WO2003035972A1 - 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
WO2003035972A1
WO2003035972A1 PCT/DK2002/000697 DK0200697W WO03035972A1 WO 2003035972 A1 WO2003035972 A1 WO 2003035972A1 DK 0200697 W DK0200697 W DK 0200697W WO 03035972 A1 WO03035972 A1 WO 03035972A1
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WO
WIPO (PCT)
Prior art keywords
enzyme
pulp
fatty acid
paper
enzymes
Prior art date
Application number
PCT/DK2002/000697
Other languages
English (en)
French (fr)
Inventor
Kim Borch
Neal Franks
Henrik Lund
Hui Xu
Jing Luo
Original Assignee
Novozymes A/S
Novozymes North America, Inc.
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 Novozymes A/S, Novozymes North America, Inc. filed Critical Novozymes A/S
Priority to EP20020772086 priority Critical patent/EP1448848A1/en
Priority to CA 2461447 priority patent/CA2461447A1/en
Priority to JP2003538460A priority patent/JP2005506472A/ja
Priority to AU2002336917A priority patent/AU2002336917B2/en
Publication of WO2003035972A1 publication Critical patent/WO2003035972A1/en

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Classifications

    • 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

Definitions

  • the present invention relates to the use of a fatty acid oxidizing enzyme in the manufacture of a paper material, as well as a process for the manufacture of a paper material, the process comprising a step in which papermaking pulp and/or papermaking process water is treated with a fatty acid oxidizing enzyme.
  • enzymes in the manufacture of paper materials.
  • enzymes used for this purpose are proteases, lipases, xylanases, amylases, cellulases, as well as various oxidizing enzymes such as oxidoreductases (phenol oxidizing enzymes), for example laccases and peroxidases.
  • dissolved and colloidal substances are dispersed into the process water during the pulp and paper production.
  • the DCS are often referred to as wood pitch or wood resin. Pitch causes problems in paper machines by sticking to the rollers and causing spots or holes in the paper material.
  • Wood contains about 1 to 10% of pitch or extractives in addition to its main components cellulose, hemicellulose and lignin.
  • Major components of pitch are fatty acids, thglycerides, sterols, steryl esters and so-called resin acids, e.g. abietic acid.
  • WO 00/53843 discloses certain steryl esterase enzyme preparations and their use in the manufacture of paper to hydrolyze the steryl ester part of pitch.
  • US Patent No. 6,066,486 discloses an enzyme preparation comprising a cholesterol esterase derived from Pseudomonas fragi, and the use thereof to hydrolyze pulp resin.
  • JP 2000080581 discloses the use of certain peroxidases for the decomposition of abietic acid during pulping or paper making processes.
  • Microbiol. Biotechnol. (2001) 55:317-320 discloses experiments in which laccases were used to treat a model pitch preparation.
  • oxidizing enzymes viz. fatty acid oxidizing enzymes
  • An important effect of these enzymes is that the deposition of pitch is reduced.
  • these enzymes have a bleaching effect on the paper pulp and the resulting paper material.
  • a de- inking effect has been observed, too.
  • Paper and Pulp By the term a “paper-making process” is meant a process, wherein the pulp is suspended in water, mixed with various additives and then passed to equipment in which the paper, cardboard, tissue, towel etc. is formed, pressed and dried.
  • paper material refers to products, which can be made out of pulp, such as paper, linerboard, corrugated paperboard, tissue, towels, corrugated containers or boxes.
  • a papermaking pulp or “pulp” means any pulp which can be used for the production of a paper material.
  • the pulp can be supplied as a virgin pulp, or can be derived from a recycled source.
  • the papermaking pulp may be a wood pulp, a non-wood pulp or a pulp made from waste paper.
  • a wood pulp may be made from softwood such as pine, redwood, fir, spruce, cedar and hemlock or from hardwood such as maple, alder, birch, hickory, beech, aspen, acacia and eucalyptus.
  • a non-wood pulp may be made, e.g., from bagasse, bamboo, cotton or kenaf.
  • a waste paper pulp may be made by re-pulping waste paper such as newspaper, mixed office waste, computer print-out, white ledger, magazines, milk cartons, paper cups etc.
  • the papermaking pulp to be treated comprises both hardwood pulp and softwood pulp.
  • the wood pulp to be treated may be mechanical pulp (such as ground wood pulp, GP), chemical pulp (such as Kraft pulp or sulfite pulp), semichemical pulp (SCP), thermomechanical pulp (TMP), chemithermomechanical pulp (CTMP), or bleached chemithermomechanical pulp (BCTMP).
  • Mechanical pulp is manufactured by the grinding and refining methods, wherein the raw material is subjected to periodical pressure impulses.
  • TMP is thermomechanical pulp
  • GW groundwood pulp
  • PGW is pressurized groundwood pulp
  • RMP refiner mechanical pulp
  • PRMP pressurized refiner mechanical pulp
  • CTMP is chemithermimechanical pulp.
  • Chemical pulp is manufactured by alkaline cooking whereby most of the lignin and hemicellulose components are removed.
  • Kraft pulping or sulphate cooking sodium sulphide or sodium hydroxide are used as principal cooking chemicals.
  • the alkaline cooking the triglyceride part of pitch will be hydrolysed into fatty acids and glycerol.
  • Fatty acid oxidizing enzymes are particularly useful in the treatment of such pulps, because, as the designation tells, these enzymes will catalyze the further degradation of the fatty acids resulting from the alkaline hydrolysis of the triglycerides.
  • the Kraft pulp to be treated may be a bleached Kraft pulp, which may consist of softwood bleached Kraft (SWBK, also called NBKP (Nadel Holz Bleached Kraft Pulp)), hardwood bleached Kraft (HWBK, also called LBKP (Laub Holz Bleached Kraft Pulp and)) or a mixture of these.
  • SWBK softwood bleached Kraft
  • HWBK hardwood bleached Kraft
  • LBKP Lab Holz Bleached Kraft Pulp and
  • the pulp to be used in the process of the invention is a suspension of mechanical or chemical pulp or a combination thereof.
  • the pulp to be used in the process of the invention may comprise 0%, 10-20%, 20-30%, 30-40%, 40-50%, 50-60%, 60-70%, 70-80%, 80-90%, or 90-100% of chemical pulp.
  • a chemical pulp forms part of the pulp being used for manufacturing the paper material.
  • the expression "forms part of means that in the pulp to be used in the process of the invention, the percentage of chemical pulp lies within the range of 1-99%.
  • the percentage of chemical pulp lies within the range of 2-98%, 3-97%, 4-96%, 5-95%, 6-94%, 7- 93%, 8-92%, 9-91 %, 10-90%, 15-85%, 20-80%, 25-75%, 30-70%, 40-60%, or 45-55%.
  • the chemical pulp is a Kraft pulp, a sulfite pulp, a semichemical pulp (SCP), a thermomechanical pulp (TMP), a chemithermomechanical pulp (CTMP), a bleached chemithermomechanical pulp (BCTMP).
  • the Kraft pulp is bleached Kraft pulp, for example softwood bleached Kraft (SWBK, also called NBKP (Nadel Holz Bleached Kraft Pulp)), hardwood bleached Kraft (HWBK, also called LBKP (Laub Holz Bleached Kraft Pulp and)) or a mixture thereof.
  • the process of the invention is particularly applicable to the oxidation and hydrolysis of compounds constituting the pitch during a pulping or paper-making process, e.g. to avoid pitch troubles.
  • the process of the invention may be applied to any pitch-containing pulp, especially to pulps with a considerable content of linoleic acid or other unsaturated free fatty acids.
  • the process according to the invention can be carried out at any pulp production stage.
  • the enzyme can be added to any holding tank, e.g. to a pulp storing container (storage chest), storage tower, mixing chest or metering chest.
  • the enzyme treatment can be performed before the bleaching of pulp, in connection with the pulp bleaching process or after the bleaching.
  • the enzyme preparation may be added together with bleaching chemicals such as chlorine, chlorine dioxide. Applying oxygen gas, hydrogen peroxide or ozone or combinations thereof may also carry out the bleaching of pulp.
  • the enzyme preparation may also be added together with these substances. Preferably the enzyme preparation is added prior to bleaching.
  • the enzyme can also be added to the circulated process water (white water) originating from bleaching and process water (brown water) originating from the mechanical or chemimechanical pulping process. In a particular embodiment of a Kraft pulping process, the enzyme is added during the brown-stock washing.
  • process water comprises i.a. 1) water added as a raw material to the paper manufacturing process; 2) intermediate water products resulting from any step of the process for manufacturing the paper material; as well as 3) waste water as an output or by-product of the process.
  • the process water is, has been, is being, or is intended for being circulated (re-circulated), i.e. re-used in another step of the process.
  • water in turn means any aqueous medium, solution, suspension, e.g. ordinary tap water, and tap water in admixture with various additives and adjuvants commonly used in paper manufacturing processes.
  • the process water has a low content of solid (dry) matter, e.g. below 20%, 18%, 16%, 14%, 12%, 10%, 8%, 7%, 6%, 5%, 4%, 3%, 20% or below 1% dry matter.
  • the use and process of the invention does not include the use of the lipoxygenase derived from Magnaporthe saivinii as described in Example 2 of PCT/DK02/00251 for bleaching dye for pulp industry in waste water.
  • the process of the invention may be carried out at conventional conditions in the paper and pulp processing.
  • the process conditions will be a function of the enzyme(s) applied, the reaction time and the conditions given.
  • the enzyme of the invention should be added in an effective amount.
  • an effective amount is meant the amount sufficient to achieve the desired and expected effect, such as oxidizing pitch components, obtaining a desired bleaching and/or de-inking etc.
  • the dosage of the fatty acid oxidizing enzyme and additional enzymes, if any, is from about 0.1 mg enzyme protein to about 100.000 mg enzyme protein (of each enzyme) per ton of paper pulp.
  • the amount of the fatty acid oxidizing enzyme and additional enzymes, if any, is in the range of 0.00001-20; or 0.0001-20 mg of enzyme
  • the enzymatic treatment can be done at conventional consistency, e.g. 0.5-10 % dry substance.
  • the consistency is within the range of 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 0.5-5% dry substance.
  • the enzymatic treatment may be carried out at a temperature of from about 10 to about 100°C. Further examples of temperature ranges (all “from about” and “to about”) are the following:
  • a typical temperature is from about 20 to 90°C, or 20 to 95°C, preferably from about 40 to 70°C, or 40 to 75°C.
  • the enzymatic treatment may be carried out at a pH of from about 2 to about 12.
  • pH ranges are the following: 3-12, 4-12, 5-12, 6-12, 7-12, 8-12, 9-12, 2-11, 2-10, 2-9, 2-8, 4-10, 5-8 as well as any combination of the upper and lower values here indicated.
  • a typical pH range is from about 2 to 11 , preferably within the range from about 4 to 9.5, or 6 to 9.
  • a suitable duration of the enzymatic treatment may be in the range from a few seconds to several hours, e.g. from about 30 seconds to about 48 hours, or from about 1 minute to about 24 hours, or from about 1 minute to about 18 hours, or from about 1 minute to about 12 hours, or from about 1 minute to 5 hours, or from about 1 minute to about 2 hours, or from about 1 minute to about 1 hour, or from about 1 minute to about 30 minutes.
  • a typical reaction time is from about 10 minutes to 3 hours, 10 minutes to 10 hours, preferably 15 minutes to 1 hour, or 15 minutes to 2 hours.
  • Molecular oxygen from the atmosphere will usually be present in sufficient quantity, if required. Therefore, the reaction may conveniently be carried out in an open reactor, i.e. at atmospheric pressure.
  • Surfactants and/or dispersants are often present in, and/or added to a papermaking pulp.
  • the process and use of the present invention may be carried out in the presence of an anionic, non-ionic, cationic and/or zwitterionic surfactant and/or dispersant conventionally used in a papermaking pulp.
  • anionic surfactants are carboxylates, sulphates, sulphonates or phosphates of alkyl, substituted alkyl or aryl.
  • Fatty acids are examples of alkyl-carboxylates.
  • non-ionic surfactants are polyoxyethylene compounds, such as alcohol ethoxylates, propoxylates or mixed ethoxy- /propoxylates, poly-glycerols and other polyols, as well as certain block-copolymers.
  • cationic surfactants are water-soluble cationic polymers, such as quartenary ammonium sulphates and certain amines, e.g. epichlorohydrin/dimethylamine polymers (EPI-DMA) and cross-linked solutions thereof, polydiallyl dimethyl ammonium chloride (DADMAC), DADMAC/Acrylamide co-polymers, and ionene polymers, such as those disclosed in US patents nos.
  • zwitterionic or amphoteric surfactants are betains, glycinates, amino propionates, imino propionates and various imidazolin-derivatives. Also the polymers disclosed in US patent no. 5,256,252 may be used.
  • surfactants such as the above, including any combination thereof may be used in a paper making process together with a fatty acid oxidizing enzyme as defined herein, and included in a composition together with such enzyme.
  • the amount of each surfactant in such composition may amount to from about 8 to about 40% (w/w) of the composition.
  • the amount of each surfactant is from about 10 to about 38, or from about 12 to about 36, or from about 14 to about 34, or from about 16 to about 34, or from about 18 to about 34, or from about 20 to about 34, or from about 22 to about 34, or from about 24 to about 34, or from about 26 to about 34, or from about 28 to about 32% (w/w).
  • each of the above ranges refers to the total amount of surfactants.
  • EC-numbers may be used for classification of enzymes, e.g. lipase EC-number for enzymes having lipase activity, etc.
  • enzyme as well as the various enzymes and enzyme classes mentioned herein, encompass wild-type enzymes, as well as any variant thereof that retains the activity in question. Such variants may be produced by recombinant techniques.
  • the wild-type enzymes may also be produced by recombinant techniques, or by isolation and purification from the natural source.
  • the enzyme in question is well-defined, meaning that only one major enzyme component is present. This can be inferred e.g. by fractionation on an appropriate Size-exclusion column.
  • Such well-defined, or purified, or highly purified, enzyme can be obtained as is known in the art and/or described in publications relating to the specific enzyme in question.
  • a fatty acid oxidizing enzyme means at least one of such enzymes.
  • at least one means one, two, three, four, five, six or even more of such enzymes.
  • a fatty acid oxidizing enzyme is an enzyme which hydrolyzes the substrate linoleic acid more efficiently than the substrate syringaldazine.
  • the enzyme in question qualifies as a fatty acid oxidizing enzyme as defined herein. If the RRD is zero, or below zero the enzyme in question is not a fatty acid oxidizing enzyme. In particular embodiments, the RRD is at least 0.05, 0.10, 0.15, 0.20, or at least 0.25 absorbancy units/minute. In a particular embodiment of the method of Example 2, the enzymes are well- defined. Still further, for the method of Example 2 the enzyme dosage is adjusted so as to obtain a maximum absorbancy increase per minute at 234 nm, or at 530 nm.
  • the maximum absorbancy increase is within the range of 0.05-0.50; 0.07-0.4; 0.08-0.3; 0.09-0.2; or 0.10-0.25 absorbancy units pr. min.
  • the enzyme dosage may for example be in the range of 0.01-20; 0.05-15; or 0.10-10 mg enzyme protein per ml.
  • a "fatty acid oxidizing enzyme” may be defined as an enzyme capable of oxidizing unsaturated fatty acids more efficiently than syringaldazine.
  • the activity of the enzyme could be compared in a standard oximeter setup as described in Example 1 of the present application at pH 6 and 30°C including either syringaldazine or linoleic acid as substrates.
  • the fatty acid oxidizing enzyme is defined as an enzyme classified as EC 1.11.1.3, or as EC 1.13.11.-.
  • EC 1.13.11.- means any of the sub-classes thereof, presently forty-nine: EC 1.13.11.1 -EC 1.13.11.49.
  • EC 1.11.1.3 is designated fatty acid peroxidase, and EC 1.13.11.- is designated oxygenases acting on single donors with incorporation of two atoms of oxygen.
  • the EC 1.13.11.- enzyme is classified as EC
  • EC 1.13.11.45 designated lipoxygenase, arachidonate 12-lipoxygenase, arachidonate 15- lipoxygenase, arachidonate 5-lipoxygenase, arachidonate 8-lipoxygenase, linoleate diol synthase, and linoleate 11 -lipoxygenase, respectively).
  • the fatty acid oxidizing enzyme is a lipoxygenase (LOX), classified as EC 1.13.11.12, which is an enzyme that catalyzes the oxygenation of polyunsaturated fatty acids, especially c/s,c/s-1 ,4-dienes, e.g. linoleic acid and produces a hydroperoxide.
  • LOX lipoxygenase
  • other substrates may be oxidized, e.g. monounsaturated fatty acids.
  • Microbial lipoxygenases can be derived from, e.g., Saccharomyces cerevisiae, Thermoactinomyces vulgaris, Fusarium oxysporum, Fusarium proliferatum, Thermomyces lanuginosus, Pyricularia oryzae, and strains of Geotrichum.
  • Saccharomyces cerevisiae Thermoactinomyces vulgaris
  • Fusarium oxysporum Fusarium proliferatum
  • Thermomyces lanuginosus Pyricularia oryzae
  • the preparation of a lipoxygenase derived from Gaeumannomyces graminis is described in Examples 3-4 of WO 02/20730.
  • Lipoxygenase may also be extracted from plant seeds, such as soybean, pea, chickpea, and kidney bean. Alternatively, lipoxygenase may be obtained from mammalian cells, e.g. rabbit reticulocytes.
  • Lipoxygenase activity may be determined spectrophotometrically at 25°C by monitoring the formation of hydroperoxides.
  • 10 micro liters enzyme was added to a 1 ml quartz cuvette containing 980 micro liter 25 mM sodium phosphate buffer (pH 7.0) and 10 micro liter of substrate solution (10 mM linoleic acid dispersed with 0.2%(v/v) Tween20 (should not be kept for extended time periods)).
  • the enzyme was typically diluted sufficiently to ensure a turn-over of maximally 10% of the added substrate within the first minute.
  • the absorbance at 234 nm was followed and the rate was estimated from the linear part of the curve.
  • the c/s-frans-conjugated hydro(pero)xy fatty acids were assumed to have a molecular extinction coefficient of 23,000 M "1 cm "1 .
  • the fatty acid oxidizing enzyme may also be applied together with a substrate for the enzyme capable of enhancing the enzymatic effect.
  • Suitable substrates are hydrolyzed oils such as oils from soybeans (rich in linoleic acid) or tall oil. Fatty acid substrates may be released from the added oil by lipolytic enzymes or produced during the Kraft pulping or sulphate cooking.
  • the substrate is a compound with 1 ,4-pentadien structure, e.g. with c/s,c/s-1 ,4-pentadien structure, i.e. compounds having at least one such element in its structural formula.
  • substrates are unsaturated fatty acids, e.g. palmitoleic acid, oleic acid, linoleic acid, linolenic acid, and arachidonic acid, as well as their salts and esters, e.g. methyl- and ethyl-esters.
  • the substrate is linoleic acid; linoleic acid methyl or ethyl ester; linolenic acid, or linolenic acid methyl or ethyl ester.
  • the spectrum of 10 mM abietic acid (emulsified in 0.2% Tween 20) is recorded. Characteristic peaks are observed around 200 nm and around 250 nm.
  • a fatty acid oxidizing enzyme is added to the abietic acid emulsion.
  • a substrate for the fatty acid oxidizing enzyme is also added. The enzyme is e.g.
  • the degradation of abietic acid is followed spectrophotometrically, and the peaks around 200 nm and around 250 nm decrease more rapidly when linoleic acid is added together with the lipoxygenase.
  • the substrate e.g. linoleic acid
  • the substrate is added in an amount of 5-10000 ppm (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 200-700 ppm.
  • 333 ppm of linoleic acid was used together with a fatty acid oxidizing enzyme.
  • the fatty acid oxidizing enzyme is used in an amount of 0.005-50 ppm (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- 0.5 ppm.
  • the amount of enzyme refers to mg of a well-defined enzyme preparation.
  • the fatty acid oxidizing enzyme may be applied alone or together with an additional enzyme.
  • an additional enzyme means at least one additional enzyme, e.g. one, two, three, four, five, six, seven, eight, nine, ten or even more additional enzymes.
  • the term “applied together with” means that the additional enzyme may be applied in the same, or in another step of the process of the invention.
  • the other process step may be upstream or downstream in the paper manufacturing process, as compared to the step in which the papermaking pulp or process water is treated with a fatty acid oxidizing enzyme.
  • the additional enzyme is an enzyme which has protease, lipase, xylanase, cutinase, oxidoreductase, cellulase, endoglucanase, amylase, mannanase, steryl esterase, and/or cholesterol esterase activity.
  • oxidoreductase enzymes are enzymes with laccase, and/or peroxidase activity.
  • the additional enzyme is lipase.
  • a step of a process means at least one step, and it could be one, two, three, four, five or even more process steps.
  • the fatty acid oxidizing enzyme of the invention may be applied in at least one process step, and the additional enzyme(s) may also be applied in at least one process step, which may be the same or a different process step as compared to the step where the fatty acid oxidizing enzyme is used.
  • enzyme preparation means a product containing at least one fatty acid oxidizing enzyme.
  • the enzyme preparation may also comprise enzymes having other enzyme activities, preferably lipolytic enzymes or enzymes having oxidoreductase activity, most preferably lipolytic enzymes.
  • enzymes having other enzyme activities preferably lipolytic enzymes or enzymes having oxidoreductase activity, most preferably lipolytic enzymes.
  • a preparation preferably contains at least one adjuvant.
  • adjuvants which are used in enzyme preparations for the paper and pulp industry are buffers, polymers, surfactants and stabilizing agents.
  • Any enzyme having protease, lipase, xylanase, cutinase, oxidoreductase, cellulase endoglucanase, amylase, mannanase, steryl esterase, and/or cholesterol esterase activity can be used as additional enzymes in the use and process of the invention. Below some non- limiting examples are listed of such additional enzymes.
  • the enzymes written in capitals are commercial enzymes available from Novozymes A/S, Krogshoejvej 36, DK-2880 Bagsvaerd, Denmark. The activity of any of those additional enzymes can be analyzed using any method known in the art for the enzyme in question, including the methods mentioned in the references cited.
  • cutinases are those derived from Humicola insolens (US 5,827,719); from a strain of Fusarium, e.g. F. roseum culmorum, or particularly F. solani pisi (WO 90/09446; WO 94/14964, WO 94/03578).
  • the cutinase may also be derived from a strain of Rhizoctonia, e.g. R. solani, or a strain of Alternaria, e.g. A. brassicicola (WO 94/03578), or variants thereof such as those described in WO 00/34450, or WO 01/92502.
  • proteases examples include the ALCALASE, ESPERASE, SAVINASE, NEUTRASE and DURAZYM proteases.
  • Other proteases are derived from Nocardiopsis, Aspergillus, Rhizopus, Bacillus alcalophilus, B. cereus, B. natto, B. vulgatus, B. mycoide, and subtilisins from Bacillus, especially proteases from the species Nocardiopsis sp. and Nocardiopsis dassonvillei such as those disclosed in WO 88/03947, and mutants thereof, e.g. those disclosed in WO 91/00345 and EP 415296.
  • amylases are the BAN, AQUAZYM, TERMAMYL, and AQUAZYM Ultra amylases.
  • An example of a lipase is the RESINASE A2X lipase.
  • An example of a xylanase is the PULPZYME HC hemicellulase.
  • Examples of endoglucanases are the NOVOZYM 613, 342, and 476 enzyme products.
  • mannanases are the Trichoderma reesei endo-beta-mannanases described in Stahlbrand et al, J. Biotechnol. 29 (1993), 229-242.
  • steryl esterases examples include steryl esterases. peroxidases, laccases, and cholesterol esterases are disclosed in the references mentioned in the background art section hereof. Further examples of oxidoreductases are the peroxidases and laccases disclosed in EP 730641 ; WO 01/98469; EP 719337; EP 765394; EP 767836; EP 763115; and EP 788547. In the present context, whenever an oxidoreductase enzyme is mentioned that requires or benefits from the presence of acceptors (e.g. oxygen or hydrogenperoxide), enhancers, mediators and/or activators, such compounds should be considered to be included.
  • acceptors e.g. oxygen or hydrogenperoxide
  • enhancers and mediators are disclosed in EP 705327; WO 98/56899; EP 677102; EP 781328; and EP 707637. If desired a distinction could be made by defining an oxidoreductase enzyme system (e.g. a laccase, or a peroxidase enzyme system) as the combination of the enzyme in question and its acceptor, and optionally also an enhancer and/or mediator for the enzyme in question.
  • an oxidoreductase enzyme system e.g. a laccase, or a peroxidase enzyme system
  • a process for reducing deposition of pitch in the paper making process comprising treating the pulp and/or process water with an enzyme preparation comprising a fatty acid oxidizing enzyme; preferably a process wherein the pulp is a mechanical pulp or a chemical pulp or a combination thereof; such as a chemical pulp.
  • the enzyme is classified in EC 1.13.11 , preferably 1.13.11.12, preferably wherein the enzyme is derived from a strain of the genus Magnaporthaceae, preferably M. saivinii or the genus Gaeumannomyces, preferably G.
  • graminis The process described above, wherein the treatment is carried out by adding a substrate for the enzyme, preferably linoleic acid.
  • a substrate for the enzyme preferably linoleic acid.
  • the enzyme preparation comprises a lipolytic enzyme and/or a further oxidoreductase.
  • the process described above wherein the treatment is carried out at a temperature is in the range 20-90 °C, preferably 40-70 °C, and/or at a pH in the range 2-11, preferably 4-9.5, more preferably 6-9, and/or wherein treatment is carried out in 10 minutes to 3 hours, preferably 15 minutes to 1 hour; and/or wherein the enzyme is added in a concentration in the range of 0.0001-20 mg/g, preferably 0.0001-10 mg/g, more preferably 0.001-1 mg/g and most preferably 0.01-0.1 mg/g.
  • the enzyme preparation is added in the storage chest or mixing chest before the paper machine.
  • lipoxygenases were prepared as previously described. The temperature was 25°C. The concentration of dissolved oxygen (mg/l) is measured and plotted as a function of time (min.). The enzymatic activity is calculated as the slope of the linear part of the curve (mg/l/min.) after addition of the enzyme.
  • the baseline was corrected by subtraction when relevant, meaning that if the curve showing oxygen concentration as a function of time had a slope of above about 0.05 mg oxygen/ml/min before addition of the fatty acid oxidizing enzyme (i.e. the control), this value was subtracted from the sample slope value.
  • Table 1 shows the results of the experiments.
  • the laccase derived from Polyporus pinsitus had a MW by SDS-Page of 65 kDa, a pi by IEF of 3.5, and an optimum temperature at pH 5.5 of 60°C.
  • the laccase derived from Coprinus cinereus had a MW by SDS-Page of 67-68 kDa, a pi by IEF of 3.5-3.8, and an optimum temperature at pH 7.5 of 65°C.
  • the enzymes were prepared and purified as described in WO 96/00290 and US patent no. 6,008,029.
  • the two lipoxygenases were derived from Magnaporthe saivinii and Gaeumannomyces graminis, and they were prepared as described previously.
  • the enzyme dosage was adjusted to ensure maximum absorbancy increase per minute at 234 nm / 530 nm, viz. in the range of 0.1 - 0.25 absorbancy units pr. min.
  • Substrate solution 11.65 mg linoleic acid (60% Sigma), as well as 12.5 ml 0.56 mM Syringaldazine (Sigma) in ethanol was mixed with deionized water to a total volume of 25 ml.
  • the enzyme preparation to be tested was transferred to a quartz cuvette containing 900 microliter phosphate buffer (50 mM, pH 7.0) and 50 microliter of the substrate solution
  • the cuvette was placed in a spectrofotometer, thermostated at 23°C, and the absorbancies at 234 nm and 530 nm were measured as a function of time.
  • the absorbancy at 530 nm is indicative of degradation of syringaldazine
  • the absorbancy at 234 nm is indicative of degradation of linoleic acid.
  • the absorbancy increase as a function of time is calculated on the basis of minutes 2 to 4 of the reaction time, i.e. d(A 234 )/dt, as well as
  • a model pitch is prepared as follows: 50 % Linoleic Acid 60% (Sigma L-1626). 20 % Abietic Acid (Sigma A9424). 20 % Oleic Acid (Merck 471). 5 % Cholesterol-Linoleate (Sigma C-0289). 5 % Olive Oil (Sigma O-1500). Mixed for 30 minutes at 65°C. Stored in refrigerator for no longer than 30 days.
  • a similar amount of buffer (50 mM borate pH 9.0) is added to the wells of microtiterplates B and D.
  • the microtiterplates are then incubated during shaking (600 rpm) for 30 minutes.
  • 20 microliter of the enzyme-treated pitch suspension is transferred onto a second set of microtiterplates corresponding to microtiterplates A-D (Corning Inc. Costar UV plate 96 well No. 3635) each containing 200 microliter ethanol per well (solubilizing the pitch components).
  • Abietic acid a major component of the pitch, absorps strongly at about 255nm. Accordingly, A 255 is indicative of the amount of pitch remaining in the suspension.
  • a 255 is determined as the average of 8 identical experiments, and the amount of pitch adsorbed onto the paper is estimated based on the variation in A 255 measured in the pitch suspensions obtained after incubation with and without paper present (after 11x dilution in ethanol).
  • the results are shown in a table like the below Table 3.
  • the basic (blind) adsorption of pitch onto the paper in the absence of a fatty acid oxidizing enzyme may be calculated as the ratio D/B.
  • the effect of the enzyme (the sample) as regards the adsorption of pitch to the paper may be calculated as the ratio C/A.
  • One way of showing hat the enzyme has caused a reduction in the deposition of pitch is if (C/A - D/B) is below zero.
  • the enzyme effect may be calculated as ((C-A)-(D-B)), and if this value is below zero, this would be another way of showing the effect of the enzyme on the deposition of pitch.
  • Other solid materials than paper may also be tested, e.g. metal, and textile (Style 400 cotton).
  • the above ways of showing reduction in pitch deposition are applicable by analogy as regards deposition on the other solid materials.
  • the assay-pH i.e. buffer
  • the assay-temperature is selected paying regard to the characteristics of the fatty acid oxidizing enzyme in question, e.g. an assay pH of around 4, 5, 6, 7, 8, 9, 10, or 11 ; and an assay-temperature of around 10, 15, 20, 25, 30, 37, 40, 50, 60, 70, 80, 90 or 95°C.
  • Example 4 Bleaching paper with a fatty acid oxidizing enzyme
  • Treatments with a fatty acid oxidizing enzyme were carried out in beakers containing 3 g dry pulp i.e. 300 ml pulp slurry. The treatments were carried out at 25°C in a water bath with agitation by magnetic stir bars, 500 rpm. 333 ppm linoleic acid was added to all beakers.
  • the fatty acid oxidizing enzyme used was a purified lipoxygenase derived from Gaeumannomyces graminis prepared as described previously. The amount of enzyme used appears from Tables 4 and 5 below.
  • the enzyme treatment was carried out for 2 hours. Two beakers were run for each condition. After two hours the enzyme reaction was stopped by addition of 5 ml (fixed amount) of
  • the content of the beaker was transferred quantitatively to a 1000 ml beaker using 700 ml deionised water.
  • This pulp suspension was poured onto a B ⁇ chner funnel (15 cm diameter) with a filter paper.
  • a paper sheet was formed by sucking the water out.
  • the paper sheet was removed from the funnel and separated from the filter paper.
  • the sheet was pressed in a sheet press manufactured by Lorentzen and Wettre.
  • the sheet was pressed in a sandwich of metal plate, 2 blotting papers, 2 filter papers, the sheet, 2 filter papers, 2 blotting papers, metal plate at 0,4 MPa for 5.5 min.
  • Wet papers were replaced by dry ones and the pressing repeated at 0.4 MPa for 2 min.
  • the sheets were air dried overnight.
  • the brightness of the sheets was measured using a Macbeth Color-Eye 7000 reflectometer. The brightness was recorded at 600nm. 4 measurements were done at each sheet. The results obtained are shown in Table 4 below.
  • the Kappa Number which describes the degree of delignification of a pulp, was also determined for each sheet using the method described in Tappi Test Methods T236 (Tappi Press). The amounts used for each determination was of that described in the standard method. The dry matter content of the sheets was determined to calculate the Kappa no. The results obtained are shown in Table 5 below. Table 4
  • the pulp was slowly stirred. 300 ml of the pulp slurry was measured and filtered through a
  • Hyper-washing of pads 900 ml of pulp slurry was measured from the container, poured slowly onto an 80 mesh sieve and shaken slowly until all free water drained. The pulp was rinsed with faucet water for 3 minutes, removed and put into a 1000 ml beaker, which was filled with water up to the 900 ml line. The pulp was slowly stirred. 300 ml of the pulp slurry was measured and filtered through a Wattman #40 filter paper to make a filter pad. The pads were dried on a speed dryer at 90°C (195°F) for 10 minutes. The brightness of the pads was determined by a Macbeth color eye using a Tappi standard method (T452).

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EP1579056A1 (en) * 2002-12-20 2005-09-28 Novozymes North America, Inc. Treatment of fabrics, fibers, or yarns
WO2005098131A1 (en) * 2004-04-08 2005-10-20 Ciba Specialty Chemicals Holding Inc. An additive, use of said additive in paper or board production, a method of improving paper or board manufacturing and a method of improving paper or board product
JP2007515570A (ja) * 2003-12-23 2007-06-14 ケミラ オサケ ユキチュア ユルキネン 機械パルプ及び高収率化学パルプの色戻りの低減方法
EP1908876A1 (en) * 2005-07-06 2008-04-09 Consejo Superior de Investigaciones Cientificas Mediator-enzyme system for controlling pitch deposits in pulp and paper production
WO2010029214A1 (en) * 2008-09-10 2010-03-18 Upm-Kymmene Corporation A method for manufacturing mechanical pulp and a use of the mechanical pulp
WO2012149192A1 (en) 2011-04-28 2012-11-01 Novozymes, Inc. Polypeptides having endoglucanase activity and polynucleotides encoding same
EP2549012A1 (fr) * 2011-07-20 2013-01-23 Realco SA Procédé de traitement de papier résistant à l'état humide
WO2013063356A3 (en) * 2011-10-27 2013-08-15 Buckman Laboratories International, Inc. Method and composition for enzymatic treatment of fiber for papermaking, and paper products made therewith
WO2013191803A1 (en) * 2012-06-22 2013-12-27 Buckman Laboratories International,Inc. Methods of using combinations of a lipase and an oxidant for pitch control in paper making processes and products thereof
US11771091B2 (en) 2012-05-29 2023-10-03 Neozyme International, Inc. Non-toxic plant agent compositions and methods and uses thereof
US11773535B2 (en) 2012-05-29 2023-10-03 Neozyme International, Inc. Papermaking additive compositions and methods and uses thereof
US11930823B2 (en) 2012-05-29 2024-03-19 Neozyme International, Inc. Non-toxic pest control compositions and methods and uses thereof

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WO1992013130A1 (en) * 1991-01-25 1992-08-06 Novo Nordisk A/S Method for avoiding pitch troubles by use of thermostable lipase
US5370770A (en) * 1992-11-09 1994-12-06 The Mead Corporation Method for deinking printed waste paper using soybean peroxidase
WO2000053843A1 (en) * 1999-03-08 2000-09-14 Valtion Teknillinen Tutkimuskeskus A process and an enzyme preparation with steryl esterase activity for controlling pitch during paper manufacture
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Cited By (17)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP1579056A1 (en) * 2002-12-20 2005-09-28 Novozymes North America, Inc. Treatment of fabrics, fibers, or yarns
EP1579056A4 (en) * 2002-12-20 2007-04-25 Novozymes North America Inc TREATMENT OF TEXTILE SURFACES, FIBERS OR YARN
JP2007515570A (ja) * 2003-12-23 2007-06-14 ケミラ オサケ ユキチュア ユルキネン 機械パルプ及び高収率化学パルプの色戻りの低減方法
WO2005098131A1 (en) * 2004-04-08 2005-10-20 Ciba Specialty Chemicals Holding Inc. An additive, use of said additive in paper or board production, a method of improving paper or board manufacturing and a method of improving paper or board product
EP1908876A1 (en) * 2005-07-06 2008-04-09 Consejo Superior de Investigaciones Cientificas Mediator-enzyme system for controlling pitch deposits in pulp and paper production
EP1908876A4 (en) * 2005-07-06 2012-03-21 Consejo Superior Investigacion MEDIATOR ENZYME SYSTEM FOR COMBATING RESIN FURNITURE IN PULP AND PAPER MANUFACTURING
WO2010029214A1 (en) * 2008-09-10 2010-03-18 Upm-Kymmene Corporation A method for manufacturing mechanical pulp and a use of the mechanical pulp
WO2012149192A1 (en) 2011-04-28 2012-11-01 Novozymes, Inc. Polypeptides having endoglucanase activity and polynucleotides encoding same
EP2549012A1 (fr) * 2011-07-20 2013-01-23 Realco SA Procédé de traitement de papier résistant à l'état humide
WO2013063356A3 (en) * 2011-10-27 2013-08-15 Buckman Laboratories International, Inc. Method and composition for enzymatic treatment of fiber for papermaking, and paper products made therewith
US8652301B2 (en) 2011-10-27 2014-02-18 Buckman Laboratories International, Inc. Method and composition for enzymatic treatment of fiber for papermaking, and paper products made therewith
US8784613B2 (en) 2011-10-27 2014-07-22 Buckman Laboratories International, Inc. Method and composition for enzymatic treatment of fiber for papermaking, and paper products made therewith
US11771091B2 (en) 2012-05-29 2023-10-03 Neozyme International, Inc. Non-toxic plant agent compositions and methods and uses thereof
US11773535B2 (en) 2012-05-29 2023-10-03 Neozyme International, Inc. Papermaking additive compositions and methods and uses thereof
US11930823B2 (en) 2012-05-29 2024-03-19 Neozyme International, Inc. Non-toxic pest control compositions and methods and uses thereof
WO2013191803A1 (en) * 2012-06-22 2013-12-27 Buckman Laboratories International,Inc. Methods of using combinations of a lipase and an oxidant for pitch control in paper making processes and products thereof
US8657996B2 (en) 2012-06-22 2014-02-25 Buckman Laboratories International, Inc. Methods of using combinations of a lipase and an oxidant for pitch control in paper making processes and products thereof

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