CN1575363A - Oxidizing enzymes in the manufacture of paper materials - Google Patents

Oxidizing enzymes in the manufacture of paper materials Download PDF

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Publication number
CN1575363A
CN1575363A CNA028211480A CN02821148A CN1575363A CN 1575363 A CN1575363 A CN 1575363A CN A028211480 A CNA028211480 A CN A028211480A CN 02821148 A CN02821148 A CN 02821148A CN 1575363 A CN1575363 A CN 1575363A
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CN
China
Prior art keywords
enzyme
paper
fatty acid
pulp
purposes
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Granted
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CNA028211480A
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Chinese (zh)
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CN100336970C (en
Inventor
金·博尔奇
尼尔·弗兰克斯
亨里克·伦德
徐辉
罗菁
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Novo Nordisk AS
Novozymes North America Inc
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Novo Nordisk AS
Novozymes North America Inc
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Publication of CN1575363A publication Critical patent/CN1575363A/en
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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0069—Oxidoreductases (1.) acting on single donors with incorporation of molecular oxygen, i.e. oxygenases (1.13)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y113/00—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13)
    • C12Y113/11—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13) with incorporation of two atoms of oxygen (1.13.11)
    • C12Y113/11012—Linoleate 13S-lipoxygenase (1.13.11.12)
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00—Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/005—Treatment of cellulose-containing material with microorganisms or enzymes
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00—Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/02—Working-up waste paper
    • D21C5/025—De-inking
    • D21C5/027—Chemicals therefor
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C9/00—After-treatment of cellulose pulp, e.g. of wood pulp, or cotton linters ; Treatment of dilute or dewatered pulp or process improvement taking place after obtaining the raw cellulosic material and not provided for elsewhere
    • D21C9/08—Removal of fats, resins, pitch or waxes; Chemical or physical purification, i.e. refining, of crude cellulose by removing non-cellulosic contaminants, optionally combined with bleaching
    • 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
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21H—PULP 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
    • D21H21/00—Non-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
    • D21H21/02—Agents for preventing deposition on the paper mill equipment, e.g. pitch or slime control
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02W—CLIMATE CHANGE MITIGATION TECHNOLOGIES RELATED TO WASTEWATER TREATMENT OR WASTE MANAGEMENT
    • Y02W30/00—Technologies for solid waste management
    • Y02W30/50—Reuse, recycling or recovery technologies
    • Y02W30/64—Paper recycling

Abstract

The use of fatty acid oxidizing enzymes in the manufacture of paper materials, such as paper, linerboard, corrugated paperboard, tissue, towels, corrugated containers and boxes. Examples of fatty acid oxidizing enzymes are oxygenases classified as EC 1.13.11. including any of the sub-classes thereof, such as lipoxygenase, EC 1.13.11.12. The effect of these enzymes is that the deposition of pitch is reduced, and bleaching and de-inking effects are also observed on the paper pulp and the resulting paper material. The fatty acid oxidizing enzyme can be used in combination with a substrate, with proteases, lipases, xylanases, cutinases, oxidoreductases, cellulases, endoglucanases amylases, mannanases, steryl esterases, and/or cholesterol esterases; or with surfactants and other adjuvants.

Description

Oxidizing ferment during paper material is made
Invention field
The present invention relates to the purposes of fatty acid oxidase in paper material is made and the method for making paper material, this method comprises the step of handling papermaking slurry (papermaking pulp) and/or paper water (process water) with fatty acid oxidase.
Background of invention
It is well-known using enzyme in the paper material manufacturing, the example of employed enzyme has protease, lipase, zytase, amylase, cellulase for this purpose, and such as the various oxidizing ferment of oxidoreducing enzyme (phenol oxidase), for example laccase and peroxidase.
The effect of these enzymes is general, for example can be used for control such as pitch (pitch) deposition, improvement intensity, deinking, improvement draining, softening tissue paper and bleaching etc.
In paper process, in the process of producing paper pulp and paper, the material (DCS) with colloidal state that dissolves is dispersed in the industrial water.DCS often is meant wood pitch or wood gum.Asphalt adhesive makes paper machine have problems on roller, and generates spot or hole in paper material.
Timber is except comprising main component: cellulose, hemicellulose and the lignin, also comprise pitch or the various extract (extractive) of about 1-10%.The main component of pitch is aliphatic acid, triglycerides, sterol, steroid ester (steryl esters) and so-called resin acid, for example rosin acid.
WO 00/53843 discloses the application that steroid ester moiety in the pitch is fallen in some steroid esterase preparations and their hydrolysis in papermaking.
United States Patent (USP) 6,066,486 disclose the enzyme preparation that comprises the cholesterase that is derived from Pseudomonas fragi (Pseudomonas fragi) and the purposes of hydrolysis pulp resin thereof.
JP 2000080581 discloses some peroxidase decomposes rosin acid in slurrying or papermaking process purposes.
X.Zhang is at Pulp ﹠amp; Paper Canada, 101:3 (2000) discloses in the 59-62 page or leaf for example laccase has been removed Research on ability dissolving and material colloidal state.
And people such as Karlsson are at Reactivity of Trametes Laccases With Fatty andResin Acids; Appl.Microbiol.Biotechnol., the experiment of use laccase treatment pitch sample (model pitch) preparation is disclosed among (2001) 55:317-320.
Yet above-mentioned document neither one discloses fatty acid oxidase defined herein purposes in paper material is made.
Summary of the invention
Inventor of the present invention finds some oxidizing ferment unexpectedly, and promptly fatty acid oxidase helps being used in the paper material manufacturing.An important result of these enzymes is to reduce the deposition of pitch; And these enzymes have the effect that slurry and the paper material that is generated are bleached; At last, also observe these enzymes and have deinking efficiency.
Detailed Description Of The Invention
Paper and paper oar
Term " paper process (paper-making processs) " is meant a kind of method, wherein with pulp suspension in water, mix with various additives, deliver to then in the equipment, in these equipment, form paper, cardboard, tissue paper and towel paper etc., then extruding and dry.
Term " paper material (paper material) " is meant the product that can prepare, for example paper, liner board (linerboard), corrugated board, tissue paper, towel paper, corrugated case or box from paper pulp.
Term " papermaking slurry (paper-making pulp) " or " paper pulp (pulp) " are meant can be as any paper pulp of production paper material.For example, paper pulp can be supplied in magma or come from reproducible source.The papermaking slurry can be a wood pulp, non-wood pulp or the slurry of being made by waste paper.Wood pulp can be by making such as the needlebush of pine tree (pine), redwood (redwood), fir (fir), dragon spruce (spruce), cdear (cedar) and Chinese hemlock spruce (hemlock), or by making such as the leaf wood of maple (maple), alder (alder), birch (birch), walnut tree (hickory), beech (beech), white poplar (aspen), wattle (acacia) and eucalyptus (eucalyptus).Non-wood pulp can by, for example make from bagasse, bamboo, cotton or mestha.Secondary stock can be made by the waste paper of making oar again, for example office's waste paper of newspaper, mixing, computer printout paper, white account book, magazine, milk pack box and dixie cup etc.
In a specific embodiments, institute's papermaking slurry to be processed comprises hardwood pulp and softwood pulp.
Wood pulp to be processed can be the CTMP (BCTMP) of mechanical pulp (for example ground wood pulp (GP)), chemical pulp (for example Kraft slurry or sulfite pulp), semi-chemical pulp (SCP), hot method mechanical pulp (TMP), CTMP (CTMP) or bleaching.
Mechanical pulp is to make by the method for grinding and make with extra care, and wherein raw material is handled with periodic pressure pulse.TMP is hot method mechanical pulp, and GW is a ground wood pulp, and PGW is the pressure ground wood pulp, and RMP is a RMP, and PRMP is the pressure RMP, and CTMP is a CTMP.
Chemical pulp is by alkaline boiling, removes most of lignin and hemicellulose and makes.In Kraft system oar or sulphate cook, with vulcanized sodium or the main boiling chemical substance of NaOH conduct.In these paper pulp types, as the result of alkaline boiling, the triglycerides of pitch part will be hydrolyzed into aliphatic acid and glycerine.Fatty acid oxidase is specially adapted to handle these paper pulp, and this is because of as described in its title, these enzymes are generated further catalytic decomposition by the triglycerides alkaline hydrolysis aliphatic acid.
Kraft to be processed slurry can be the Kraft slurry of bleaching, it can comprise the Kraft (SWBK of needlebush bleaching, be also referred to as NBKP (Nadel Holz Bleached Kraft Pulp)), Kraft (HWBK is also referred to as LBKP (Laub Holz Bleached Kraft Pulp)) or its mixture of leaf wood bleaching.
The paper pulp that uses in the inventive method is the suspension of machinery or chemical pulp or its combination.For example, the paper pulp that uses in the inventive method can comprise 0%, 10-20%, 20-30%, 30-40%, 40-50%, 50-60%, 60-70%, 70-80%, the chemical pulp of 80-90% or 90-100%.In a specific embodiment, the chemical pulp component part is used to make the used paper pulp of paper material.In the context herein, " component part " is meant in the paper pulp that the inventive method will be used, and the shared percentage of chemical pulp is in the scope of 1-99%.In specific embodiments, the shared percentage of chemical pulp is at 2-98%, 3-97%, and 4-96%, 5-95%, 6-94%, 7-93%, 8-92%, 9-91%, 10-90%, 15-85%, 20-80%, 25-75%, 30-70% is in 40-60% or the 45-55% scope.
In the specific embodiments of purposes of the present invention and method, chemical pulp is the CTMP (BTMP) of Kraft slurry, sulfite pulp, semi-chemical pulp (SCP), hot method mechanical pulp (TMP), CTMP (CTMP), bleaching.In specific embodiment, the Kraft slurry is the Kraft slurry of bleaching, Kraft (the SWBK of needlebush bleaching for example, be also referred to as NBKP (Nadel Holz Bleached Kraft paper pulp)), Kraft (HWBK is also referred to as LBKP (Laub Holz Bleached KraftPulp)) or its mixture of leaf wood bleaching.
Process conditions
The inventive method is specially adapted to the compound that in system oar or paper process technology oxidation and hydrolysis constitute pitch, and doing like this is in order for example to avoid the pitch problem.
The inventive method may be used on any bitumeniferous paper pulp, may be used on containing the paper pulp of a large amount of linoleic acid or other unsaturated free fatty especially.
Under the situation of converted paper and paper pulp, can move method of the present invention in any stage of pulp production.Enzyme can add to any retainer (holding tank), for example storage slurry device (storage tank (chest)), storage tower, mixing channel or measuring tank.Enzyme is handled can be before the association with pulp bleaching, carry out with pulp bleaching process or after bleaching.When carrying out with association with pulp bleaching, can use chemical substance together with bleaching, for example chlorine and chlorine dioxide add enzyme preparation together.But apply also bleached pulp of oxygen, hydrogen peroxide or ozone or its combination.Also can add enzyme preparation together with these materials.Preferably before bleaching, add enzyme preparation.Also enzyme can be added and come from the cyclic production water (plain boiled water) of bleaching and come from machinery or the industrial water of chemical-mechanical pulping process (brown water (brown water)).In the specific embodiments of Kraft pulping process, in thick liquid washing process, add enzyme.
In the context herein, " industrial water " comprises 1) as the water in the raw material adding paper process; 2) the middle aquatic products of in any step of making the paper material method, producing; 3) as the output of method or the waste water of byproduct.In specific embodiments, industrial water is, is, is now maybe will to be circulation (recirculation), promptly re-uses in another step of this method.Term " water " also refers to any aqueous medium, solution, suspension, the various additives of using always in for example common running water and running water and the paper process and the mixture of adjuvant.In a specific embodiments, industrial water contains solid-state (doing) material of low content, for example is lower than 20%, 18%, 16%, 14%, 12%, 10%, 8%, 7%, 6%, 5%, 4%, 3%, 2% or be lower than 1% dry.
Purposes of the present invention and method do not comprise the purposes of lipoxygenase of the Magnaporthe salvinii of the dyestuff that the embodiment of PCT/DK02/00251 is 2 described, be derived from the waste water that is used for bleached pulp industry.
Method of the present invention can be carried out under the normal condition of paper and paper pulp processing.Process conditions will be the functions of the enzyme, reaction time and the specified criteria that are applied.
Enzyme of the present invention should add with effective amount.So-called " effectively amount " is meant that this amount is enough to obtain required and effect that expected, for example effects such as oxidized asphalt component, the required bleaching of acquisition and/or deinking.
In a specific embodiment, the dosage of fatty acid oxidase and other enzyme (if any) is that paper pulp per ton adds the 0.1mg zymoprotein to 100.000mg zymoprotein (various enzyme).
In another embodiment, the amount of fatty acid oxidase and other enzyme (if any) is in the 0.00001-20 scope, or every gram lignocellulosic material (dry weight) 0.0001-20mg enzyme (calculating) with pure enzyme protein, for example every gram lignocellulosic material 0.0001-10mg/g, 0.0001-1mg/g, 0.001-1mg/g, the enzyme of 0.001-0.1mg/g or 0.01-0.1mg/g.Explanation once more, this tittle is meant the amount of various enzymes.
Can under conventional concentration (consistency), carry out enzyme and handle, for example the 0.5-10% dry.In specific embodiments, concentration is at 0.5-45; 0.5-40; 0.5-35; 0.5-30; 0.5-25; 0.5-20; 0.5-15; 0.5-10; 0.5-8; 0.5-6 or in the 0.5-5% dry scope.
Enzyme is handled and can be carried out under about 10 ℃ to 100 ℃ temperature.The example of other temperature range (being " from approximately " and " to approximately ") is as follows: 20-100,30-100,35-100,37-100,40-100,50-100,60-100,70-100,10-90,10-80,10-70,10-60 and 30-60 ℃ and any combination of the upper and lower bound of explanation herein.Typical temperature is at about 20-90 ℃ or about 20-95 ℃, preferably about 40-70 ℃ or about 40-75 ℃.
Enzyme is handled and can be carried out under about 2 to about 12 pH value.The example of other pH scope (being " from approximately " and " to approximately ") is as follows: 3-12,4-12,5-12,6-12,7-12,8-12,9-12,2-11,2-10,2-9,2-8,4-10 and 5-8 and any combination of the upper and lower bound of explanation herein.Usually pH is in about 2-11 scope, preferably in the scope of about 4-9.5 or about 6-9.
The suitable duration that enzyme is handled can for the several seconds to a few hours, for example about 30 seconds to about 48 hours, or about 1 minute to about 24 hours, or about 1 minute to about 18 hours, or about 1 minute to about 12 hours, or about 1 minute to about 5 hours, or about 1 minute to about 2 hours, or about 1 minute to about 1 hour, or about 1 minute to about 30 minutes.Usually the reaction time is about 10 minutes to 3 hours, 10 minutes to 10 hours, is preferably 15 minutes to 1 hour or 15 minutes to 2 hours.
If required, airborne molecular oxygen will exist with enough amounts usually.Therefore, reaction can promptly be carried out under the normal pressure easily in open system.
Except that fatty acid oxidase and other enzyme (if any), various additives also can be used in purposes of the present invention or the method.Because surfactant and/or dispersant exist and/or are added in the papermaking slurry, so the inventive method and purposes can be in the papermaking slurries carried out in the presence of conventional anion, nonionic, CATION and/or amphion (zwitterionic) surfactant that uses and/or the dispersant.The example of anion surfactant is carboxylate, sulfate, sulfonate or the phosphate of alkyl, substituted alkyl or aryl.Aliphatic acid is alkyl carboxylate's example.The example of non-ionic surface active agent is a polyoxyethylene compound, for example ethyoxyl/the propoxylate of alcohol ethoxylate, propoxylate or mixing, polyglycereol and other polyalcohol and certain block copolymers.The example of cationic surfactant is the water-soluble cationic polymer of quaternary ammonium sulfate and some amine for example, the for example amine of chloropropylene oxide/dimethyl amine polymer (EPI-DMA) and interlinkage solution thereof, diallyl dimethyl ammoniumchloride (DADMAC), DADMAC/ acrylamide copolymer and for example United States Patent (USP) 5,681,862 and 5,575,993 disclosed ionene polymers.Amphion or examples of amphoteric surfactants are betaine, Glycinates, aminopropionate, iminopropinate and various imidazolidine derivatives.Also can use United States Patent (USP) 5,256, disclosed polymer in 252.
According to the present invention, surfactant, for example above-mentioned surfactant and any combination thereof also can be used with fatty acid oxidase defined herein, and are included in the composition with this kind of enzyme.In the composition amount of various surfactants can for composition about 8 to about 40% (w/w).In specific embodiments, the amount of various surfactants is about 10 to 38, or about 12 to 36, or about 14 to 34, or about 16 to 34, or about 18 to 34, or about 20 to 34, or about 22 to 34, or about 24 to 34, or about 26 to 34, or about 28 to 32% (w/w).
In another embodiment, each above-mentioned scope is meant the surfactant total amount.Enzyme
EC numbering (EC-number) can be used for enzyme classification, and for example lipase EC numbering is used to contain the enzyme of lipase active.Please refer to Recommendations (1992) of the Nomenclature Committeeof the International Union of Biochemistry and Molecular Biology, AcademicPressInc., 1992.
Be to be understood that term " enzyme " herein, and various enzyme and enzyme class comprise wild-type enzyme, and the variant of retentive activity (variant).These variants can pass through recombinant technique (recombinant technique) and generate.Wild enzyme also can separate by recombinant technique or from natural materials and purification obtains.
In a specific embodiments, described enzyme has clear and definite definition, and this is meant to have only a main enzyme component to exist.This can fractionation obtains on the post by getting rid of in suitable dimensions.Can obtain these well-defined or that purify or highly purified enzymes, as known in the art and/or the publication relevant with described concrete enzyme described.
Fatty acid oxidase
Term " a kind of " fatty acid oxidase is meant at least a such enzyme.Term " at least a " is meant a kind of, two kinds, three kinds, four kinds, five kinds, six kinds or even more kinds of such enzyme.
In the context herein, fatty acid oxidase is than hydrolyte syringaldazine (syringaldazine) the linoleic enzyme of hydrolysis more effectively." more effective " is meant to have higher reaction rate.Mensuration can be used embodiment 2 described methods, and calculate (1) matrix linoleic acid (absorbance is at 234nm) and go up poor between the recruitment of the recruitment of per minute absorbance (absorbancy) and the last per minute absorbance of (2) matrix syringaldazine (absorbance is at 530nm), promptly calculate reaction rate differences (ReactionRate difference, RRD)=(d (A 234)/dt-d (A 530)/dt).If RRD is greater than zero, then described enzyme is suitably for the fatty acid oxidase of definition herein.If RRD is zero or less than zero, then described enzyme is not a fatty acid oxidase.
In specific embodiments, RRD is at least 0.05,0.10,0.15,0.20 or at least 0.25 absorbance unit/minute.
In the specific embodiments of embodiment 2 methods, enzyme clearly defines.Further, in the method for embodiment 2, the dosage of regulatory enzyme is to obtain per minute maximum absorbance recruitment on 234nm or 530nm.In specific embodiments, the maximum absorbance recruitment is at 0.05-0.50; 0.07-0.4; 0.08-0.3; 0.09-0.2 or in 0.10-0.25 absorbance unit/minute scope.The dosage of enzyme for example can be at 0.01-20; 0.05-15 or in the scope of 0.10-10mg zymoprotein/milliliter.
In addition, " fatty acid oxidase " may be defined as can be than the syringaldazine enzyme of the efficient oxidation unrighted acid more.Can comprise syringaldazine or linoleic acid as matrix and pH be 6 and temperature be under 30 ℃ the situation, in the standard oximeter device described in the present embodiment 1, relatively obtain the activity of enzyme.
In specific embodiments, fatty acid oxidase is defined as the enzyme that is categorized as EC 1.11.1.3 or EC1.13.11.-, and wherein EC 1.13.11.-is meant enzyme any in its subclass, has 49 kinds at present: EC1.13.11.1-EC 1.13.1 1.49.EC 1.11.1.3 is the fatty acid peroxidase of appointment, and EC1.13.11.-is meant by incorporating the oxygenase that two oxygen atoms act on the appointment on the single donor into.
In another embodiment, EC 1.13.11.-enzyme is by for becoming EC 1.13.11.12, EC1.13.11.31, EC 1.13.11.33, EC 1.13.11.34, EC 1.13.11.40, EC 1.13.11.44 or EC 1.13.11.45 class are respectively the lipoxygenase of appointment, arachidonate 12-lipoxygenase (arachidonate 12-lipoxygenase), arachidonate 15-lipoxygenase, arachidonate 5-lipoxygenase, arachidonate 8-lipoxygenase, linoleate glycol synzyme (linoleate diol synthase) and linoleate 11-lipoxygenase.
In another embodiment, fatty acid oxidase is the aliphatic acid oxygenase (LOX) that is categorized as EC1.13.11.12, and this enzyme-catalyzed polymerization unrighted acid is particularly for example linoleic suitable, suitable-1, the oxidation of 4-diene and generate the enzyme of hydrogen peroxide.But other matrix also may be oxidized, for example monounsaturated fatty acids.
Microorganism lipoxygenase (Microbial lipoxygenase) can be derived from, saccharomyces cerevisiae (Saccharomyces cerevisiae) for example, thermoactinomyces vulgaris (Thermoactinomyces vulgaris), fusarium oxysporum (Fusarium oxysporum), fusarium moniliforme (Fusarium proliferatum), Thermomyces lanugmosus, Pyricularia oryzae and Geotrichum bacterial strain.The lipoxidase enzyme preparation that is derived from Gaeumannomyces graminis has been described among the embodiment 3-4 of WO02/20730; The expression formula of Aspergillus oryzae (Aspergillus oryzae) lining in the lipoxygenase that is derived from Magnaporthesalvinii has been described among the embodiment 2 of PCT/DK02/00251, and this endonuclease capable uses standard method, and the method described in the embodiment 4 of WO 02/20730 is purified.
Lipoxygenase (LOX) can for example be extracted in soybean, pea, chick-pea and the Kidney bean from vegetable seeds.In addition, lipoxygenase can for example obtain in the rabbit desmacyte from mammalian cell.
By detecting the formation of hydroperoxides, can under 25 ℃, determine activity of fatty oxygenase by public spectrophotometer.For standard analysis, 10 microlitre enzymes are added in the quartz cuvette of the 25mM sodium phosphate buffer agent (pH7.0) contain 980 microlitres and 10 microlitre matrix solutions (being dispersed in the 10mM linoleic acid (can not cross long-time preservation) among 0.2% (v/v) Tween20).Usually, fully dilute enzyme and guarantee that with beginning added matrix has maximum 10% upset (turn-over) when (first minute).Obtain absorbance, then from the linear segment estimation rate of obtaining curve at 234nm.Suitable-anti--conjugation hydroxyl (hydrogen peroxide) aliphatic acid is considered to have 23,000M -1Cm -1Molecular extinction coefficient.
Fatty acid oxidase also can add together with the matrix that can strengthen its enzyme effect concerning enzyme.Suitable matrix is the oil of hydrolysis, for example from the oil of soybean (being rich in linoleic acid) or tall oil.The aliphatic acid matrix that can from the oil that adds, discharge or in Kraft system oar or sulphate cook, produce by lipolytic enzyme.
In specific embodiments, matrix is to have 1, and 4-pentadiene structure is for example suitable, suitable-1, the compound of 4-pentadiene structure, and promptly its structural formula contains the compound of this at least structure.The example of this type of matrix is a unrighted acid, for example palmitoleic acid, oleic acid, linoleic acid, linolenic acid and arachidonic acid and salt thereof and ester, for example methyl esters and ethyl ester.
In other specific embodiments, matrix is linoleic acid, linoleic acid first or ethyl ester, linolenic acid or linolenic acid first or ethyl ester.
For research adds the effect of matrix to described fatty acid oxidase, can use following method: the spectrum of record (being emulsified among the 0.2%Tween20) 10mM rosin acid, observing characteristic peak near the 200nm and near the 250nm.In first experiment, fatty acid oxidase is added in the rosin acid emulsion; In second experiment, also add fatty acid oxidase matrix.Enzyme for example is the above-mentioned lipoxygenase that is derived from M.salvinii; Matrix for example is linoleic acid.With the decomposition of spectrophotometry Technical Follow-Up rosin acid, when adding linoleic acid and lipoxygenase together, find very fast reduction near near the peak the 200nm and the 250nm.
In the specific embodiments of said method of the present invention and process, matrix, for example linoleic addition are 5-10000ppm (mg/l) or 10-9000,10-8000,25-7500,30-7000,50-6000,50-5000,50-4000,75-3000,75-2500,80-2000,90-1500,100-1000,150-800 or 200-700ppm.In embodiment 4, add the linoleic acid of 333ppm with fatty acid oxidase.
In other specific embodiments of said method of the present invention and process, the addition of fatty acid oxidase is 0.005-50ppm (mg/l) or 0.01-40,0.02-30,0.03-25,0.04-20,0.05-15,0.05-10,0.05-5,0.05-1,0.05-0.8,0.05-0.6 or 0.1-0.5ppm.The amount of enzyme refers to the clearly mg of the enzyme preparation of definition.
In the methods of the invention, can apply separately or apply fatty acid oxidase together in conjunction with other enzyme.Term " other enzyme " is meant at least a other enzyme, for example a kind of, two kinds, three kinds, four kinds, five kinds, six kinds, seven kinds, eight kinds, nine kinds, ten kinds or even more kinds of other enzyme.
Term " apply together (together use) " is meant and can applies other enzyme in the same step of the inventive method or other step.Other method step can be the step in paper process middle and upper reaches or downstream, for the step of handling papermaking slurry or industrial water with fatty acid oxidase.
In specific embodiments, other enzyme is the enzyme with protease, lipase, zytase, keratoprotein enzyme (cutinase), oxidoreducing enzyme, cellulase, endoglucanase (endoglucanase), amylase, mannase (mannanase), steroid esterase (steryl esterase) and/or cholesterol ester enzymatic activity.The example of oxidoreducing enzyme is the enzyme with laccase and/or peroxidase activity.In preferred embodiments, other enzyme is a lipase.
" step " is meant at least one step in the method, and it may be one, two, three, four, five or multi-method step more.In other words, can apply fatty acid oxidase of the present invention at least one step, for the step that adds fatty acid oxidase, this step can be identical or different step.
Term " enzyme preparation " is meant the product that comprises at least a fatty acid oxidase.Enzyme preparation also can comprise the enzyme that contains other enzyme additive, is preferably lipolytic enzyme or contains the enzyme of oxidoreductase activity, most preferably is lipolytic enzyme.Except enzymatic activity, this type of preparation preferably comprises at least a adjuvant.The example that is used in adjuvant in the enzyme preparation of paper and pulp industry is buffer, polymer, surfactant and stabilizing agent.
Other enzyme
Any enzyme with protease, lipase, zytase, keratoprotein enzyme, oxidoreducing enzyme, cellulase, endoglucanase, amylase, mannase, steroid esterase and/or cholesterol ester enzymatic activity can be used as other enzyme of purposes of the present invention and method.These other enzymes in more following non-limiting examples, have been listed.The enzyme of representing with capitalization English letter is can be from the DK-2880Bagsvaerd of Denmark, the enzyme that the Novozymes A/S of Krogshoejvej 36 buys.Any activity in those other enzymes can be used methods analyst as known in the art, comprises the method in the above-mentioned document of quoting.
The example of keratoprotein enzyme is that those are derived from Humicola insolens (US 5,827,719), are derived from the bacterial strain of Fusarium (Fusarium), F.roseumculmorum for example, or particularly the F.solanipisi bacterial strain (WO 90/09446; WO 94/14964, and WO 94/03578) enzyme.The keratoprotein enzyme also can be derived from Rhizoctonia (Rhizoctonia), the bacterial strain of Solanum rhizoctonia (R.solani) for example, or Alternaria (Alternaria), the bacterial strain of wild cabbage chain lattice spore (A.brassicicola) (WO 94/03578) for example, or its variant, the variant described in WO 00/34450 or WO 01/92502.
The example of protease is ALCALASE, ESPERASE, SAVINASE, NEUTRASE and DURAZYM protease.Other protease is derived from nocardia and belongs to (Nocardiopsis), aspergillus (Aspergillus), Rhizopus (Rhizopus), Alkaliphilic bacillus (Bacillusalcalophilus), Bacillus cercus (B.cereus), bafillus natto (B.natto), B.vulgatus, bacillus mycoides (B.mycoide) and from the subtilopeptidase A (subtilisins) of bacillus (Bacillus), particularly belong to subspecies (Nocardiopsis sp.) and Da Songweier nocardia and belong to those of (Nocardiopsisdassonvillei) and mutant thereof, as those mutant of WO 91/00345 and EP 415296 as disclosed kind of (species) nocardia that is derived among the WO 88/03947.
Diastatic example is BAN, AQUAZYM, TERMAMYL and AQUAZYM Ultra amylase.The example of lipase is a RESINASE A2X lipase.The example of zytase is a PULPZYME HC hemicellulase.The example of endoglucanase is NOVOZYM 613,342 and 476 enzyme products.
The example of mannase is that people such as Stahlband is in J.Biotechnol.29 (1993), among the 229-242 in the disclosed Trichoderma reesei-'beta '-mannase.
The example of steroid esterase, peroxidase, laccase and cholesterase is those disclosed in the described list of references of background parts of the present invention.Other example of oxidoreducing enzyme is at EP 730641, WO 01/98469, EP 719337, EP 765394, EP 767836, EP 763115 and EP 788547 disclosed peroxidase and laccases.Herein in the context, the enzyme of whenever mentioning oxidoreducing enzyme is meant the existence that requires or benefit from acceptor (for example oxygen or hydrogen peroxide), enhancer (enhancer), medium (mediator) and/or activator (activator), should consider to comprise this compounds.The example of enhancer and medium is disclosed in EP705327, WO 98/56899, EP 677102, EP 781328 and EP 707637.In case of necessity, the acceptor by the enzyme of oxidoreducing enzyme system (for example enzyme of laccase or peroxidase system) being defined as enzyme and enzyme, optional enhancer and/or the combination of medium are distinguished with this.
The present invention has some specific embodiments, and wherein the purposes of fatty acid oxidase is to reduce the deposition of paper process medium pitch.Be used to reduce the method for paper process medium pitch deposition, wherein this method comprises with the processing with enzyme preparation paper pulp and/or the industrial water that comprise fatty acid oxidase; Preferable methods, wherein paper pulp is mechanical pulp or chemical pulp or its combination, for example chemical pulp.Aforesaid method, wherein enzyme is the EC1.13.11 class, preferably in the 1.13.11.12 class, preferred wherein enzyme is derived from the bacterial strain that Magnaporthaceae belongs to, and is preferably M.salvinii, or the Gaeumannomyces genus, is preferably G.graminis.Aforesaid method, wherein said processing are the matrix that is used for enzyme by adding, are preferably linoleic acid and carry out.Aforesaid method, wherein enzyme preparation comprises lipolytic enzyme and/or another kind of oxidoreducing enzyme.Aforesaid method, wherein handling is at 20-90 ℃, be preferably under the temperature in the 40-70 ℃ of scope and/or 2-11, be preferably and carry out under the pH in the 4-9.5 scope, and/or wherein handle be 10 minutes in 3 hours, is preferably and carries out in 15 minutes to 1 hour, and/or wherein enzyme is at 0.0001-20mg/g, be preferably 0.0001-10mg/g, more preferably the 0.001-1mg/g concentration interior with most preferably being the 0.01-0.1mg/g scope adds.In the embodiment of said method, enzyme preparation is added in the material-storing box or blending bin of paper machine front.
In the scope of described herein and the disclosed specific embodiments in the not limited thereto place of invention that require, its reason is that these embodiments are intended to describe concrete aspects more of the present invention.Embodiment of equal value also will comprise within the scope of the invention.From the above description as can be known, to one skilled in the art, various modifications of the present invention and shown here and described be conspicuous really, these modifications are also included within the scope of additional claim.Under the situation of conflict, comprise that the disclosure in being defined in will play definite effect.
Quote various documents at this, integral body is quoted it openly as a reference.
Embodiment
Embodiment 1
Measure the activity of fatty acid oxidase on the linoleic acid
Use contain TriOxmatic 300 oxygen electrodes and 4 milliliters of standard reaction volumes " Oxi 3000Oximeter " (WTW, Weilheim, Germany).
10mg linoleic acid (10ml60% linoleic acid) is dissolved in the 1ml ethanol, adds 2 microlitre Tween20 then.From this raw material matrix solution, use little stirring rod that 50 microlitres are added and contain 3.85ml cushioning liquid (Britton-Robinson:100mM phosphoric acid, acetate and boric acid; Regulate pH with NaOH) reaction beaker in, stir solution fully mixed, oxygen electrode is inserted in the reaction beaker.Add the enzyme solutions that 100 microlitres are purified, i.e. the lipoxygenase that is derived from Magnaporthe salvinii of the about 0.4mg/ml of (a) concentration; (b) lipoxygenase that is derived from Gaeumannomyces (it is about 0.02mg/ml in end reaction) of the about 0.76mg/ml of concentration.The preparation method of these lipoxygenase is as implied above.Reaction temperature is 25 ℃.Measure dissolved oxygen concentration, and with the time (minute) be function plotting.Enzymatic activity (mg/l/min) is calculated as the slope of the linear segment of the curve behind the adding enzyme.When relevant, by subtracting each other with check baseline, this is meant that oxygen concentration and time are that the curve of function has greater than about 0.05O if preceding at adding fatty acid oxidase (that is, object of reference) 2The slope of/ml/min then deducts this slope from the specimen slope value.
Experimental result is as shown in table 1 below.
Table 1
Fatty acid oxidase
pH (a) be derived from the LOX mgO of M.salvinii 2/ml/min (b) be derived from the LOX mgO of G.graminis 2/ml/min
2 0.0 0.0
4 0.4 0.1
5 0.7 0.4
6 1.1 0.4
7 1.0 0.4
8 0.7 0.5
9 0.8 0.4
10 0.7 0.4
11 0.6 0.2
Embodiment 2
Fatty acid oxidase
As follows, test four kinds of enzymes, i.e. two kinds of laccases and two kinds of lipoxygenase.The laccase that is derived from Polyporus pinsitus has the 65kDa MW of SDS-Page, the 3.5pl of IEF, and under pH5.5 60 ℃ optimum temperature.The laccase that is derived from Coprinus cinereus has the 67-68kDa MW of SDS-Page, the 3.5-3.8pl of IEF, and under pH7.5 65 ℃ optimum temperature.Of WO96/00290 and United States Patent (USP) 6,008,029, preparation and enzyme purification.Two kinds of lipoxygenase are derived from Magnaporthe salvinii and Gaeumannomyces graminis, and its preparation method as mentioned above.
The dosage of regulatory enzyme is to guarantee obtaining per minute maximum absorbance recruitment on 234nm/530nm, promptly in 0.1-0.25 absorbance unit/minute scope.
Matrix solution: with 11.65mg linoleic acid (60%Sigma), and the 12.5ml0.56mM syringaldazine (Sigma) in ethanol mixes with deionized water, and cumulative volume is added to 25ml.
With the 50 microlitre enzyme preparations that will test transfer to contain 900 microlitre sodium phosphate buffer agents (50mM, pH7.0) and the quartz cuvette of 50 microlitre matrix solutions.Cuvette is put into constant temperature at 23 ℃ spectrophotometer, is the absorbance of function measurement 234nm and 530nm with time.The decomposition of the absorbance indication syringaldazine at 530nm place, and the absorbance at 234nm place is indicated linoleic decomposition.At 2 to 4 minute reaction time, i.e. d (A 234)/dt and d (A 530Calculate absorbance recruitment on the basis of)/dt with the function of time.
The result is as shown in table 2 below.In these four kinds of enzymes, have only two kinds of lipoxygenase to be suitably for defined fatty acid oxidase herein, this is because have only the RRD=reaction rate differences=(dA of these two kinds of enzymes 234/ dt-dA 530/ dt) greater than zero.
Table 2
Enzyme dA 530/ dt (unit/minute) dA 234/ dt (unit/minute) dA 234/dt-dA 530/ dt (unit/minute)
Polyporus pinsitu laccase 0.20 0.002 * -0.20
Magnaporthe salvini lipoxidase 0.0001 * 0.13 0.13
Coprinus cinereus laccase 0.17 -0.001 * -0.17
Gaeumannomyces graminis lipoxygenase -0.03 * 0.21 0.21
*This and odd jobs are equal to (profiling error)
Embodiment 3
Reduce pitch with fatty acid oxidase
The pitch specimen preparation is as follows:
50% linoleic acid 60% (Sigma L-1626),
20% rosin acid (Sigma A9424),
20% oleic acid (Merck 471),
5% cholesterine linoleate (Sigma C-0289),
5% olive oil (Sigma O-1500),
Stirred 30 minutes down at 65 ℃, in refrigerator, preserve and be no more than 30 days.
Prepare 0.1% pitch suspension:
50mg pitch sample,
1ml ethanol,
1ml0.1MNaOH，
48ml buffer (50mM borate pH9.0),
At room temperature stirred 10 minutes.
With circular paper (diameter=5.5-6mm; Multicopy80g/m 2) transfer in the hole of microtiter plate (from the ID 269620 of NUNC) in two 96 holes being appointed as A and B.Also use other two similar microtiter plate C and D, but do not have the scraps of paper.0.1% pitch suspension of 100 microlitres is added in each hole of these four microtiter plates.The above-mentioned lipoxygenase that is derived from Magnaporthe salvinii is as fatty acid oxidase, and it is added in the hole of microtiter plate A and C to obtain the hole concentration (in-well-concentration) of 10ppm.The buffer (50mM borate pH9.0) of similar quantity is added in the hole of microtiter plate B and D.In vibration (600rpm) process, cultivated microtiter plate 30 minutes then.After 30 minutes, the pitch suspension of 20 microlitre enzymes processing is transferred to another set of microtiter plate (Coming Inc.Costar UV plate 96 holes of corresponding microtiter plate A-D, No.3635), wherein contain 200 microlitre ethanol (solubilising asphalt component) in every hole of each plate.Rosin acid, the key component of pitch absorbs consumingly at about 255nm place.Therefore, A 255Indication remains the amount of pitch in suspension.A 255Be confirmed as the mean value of eight identical experiment, according to and cultivate without paper after, measured A in the pitch suspension 255Difference become (variation) (through 11 dilution backs in ethanol), estimate to be adsorbed onto the pitch amount on the paper.
The result is as shown in table 3 below.Lacking under the situation of fatty acid oxidase, basic (blind) of pitch on paper absorbs the ratio that may be calculated D/B.As for the absorption of paper to pitch, the effect of enzyme (sample) can be calculated as the ratio of C/A.If (C/A-D/B) less than zero, then it is a kind of method that shows that enzyme has made the pitch deposition reduce.In addition.Described enzyme effect can be calculated as ((C-A)-(D-B)), if should be worth less than zero, then this will be that the another kind of enzyme that shows has reduced the method for pitch deposition effect.Except paper, other solid-state material also can be used for test, for example metal and textiles (Style400 cotton).By comparing the deposition on other solid-state material, show that the method for above-mentioned demonstration minimizing pitch deposition can be practical.
Certainly, consider that the feature of described fatty acid oxidase selects test-pH (being buffer) and test-temperature, for example in about 4,5,6,7,8,9,10 or 11 test pH and 10,15,20,25,30,37,40,50,60,70,80,90 or 95 ℃ test temperature.
Table 3
A 255 Use the M.salvinii lipoxygenase Do not use the M.salvinii lipoxygenase
Contain paper A B
Do not contain paper C D
Embodiment 4
Bleaching contains the paper of fatty acid oxidase
Use is from the unbleached Kraft slurry of Eucalyptus grandis.In the pulper of making by Loretzen and Wettre, starch with the recasting of 4% concentration.Under pH=9.0, in buffer (Britton-Robinson), finish the recasting slurry.
Britton Robinson buffer:
100mM phosphoric acid (85%) 6.28ml
100mM acetate (100%) 5.72ml
100mM boric acid 6.18g
Dem. water is up to 1000ml
By adding NaOH pH is transferred to 9.0.
Behind the recasting slurry, by adding buffer slurry is diluted to 1% concentration, with pH regulator to 9.0.
Containing the 3g dry pulp, promptly in the beaker of 300ml pulp, handling with fatty acid oxidase.In 25 ℃ of water-baths, handle with 500rpm with magnetic stirring bar.The 333ppm linoleic acid is added in all beakers.Used fatty acid oxidase is the lipoxygenase that is derived from Gaeumannomyces graminis of above-mentioned prepared purification.The amount of the enzyme that uses is shown in table 4 and 5.Carry out enzyme and handled 2 hours, moving beaker under the condition separately.
After two hours, stop enzyme reaction by the NaOH (27.65% solution) that adds 5ml (fixed amount), this makes pH rise to greater than 12, makes enzyme deactivation.
Use the 700ml deionized water that object in the beaker is transferred in the 1000ml beaker quantitatively.This pulp suspension is poured in the Buchner funnel (15cm diameter) that contains filter paper.Take out anhydrate after, just formed the scraps of paper (paper sheet).From funnel, remove the scraps of paper, separate with filter paper then.In the nipper of making by Lorentzenand Wettre (sheet press), the compacting scraps of paper.In the sandwich structure of metallic plate, 2 blotting papers, 2 filter papers, these scraps of paper, 2 filter papers, 2 blotting papers, metallic plate, suppressed these scraps of paper 5.5 minutes with 0.4MPa pressure.Replace l Water Paper with dried paper, suppressed again 2 minutes with 0.4Mpa then.These scraps of paper of drying overnight in air then.
The brightness of using Macbeth Color-Eye7000 reflectometer to measure the scraps of paper, in this brightness of record of 600nm place, and to every scraps of paper measurement four times, measurement result is as shown in table 4 below.
Use the method described in the Tappi Test Methods T236 (Tappi Press) to measure the Kappa number (Kappa Number) of every scraps of paper, Kappa number is described the delignified degree of paper pulp.The employed amount of each measurement is 1/4 described in the standard method.The content of dry decides by calculating Kappa number in the scraps of paper.The result as shown in table 5 below.
Table 4
LOX[mg/l] The brightness that the scraps of paper 1 reflect at 600nm, the mean value of four mensuration The brightness that the scraps of paper 2 reflect at 600nm, the mean value of four mensuration Average brightness in the 600nm reflection
0 46.93 46.60 46.77
0.1 49.69 50.23 49.96
1.3 48.51 47.15 47.83
3.2 49.16 50.12 49.64
6.3 48.56 52.56 50.56
Table 5
LOX[mg/l] The Kappa number of the scraps of paper 1, the mean value of three mensuration The Kappa number of the scraps of paper 2, the mean value of three mensuration Kappa number mean value
0 18.44 18.43 18.44
0.1 14.80 14.68 14.74
1.3 14.94 14.93 14.94
3.2 14.65 14.42 14.54
6.3 14.83 14.40 14.61
Embodiment 5
With fatty acid oxidase to stale news paper deinking
The stale news that 200g is torn up places Hobart blender (Hobart Mixer) together with paper and 1500ml water.Bath temperature is set at 45 ℃.During beginning the about 0.5-1 of stirring at low speed minute, the lipoxygenase that is derived from Magnaporthe salvinii for preparing as mentioned above with 3.6 kilograms of/ton (7 pounds/ton) surfactants and 2mg (10mg/ ton paper pulp) adds in the blender then, add 500ml water then to Hobart, fully mix.Made the agitator low cruise about 30 minutes, the pulper temperature is set at 45 ℃, and the pH value is 7.
Half paper pulp is transferred in the container from blender, and is diluted to 10 liters, stirred then 2 minutes.
Raw material pad (feed pad): from blender, measure 30ml paper pulp, be diluted with water to 300ml, fully mix then.Use Wattman#40 filter paper filter paper pulp under vacuum.Filled up 10 minutes 90 ℃ (195F) dry down being somebody's turn to do.
Conventional Rubbing pad for washing use: measure the 900ml slurry from container, slowly to 80 purpose screen packs, shake lentamente then until discharging all water.Remove paper pulp, put it into then in the 1000ml beaker, the beaker water is added into the 900ml scale.Slow then agitating pulp, weighing 300ml slurry uses Wattman#40 filter paper filter paper pulp under vacuum then.Filled up 10 minutes 90 ℃ (195) dry down being somebody's turn to do.
The height Rubbing pad for washing use: weighing 900ml pulp from container, slowly to 80 purpose screen packs, shake until discharging all water then lentamente.Cleaned paper pulp 3 minutes with running water, remove paper pulp then, put it in the 1000ml beaker, the beaker water is added into the 900ml scale.Slow agitating pulp then, weighing 300ml slurry, use then the Wattman#40 filter paper under vacuum filter paper pulp to form filter pad.Should fill up 10 minutes with high speed drier (speed dryer) is dry down at 90 ℃ (195 °F).
Use Tappi standard method (T452), measure the brightness of pad by Macbeth color eye (color eye).
Use two kinds of commercial enzymes of buying, promptly lipase RESINASE A 2X and cellulase DENIMAX L compare experiment according to the above, and these two kinds of enzymes all can be available from the DK-2880Bagsvaerd of Denmark, the Novozymes A/S of Krogshoejvej 36.These two kinds of enzyme preparation amount are 0.51 kilogram of/ton paper pulp (1 pounds/ton).
The result is as shown in table 6.
Table 6
Enzyme Brightness
Raw material pad The pad that cleans The pad of Qing Xiing highly
Object of reference (not having enzyme) 38.5 41.7 45.9
Fatty acid oxidase 38.1 44.0 48.2
RESINASE A 2X (lipase) 40.6 42.9 45.9
DENIMAX L (cellulase) 37.6 39.0 44.2

Claims (19)

1. the purposes during the fatty acid oxidase paper material is made.
2. purposes as claimed in claim 1 is used to reduce the deposition of pitch.
3. as each described purposes among the claim 1-2, be used for bleaching.
4. as each described purposes among the claim 1-3, be used in, be used for deinking by making in the method for paper material in the papermaking slurry that comprises from the paper wood slip that reclaims, prints.
5. as each described purposes among the claim 1-4, wherein chemical pulp forms part and makes paper pulp used in the paper material.
6. as the purposes of each described fatty acid oxidase among the claim 1-5, use with the matrix that is used for this enzyme.
7. as the purposes of each described fatty acid oxidase among the claim 1-6, use with other enzyme with protease, lipase, zytase, keratoprotein enzyme, oxidoreducing enzyme, cellulase, endoglucanase, amylase, mannase, steroid esterase and/or cholesterol ester enzymatic activity.
8. purposes as claimed in claim 7, wherein other oxidoreducing enzyme has laccase and/or Peroxidase activity.
9. as each described purposes among the claim 7-8, wherein other enzyme has lipase active.
10. make the method for paper material, this method comprises the step of handling papermaking slurry and/or industrial water with fatty acid oxidase.
11. method as claimed in claim 10 also comprises forming and the step of the slurry of dry enzyme processing.
12. as each described method among the claim 10-11, wherein the result of enzyme processing generation is:
A) reduce the pitch deposition;
B) paper material of bleaching generation.
13. as each described method among the claim 10-12, wherein chemical pulp forms part and makes paper pulp used in the paper material.
14. as each described method among the claim 10-13, wherein papermaking slurry comprises from the slurry that reclaims the printing paper material, wherein enzyme is handled the result who produces the paper material that bleaching generated, and this result is that deinking efficiency owing to described enzyme brings to small part.
15. as each described method among the claim 10-14, wherein before the enzyme treatment step or among, add the matrix be used for described enzyme.
16., also comprise the step of handling papermaking slurry and/or industrial water with other enzyme with protease, lipase, zytase, keratoprotein enzyme, oxidoreducing enzyme, cellulase, endoglucanase, amylase, mannase, steroid esterase and/or cholesterol ester enzymatic activity as each described method among the claim 10-15.
17. method as claimed in claim 16, wherein other oxidoreducing enzyme has laccase and/or Peroxidase activity.
18. as each described method among the claim 16-17, wherein other enzyme has the activity of lipase.
19. as each described method among the claim 16-18, wherein the processing of carrying out with described other enzyme occurs in before the processing of carrying out with fatty acid oxidase, simultaneously and/or afterwards.
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