CN104342425B - For improving fiber oxidation enzymatic compositions and papermaking process and the application of Paper White Degree - Google Patents

For improving fiber oxidation enzymatic compositions and papermaking process and the application of Paper White Degree Download PDF

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CN104342425B
CN104342425B CN201410366880.4A CN201410366880A CN104342425B CN 104342425 B CN104342425 B CN 104342425B CN 201410366880 A CN201410366880 A CN 201410366880A CN 104342425 B CN104342425 B CN 104342425B
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enzyme
fiber oxidation
fiber
enzymatic compositions
component
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CN104342425A (en
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王祥槐
谢焱
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Rui Xing Biotechnology (guangzhou) Co Ltd
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Rui Xing Biotechnology (guangzhou) Co Ltd
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Abstract

The invention discloses a kind of fiber oxidation enzymatic compositions and papermaking process and application for being used to improve Paper White Degree, the fiber oxidation enzymatic compositions are mainly composed of the following components:There is the biology enzyme component of oxidative function to fiber, the biology enzyme component is to change the fiber oxidation enzyme of property of fiber surface by redox reaction;With the helper component to fiber oxidation enzyme with increase catalytic activity, the helper component is the reaction substrate of fiber oxidation enzyme;Present invention also offers the method that above-mentioned composition is used for papermaking.The compositions-treated paper pulp, can make the whiteness of obtained paper be significantly improved.

Description

For improving fiber oxidation enzymatic compositions and papermaking process and the application of Paper White Degree
Technical field
Improve the technical field of fibrous physics chemical property the present invention relates to biology enzyme and using biology enzyme, specifically, relate to A kind of and fiber oxidation enzymatic compositions and papermaking process and application for being used to improve Paper White Degree.
Background technology
China paper industry keeps high growth rate in continuous 10 years between 2000-2010, to China's paper in 2011 and cardboard Output and consumption figure more than 100,000,000 tons, rank first in the world.The constitutive material of Paper or cardboard is mainly fiber, due to Slurrying, papermaking need substantial amounts of raw material, and environment are had a certain impact, and countries in the world paper industry is all made in compression at present Slurry production, it is slow plus internal sources woods construction of base to ensure the forest reserves, it is limited for material, rather than wood pulp development is by clear The influence of clean production new technology exploitation hysteresis, the constraint of resource, the energy and environment that China paper industry development faces are increasingly prominent It is aobvious.
And waste paper can both protect forest resources certain as a kind of recycling secondary stock resource, recovery papermaking Alleviate great demand pressure of the paper industry development to natural resources in degree, and can reduces the consumption of water and the energy, reduces ring Pollute in border.Recycling dynamics of the China to waste paper resources is also increasing year by year, is counted according to Chinese papermaking association, and 2002 complete In state's paper pulp consumption, secondary stock ratio only accounts for 47%, and secondary stock consumes 56,600,000 tons within 2011, accounts for the ratio of national paper pulp consumption Example rises to 62%, and therefore, the research of deinking receives more and more attention as the committed step of Waste Paper Handling.
Traditional Chemical Deinking is to add the chemistry such as sodium hydroxide, sodium metasilicate, hydrogen peroxide, chelating agent and surfactant Reagent, in the basic conditions various chemokineses promote ink to be saponified and come off from fiber, then utilize flotation or washing Method ink is removed.Deinking agent is mainly used in destroying ink to the adhesion of fiber in waste paper recycling, makes ink from fibre Peel off and be dispersed in water in dimension.Chemical Deinking method is due to using compared with multi-chemistry, can not only cause pollution environment, and discomfort For laser printing and the wastepaper duplicated.Mixed Office WasteMOW using laser printing and xerography as representative, because table Face degree of sizing is high, ink melt on fiber, only by conventional flotation and washing by mechanical agitation and phase mutual friction be difficult by Ink detachment.The introducing of biology enzyme can suitably interrupt the connection between ink and fiber and be allowed to depart from fiber surface, improve The whiteness of secondary stock, while improve the physical property of paper.
In the past few decades, many enzymes (such as cellulase/hemicellulose, lipase, laccase) are in deinking The substitutability of chemical method has been studied in recovery industry.The deinking mechanism of various enzymes is different and waits further to grind Study carefully, what is more accepted at present is:The noncrystalline domain part on cellulase/hemicellulase hydrolysis fiber surface, make ink and fibre Connection between dimension dies down, so as to be advantageous to separate;Lipase targetedly degrades the oil based vehicles in ink, makes in ink Carbon black and pigment shed, depart from from paper.Lignin-degrading enzymes, such as laccase, it can optionally remove the wood of paper surface Quality, so as to promote the removing of ink.Enzymatic deinking agent is that a variety of highly effective biological zymes compounding preferably with strong points forms, with Enzyme activition special assistant is used cooperatively, the deinking for newspaper, Mixed Office WasteMOW, books, magazine etc..
Compared with traditional chemical deinking, enzymatic deinking has the advantages of a series of prominent:1. enzymatic deinking condition temperature With chemicals usage is few, and fiber loss is small, keeps good fiber properties;2. COD of sewage and BOD is greatly lowered, mitigate dirty Water process pressure;3. improve paper pulp yield and improve paper strength;4. clean manufacturing, saving the energy, material consumption is reduced;5. use letter It is single, matched with existing most of deinking process.At present, enzymatic deinking agent is applied to paper-making deinking field;But using existing The action effect for having the biology enzyme in technology is only limited to improve dissociation of the ink point from fiber surface.
The content of the invention
Based on this, an object of the present invention is a kind of fiber oxidation enzymatic compositions for being used to improve Paper White Degree of offer.
The concrete technical scheme for solving above-mentioned technical problem is as follows:
A kind of fiber oxidation enzymatic compositions for being used to improve Paper White Degree, including consisting of:
I) there is the biology enzyme component of oxidative function to fiber, the biology enzyme component is to change by redox reaction Become the fiber oxidation enzyme of property of fiber surface;With
Ii) there is the helper component of increase catalytic activity to fiber oxidation enzyme, the helper component is fiber oxidation enzyme Reaction substrate;
The weight ratio of the biology enzyme component and helper component is 1:1-100.
In wherein some embodiments, the fiber oxidation enzyme be family's molecular weight in 20-50KDa, there is copper dependence Small molecule metalloenzyme glycan oxygenase, the reaction substrate of the fiber oxidation enzyme is oxygen, air or oxygen releaseization Compound;The oxygen release compound is peroxide or ozone.
In wherein some embodiments, the peroxide is hydrogen peroxide, sodium peroxide, calper calcium peroxide or potassium peroxide At least one of.
In wherein some embodiments, the weight ratio of the biology enzyme component and helper component is 1:1-75.
In wherein some embodiments, the weight ratio of the biology enzyme component and helper component is 1:20-75.
In wherein some embodiments, the weight ratio of the biology enzyme component and helper component is 1:30-70.
In wherein some embodiments, the fiber oxidation enzymatic compositions also include having facilitation to fiber oxidation enzyme Protein, the protein to fiber oxidation enzyme with facilitation is the biology enzyme or catalytically inactive for having catalytic activity Cellulose binding protein.
In wherein some embodiments, the biology enzyme for having a catalytic activity is oxidoreducing enzyme, is taken off selected from cellobiose One or more in hydrogen enzyme, laccase, glucose oxidase, Catalase, alcohol dehydrogenase or lignin peroxidase; Or it is described have a catalytic activity biology enzyme be non-cellulose hydrolase hydrase, selected from amylase, zytase, pectase or One or more in esterase.
Fiber oxidation enzyme and have in wherein some embodiments, in the fiber oxidation enzymatic compositions to fiber oxidation enzyme The weight ratio of the protein of facilitation is 1:(0.5-3).
In wherein some embodiments, the protein of the catalytically inactive is fibronectin and/or filament expansion Albumen.
Another object of the present invention is made to provide a kind of fiber oxidation enzymatic compositions or fiber oxidation enzyme in paper technology To improve the bleaching agent of Paper White Degree, deinking agent or the application of brightening agent.
Another object of the present invention mainly includes the following steps that to provide a kind of papermaking process:
A) aqueous cellulosic papermaking slurry material is formed,
B) the above-mentioned fiber oxidation enzymatic compositions for improving Paper White Degree are added in paper making pulp and reacted,
C) paper making pulp obtained in step b) is served into net, paper is formed by fibre solid component from there through water is filtered out Page,
D) page is passed through into squeeze section and dryer section, final production goes out paper product.
In wherein some embodiments, the fiber oxidation enzyme dosage described in step b) in fiber oxidation enzymatic compositions is every 0.01-10 kilograms of dry finish of ton, the dosage of helper component is 0.05-10 kilograms of dry finish per ton.
In wherein some embodiments, the fiber oxidation enzyme dosage described in step b) in fiber oxidation enzymatic compositions is every 0.05-10 kilograms of dry finish of ton, the dosage of helper component is 0.1-10 kilograms of dry finish per ton.
In wherein some embodiments, the fiber oxidation enzyme dosage described in step b) in fiber oxidation enzymatic compositions is every 0.1-1 kilograms of dry finish of ton.
In wherein some embodiments, the fiber oxidation enzyme dosage described in step b) in fiber oxidation enzymatic compositions is every 0.1-0.5 kilograms of dry finish of ton.
In wherein some embodiments, the reaction time of the fiber oxidation enzymatic compositions and paper making pulp is 5-600 points Clock, pH 3-10, temperature are 20-80 DEG C.
In wherein some embodiments, the reaction time of the fiber oxidation enzymatic compositions and paper making pulp is 20-300 points Clock, reaction pH are 5-10, and reaction temperature is 30-65 DEG C.
In wherein some embodiments, the reaction time of the fiber oxidation enzymatic compositions and paper making pulp is 60-120 points Clock, reaction pH are 8-10, and reaction temperature is 50-65 DEG C.
A kind of fiber oxidation enzymatic compositions for being used to improve Paper White Degree and papermaking process of the present invention and application have Advantages below and beneficial effect:
The present invention is largely tested and studied through inventor, show that fiber oxidation enzyme and combinations thereof can significantly improve paper Whiteness, and the best composition and its proportioning of fiber oxidation enzymatic compositions are determined, during old paper stock is handled, adding should Fiber oxidation enzymatic compositions or fiber oxidation enzyme, the connecting key near fiber surface or ink ion can be changed, promote fiber Swollen, cause the connection between fiber and ink to weaken, then by appropriate mechanical treatment, further compare ink particle Intactly depart from from fiber surface, then scrubbed or flotation can be removed effectively.Meanwhile fiber oxidation enzyme or its composition can also The decomposition of Catalytic lignin, it is the main source of slurrying color due to the chromophoric group in lignin structure, and point of lignin Solution, fiber oxidation enzyme can destroy chromophoric group, so as to significantly improve the whiteness of paper pulp, can also substantially reduce in the prior art Deinking agent used and the dosage of the material added for increase Paper White Degree.
Embodiment
Cellulolytic enzyme:" cellulolytic enzyme " in the present invention refer to it is all by hydrolysis come degradation of fibers The biology enzyme of element, is at present usually used alternatingly the terms such as cellulolytic enzyme and cellulase, fiber hydrolase and cellulase. The different modes of action can be divided into 3 classes during according to cellulose degraded substrate:
(1) endo cellulase is also referred to as endoglucanase (Endoglucanase, EG;EC 3.2.1.4);
(2) exocellulase is also referred to as cellobiohydrolase (Cellobiohydrolase, CBH; EC3.2.1.91);
(3) beta-glucosidase (β-glucosidase, BGL;EC 3.2.1.21).
(a) endo cellulase (also known as endoglucanase, endo-1,4- β-D-glucanase, EC 3.2.1.4), The noncrystalline domain that the fermentoid is mainly acted on inside cellulose, random hydrolysis β-Isosorbide-5-Nitrae-glycosidic bond, long chain cellulose molecule is cut It is short, the small molecule cellulose of a large amount of non reducing ends is produced, its molecular size range is about 23-146KD;
(b) exocellulase (also known as exoglucanase, exo-1,4- β-D-glucanase, EC 3.2.1.91), Such enzyme effect hydrolyzes β-Isosorbide-5-Nitrae-D-14 glycosidic bonds, cuts next cellobiose molecule successively in cellulose linear molecule end, Therefore also known as cellobiohydrolase (cellobiohydrolase, CBH), molecular weight about 38-118KD.
(c) cellobiase (also known as beta-glucosidase, β-Isosorbide-5-Nitrae-glucosidase, EC 3.2.1.21), abbreviation BG. The cellodextrin of cellobiose or solubility is typically hydrolyzed into glucose molecule by this fermentoid, and its molecular weight is about 76KD.
The enzymatic activity (CMCase) of cellulase:The enzymatic activity of cellulolytic enzyme refers to cellulose components in the present invention They by cellulose degradation into glucose, cellobiose and disaccharides ability in terms of dextran enzymatic activity.Cellulase Activity typically determined with the reduction of the solution viscosity of carboxymethyl cellulose.
Cellulose binding protein matter (cellulose binding protein, CBP):" cellulose combination in the present invention Protein " refer to there is cellulose surface special affinity, can be strongly adsorbed to cellulose surface but itself to fibre Protein of the dimension element without catalytic hydrolysis reaction activity.In the literature, also known as cellulose binding domain (Cellulose Binding Domain, CBD), cellulose binding module (Cellulose Binding Module, CBM), cellulose absorption knot Structure domain, cellulose affinity domain.
Filament expansion albumen (Swollenin or Expansin):" filament expansion albumen " in the present invention refers to one kind The fibre structure of the natural substrates such as avicel cellulose and hemicellulose can be made to expand loose protein/polypeptide compound, this kind of egg Catalysis to cellulose without degraded in vain, but hydrolysis ability of the cellulase to microcrystalline cellulose can be improved." filament expansion Albumen " is also referred to as the filament expansion factor, and English claims Swollenin and Expansin, is a kind of plant cell wall extension albumen, its Non-hydrolytic activated protein with cellulase typical structure domain composition (containing cellulose binding structural domain (CBD)).Come from plant Fiber expansin mainly have two classes, be respectively designated as α-expansin and β-expansin.Two types of fibers expansin exists Structurally and functionally there is higher homology:α-expansin molecular weight about 25kDa, amino acid sequence is highly conserved, homology Up to 70%~90%;β-expansin molecular weight about 29kDa, but amino acid sequence changes greatly.
Fiber oxidation enzyme (Cellulose Oxidative Enzymes):" fiber oxidation enzyme " in the present invention refers to gather Glycosyloxy synthase (polysaccharide monooxygenase, PMO), " the glycan oxygenase " refer to that family's molecular weight exists 20-50KDa, the small molecule metalloenzyme (metalloenzyme) containing copper (II), oxygenation or dehydrogenation can be carried out with fiber surface Oxidation reaction, so as to change the biology enzyme of fiber surface chemical property.Other titles of glycan oxygenase add including poly- glucose Oxygenase claims poly- glucose monooxygenase (polysaccharide monooxygenase, PMO), cracking performance glycan oxygenase (lytic polysaccharide monooxygenase, LPMO), and the race (glycosyl of glucosides hydrase 61 hydrolase 61,GH61)。
The difference of fiber oxidation enzyme and cellulolytic enzyme is:Cellulolytic enzyme is by β -1,4-D-14 glucosides Reaction is hydrolyzed in key, makes cellulose degradation;And fiber oxidation enzyme is by carrying out redox reaction to cellulose, reacting institute The key mapping of change is not limited to β -1,4-D-14 glycosidic bonds.Although PMO is early in 1974 just advantageously, it has been found that due to CMCase (activity methods for testing endo cellulase) analysis method, it is found that PMO is non-to the hydrolysis of β-Isosorbide-5-Nitrae-D-14 glycosidic bonds It is often faint, then people do not have to carry out to the effect of the enzyme and its reaction mechanism deeper into research understanding, CAZy (Carbohydrate Active Enzymes, abbreviation CAZy, http://www.cazy.org/) they are divided into The races of Glycosyl Hydrolases 61 (GH61).However, current research surface, PMO is really that a kind of copper-dependence list oxygen adds Synthase (Copper-dependent monooxygenases, EC 1.14.17.x), it is that fiber is entered by oxidation reaction Row effect, fiber is acted on by hydrolysis like that rather than common cellulolytic enzyme, therefore PMO is oxidation Enzyme rather than hydrolase.Classical cellulolytic enzyme has many enzyme races, on the contrary, PMO only has Liang Ge families, i.e., Carbohydrate binding module family 33 (CBM33, Tan Shui binding domain family 33) and glycosyl Hydrolase (GH61, glycoside hydrolase Families 61).CAZy recently arranges PMO again is divided into AA9 classes and AA10 class biology enzymes. The former main source is fungi (fungus), and the latter mostlys come from bacterium, virus and some fungies.
PMO is present in the microorganism of many lignin fiber degradeds, can purify and express according to this, or pass through modern egg White engineering technology recombinantly expresses to zymoprotein.For example, United States Patent (USP) US Pat.7,273,738, U.S. Patent application USA2009/099079, U.S. Patent application USA2013/0052698 disclose a series of row sequence of new GH61 enzymes.The U.S. Patent US8,298,795 and U.S. Patent application USA2012/0083019 are disclosed from fungal host strain Myceliophthora thermophila (also known as Chrysosporium lucknowense) obtain restructuring GH61 albumen (recombinant GH61 proteins) and be used in combination the GH61 and with cellulase (cellulase) composition Manage lignocellulose material increase biorefining efficiency, improve the technology of alcohol output.So far, the application about PMO is all in life Thing refines (biorefinery), the report also applied without PMO in pulping and paper-making.
Cut-off 2 months 2013, CAZy database have collected 249 kinds of PMO (i.e. GH61) Argine Monohydrochloride row ordinal numbers According to largely belonging to ascus category bacterial strain (ascomycetous) and basidiomycetes (basidiomycetous).And in NCBI/ JGIBlast search result is shown, shares 761 sets of GH61 genic system at present.With research deeply, it is anticipated that PMO's Data may proceed to increase sharply.
Fiber oxidation enzymatic compositions:" fiber oxidation enzymatic compositions " in the present invention refer to that said composition contains the following two kinds Component, a component is glycan oxygenase (polysaccharide monooxygenase), and another component is to protect Hold or increase the adminicle to tieing up oxidase active, the wherein adminicle can be one or more chemical combination of following compound Thing, reaction substrate oxygen or oxygen the release compound (oxygen precursors) of (1) fiber oxidation enzyme, (2) reaction production The scavenger (radical scavengers) of thing and (3) have the protein of facilitation to fiber oxidation enzyme.
" reaction substrate of fiber oxidation enzyme " of the present invention refers to that in addition to fiber glycan oxidizing ferment reacts must Electron acceptor -- the oxygen needed;The reaction substrate can provide in the following way:Oxygen, air or oxygen release chemical combination Thing, the oxygen release compound in the present invention refer to peroxide or ozone, and wherein peroxide includes hydrogen peroxide, peroxide Change sodium, calper calcium peroxide, potassium peroxide.
The present invention's refers to increase glycan oxydase reaction work " to the protein for having facilitation of fiber oxidation enzyme " Biology enzyme, cellulose binding protein and the filament expansion albumen of property;The biology enzyme for wherein having facilitation to glycan oxidizing ferment is Refer to other class hydrolases (including amylase, pectase, lipase, esterase and zytase) in addition to cellulolytic enzyme With oxidoreducing enzyme (including cellobiose dehydrogenase, glucose oxidase, laccase and lignin peroxidase).
Cellulose oxidation enzymatic compositions involved in the present invention can be separately added into make with the product of its single enzyme component During paper, two components can also be separately added into different positions or be mixed into a product formula addition paper-making process Middle agreement position, to reach optimal effect.
" kg/T " of the present invention refers to kilogram number to be added materials in oven dry stock per ton.
Raw material described in following embodiments is conventional commercial product.
Below with reference to specific embodiment, the present invention will be further described.
Fiber oxidation enzyme of embodiment 1 and combinations thereof handles ONP paper pulp
First, experiment purpose
Influence of the fiber oxidation enzyme and combinations thereof to Paper White Degree is evaluated by comparative analysis.
2nd, experimental method
(1) test material prepares
Old newspaper (ONP) and outdated magazine (OMG) waste paper is reclaimed according to 80%:20% ratio is mixed.It is mixed by 200 grams Close waste paper and 1300 grams of plain boiled waters (add CaCl2Hardness is adjusted to 400 PPM;Temperature 70 C), it is placed on 10 liters of hydraulic pulping In machine, caustic soda, pulping 7.5 minutes are added;After pulping, then add 2700 grams of plain boiled waters, with 5% slurry.
The GH61 that fiber oxidation enzyme (PMO) is provided by Dyadic companies of the U.S., the enzyme is from bacterial strain Myceliophthora Thermophila is produced, and its amino acid row sequence is in United States Patent (USP) US8,298,795 and U.S. Patent application USA2012/ 0083019 has detailed statement.
Glucose oxidase (Glucose Oxidase, GOX) is the business of Genencor companies of display drivers of DuPont groups Industry product.
(2) papermaking
A, cellulase treatment condition:Above-mentioned 600 grams of the slurry prepared is taken, is put into 1000ml mixing agitators, with constant temperature control The temperature of device control slurry processed is at 60 DEG C;
Experimental group and control group are set B,
The control group is:Caustic soda 1-10kg/T, waterglass 15-30kg/T, hydrogen peroxide 10- are added in the slurry 20kg/T, deinking agent 0.5-3kg/T;(note:All dosages are oven dry stock, it is following similarly).
The experimental group is divided into 3 groups, wherein,
Experimental group 1 is:Fiber oxidation enzyme (PMO) 150-300g/T (oven dry stock), deinking agent 0.5kg/ are added in the slurry T, add caustic soda 2kg/T, waterglass 15kg/T, hydrogen peroxide 10kg/T;
Experimental group 2 is:Glucose oxidase 250-500g/T, deinking agent 1kg/T are added in the slurry, add caustic soda 2kg/T, Waterglass 15kg/T, hydrogen peroxide 10kg/T;
Experimental group 3 is:Addition fiber oxidation enzyme and glucose oxidase combined treatment in the slurry, PMO 150-300g/T, GOX 250-500g/T, deinking agent 0.5kg/T, add caustic soda 1-2kg/T, waterglass 15kg/T, hydrogen peroxide 10kg/T;
Above-mentioned reaction condition is:Temperature is 60 DEG C, and the reaction time is 90 minutes, and reaction pH is 8-10, and constant speed stirs.
C, deinking is tested:3 liters of Denver's formula flotation device will be added to spreading mass by taking, add plain boiled water (50 DEG C, 400 PPM Hardness) diluted slurry to 1% or so, is stirred 3 minutes, it is uniform to being formed then to open compressed air valve and regulation flow Tiny bubble and stable froth bed, foam is scraped, and flotation time is 4 minutes, obtains Deinking Pulp.
D, handmade paper preparation and ionization meter:By the above-mentioned Deinking Pulp prepared, running water is added to be diluted to 1.0% slurry It is dense, mix, measurement temperature and slurry concentration, by TAPPI methods, the accurate handmade paper for preparing 10-12 6.5 grammes per square metres.After drying, hand Copy paper is placed in the control cabinet of constant temperature and constant humidity degree 24 hours, then measures its whiteness by TAPPI measuring methods.
3rd, experimental result
As a result referring to table 1, as can be seen from Table 1:Conventional deinking raw material, PMO and GOX are useless using processing alone or in combination Influence of the paper paper pulp to deinking efficiency.80% is reduced in amount of caustic soda, waterglass reduces the bar of 50% and hydrogen peroxide reduction 50% Under part, after fiber oxidation enzyme and combinations thereof processing, the whiteness of paper just dramatically increases before flotation, compares than condition Whiteness improves 2-4%ISO;After flotation, whiteness increase is more notable, compares and improves 3-4%ISO than condition.Individually GOX processing is added, the whiteness increase of paper compares slightly to improve than condition, but not notable.When fiber oxidation enzyme and glucose aoxidize Enzyme-linked conjunction is in use, most pronounced effects, the whiteness of its paper reach more than 54%ISO.
Influence of the processing reclaimed waste paper slurry to paper physical index is used in combination in the fiber oxidation enzyme of table 1 and glucose oxidase
Embodiment described above only expresses the several embodiments of the present invention, and its description is more specific and detailed, but simultaneously Therefore the limitation to the scope of the claims of the present invention can not be interpreted as.It should be pointed out that for one of ordinary skill in the art For, without departing from the inventive concept of the premise, various modifications and improvements can be made, these belong to the guarantor of the present invention Protect scope.Therefore, the protection domain of patent of the present invention should be determined by the appended claims.

Claims (7)

1. a kind of fiber oxidation enzymatic compositions for being used to improve Paper White Degree, it is characterised in that including consisting of:
I) there is the biology enzyme component of oxidative function to fiber, the biology enzyme component is to change fibre by redox reaction The fiber oxidation enzyme of dimension table surface properties;With
Ii) there is the helper component of increase catalytic activity to fiber oxidation enzyme, the helper component is the reaction of fiber oxidation enzyme Substrate;
The weight ratio of the biology enzyme component and helper component is 1:1-100;
The fiber oxidation enzymatic compositions also include the protein to fiber oxidation enzyme with facilitation, described to fiber oxidation It is the biology enzyme for having catalytic activity that enzyme, which has the protein of facilitation, and the biology enzyme for having catalytic activity is redox Enzyme, selected from cellobiose dehydrogenase, laccase, glucose oxidase, Catalase, alcohol dehydrogenase or lignin peroxidating One or more in enzyme;Fiber oxidation enzyme and there is facilitation to fiber oxidation enzyme in the fiber oxidation enzymatic compositions The weight ratio of protein is 1:(0.5-3);
The fiber oxidation enzyme is family's molecular weight in 20-50KDa, the glycan oxygenation of the small molecule metalloenzyme with copper dependence Enzyme.
2. the fiber oxidation enzymatic compositions according to claim 1 for being used to improve Paper White Degree, it is characterised in that the fibre The reaction substrate for tieing up oxidizing ferment is oxygen, air or oxygen discharge compound;The oxygen release compound is peroxide Or ozone.
3. the fiber oxidation enzymatic compositions according to claim 2 for being used to improve Paper White Degree, it is characterised in that the mistake Oxide is at least one of hydrogen peroxide, sodium peroxide, calper calcium peroxide or potassium peroxide.
4. the fiber oxidation enzymatic compositions according to claim 1 for being used to improve Paper White Degree, it is characterised in that the life Thing enzyme component and the weight of helper component ratio are 1:30-70.
5. fiber oxidation enzyme or the fiber oxidation enzymatic compositions as described in claim any one of 1-4 are used as in paper technology and changed The application of the bleaching agent of kind Paper White Degree, deinking agent or brightening agent;The fiber oxidation enzyme be family's molecular weight 20-50KDa, The glycan oxygenase of small molecule metalloenzyme with copper dependence.
6. a kind of papermaking process, it is characterised in that mainly include the following steps that:
A) aqueous cellulosic papermaking slurry material is formed,
B) the fiber oxidation enzymatic compositions for being used to improve Paper White Degree described in claim any one of 1-4 are added to pulping Reacted in material,
C) paper making pulp obtained in step b) is served into net, page is formed by fibre solid component from there through water is filtered out,
D) page is passed through into squeeze section and dryer section, final production goes out paper product.
7. papermaking process according to claim 6, it is characterised in that described in step b) in fiber oxidation enzymatic compositions Fiber oxidation enzyme dosage is 0.01-10 kilograms of dry finish per ton, and the dosage of helper component is 0.05-10 kilograms of dry finish per ton; And/or
The time of the fiber oxidation enzymatic compositions and paper making pulp reaction is 5-600 minutes, pH 3-10, temperature 20-80 ℃。
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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
ES2623288T3 (en) * 2010-08-20 2017-07-10 Codexis, Inc. Use of glycolide hydrolase 61 family 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

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