulp industries for bioleaching application
Prasetyo et al. Efficient cellulase-catalyzed saccharification of untreated paper sludge targeting for biorefinery
US9963824B2 (en) Methods for deinking wastepaper by combined use of cutinase and chemical reagents
Yakubu et al. Industrial application of alkaline cellulase enzymes in pulp and paper recycling: a review
CN113462227A (en) Biological enzyme preparation for deinking waste paper, preparation method and deinking process

Legal Events

Date Code Title Description
C06 Publication
PB01 Publication
C10 Entry into substantive examination
SE01 Entry into force of request for substantive examination
GR01 Patent grant
GR01 Patent grant