WO2007095575A1 - Chemical pulp treatment compositions and methods - Google Patents
Chemical pulp treatment compositions and methods Download PDFInfo
- Publication number
- WO2007095575A1 WO2007095575A1 PCT/US2007/062136 US2007062136W WO2007095575A1 WO 2007095575 A1 WO2007095575 A1 WO 2007095575A1 US 2007062136 W US2007062136 W US 2007062136W WO 2007095575 A1 WO2007095575 A1 WO 2007095575A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- strain
- pulp
- lipase
- chemical pulp
- peroxide source
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims abstract description 75
- 229920001131 Pulp (paper) Polymers 0.000 title claims abstract description 30
- 239000000203 mixture Substances 0.000 title abstract description 11
- 108090001060 Lipase Proteins 0.000 claims abstract description 35
- 102000004882 Lipase Human genes 0.000 claims abstract description 35
- 239000004367 Lipase Substances 0.000 claims abstract description 33
- 235000019421 lipase Nutrition 0.000 claims abstract description 33
- 150000002978 peroxides Chemical class 0.000 claims abstract description 29
- 150000007524 organic acids Chemical class 0.000 claims abstract description 7
- 102000004190 Enzymes Human genes 0.000 claims description 43
- 108090000790 Enzymes Proteins 0.000 claims description 43
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical group OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims description 26
- 239000002655 kraft paper Substances 0.000 claims description 23
- 239000000123 paper Substances 0.000 claims description 22
- 241000222120 Candida <Saccharomycetales> Species 0.000 claims description 11
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 5
- 241000228212 Aspergillus Species 0.000 claims description 4
- 241000235527 Rhizopus Species 0.000 claims description 4
- LSNNMFCWUKXFEE-UHFFFAOYSA-N Sulfurous acid Chemical compound OS(O)=O LSNNMFCWUKXFEE-UHFFFAOYSA-N 0.000 claims description 4
- 241000766694 Hyphozyma Species 0.000 claims description 3
- 238000004061 bleaching Methods 0.000 claims description 3
- 239000002243 precursor Substances 0.000 claims description 3
- 239000000758 substrate Substances 0.000 claims description 3
- 241000590020 Achromobacter Species 0.000 claims description 2
- 101710098556 Lipase A Proteins 0.000 claims description 2
- 101710099648 Lysosomal acid lipase/cholesteryl ester hydrolase Proteins 0.000 claims description 2
- 102100026001 Lysosomal acid lipase/cholesteryl ester hydrolase Human genes 0.000 claims description 2
- 241000235402 Rhizomucor Species 0.000 claims description 2
- 239000011087 paperboard Substances 0.000 claims description 2
- MWNQXXOSWHCCOZ-UHFFFAOYSA-L sodium;oxido carbonate Chemical compound [Na+].[O-]OC([O-])=O MWNQXXOSWHCCOZ-UHFFFAOYSA-L 0.000 claims description 2
- 101710098554 Lipase B Proteins 0.000 claims 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 claims 1
- 239000001301 oxygen Substances 0.000 claims 1
- 229910052760 oxygen Inorganic materials 0.000 claims 1
- 230000008569 process Effects 0.000 abstract description 48
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 abstract description 22
- 229940088598 enzyme Drugs 0.000 description 40
- 229960002163 hydrogen peroxide Drugs 0.000 description 9
- 239000011347 resin Substances 0.000 description 9
- 229920005989 resin Polymers 0.000 description 9
- 238000004519 manufacturing process Methods 0.000 description 8
- -1 triglycerdies Chemical class 0.000 description 8
- 230000002255 enzymatic effect Effects 0.000 description 7
- 239000004094 surface-active agent Substances 0.000 description 7
- 241000589516 Pseudomonas Species 0.000 description 6
- 239000002253 acid Substances 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- 108090000854 Oxidoreductases Proteins 0.000 description 5
- 102000004316 Oxidoreductases Human genes 0.000 description 5
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- 102000003992 Peroxidases Human genes 0.000 description 5
- 239000004365 Protease Substances 0.000 description 5
- 150000007513 acids Chemical class 0.000 description 5
- 235000014113 dietary fatty acids Nutrition 0.000 description 5
- 229930195729 fatty acid Natural products 0.000 description 5
- 239000000194 fatty acid Substances 0.000 description 5
- 150000004665 fatty acids Chemical class 0.000 description 5
- ROSDSFDQCJNGOL-UHFFFAOYSA-N Dimethylamine Chemical compound CNC ROSDSFDQCJNGOL-UHFFFAOYSA-N 0.000 description 4
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- 241000223198 Humicola Species 0.000 description 4
- 238000010411 cooking Methods 0.000 description 4
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- 238000002360 preparation method Methods 0.000 description 4
- BTXXTMOWISPQSJ-UHFFFAOYSA-N 4,4,4-trifluorobutan-2-one Chemical compound CC(=O)CC(F)(F)F BTXXTMOWISPQSJ-UHFFFAOYSA-N 0.000 description 3
- BQACOLQNOUYJCE-FYZZASKESA-N Abietic acid Natural products CC(C)C1=CC2=CC[C@]3(C)[C@](C)(CCC[C@@]3(C)C(=O)O)[C@H]2CC1 BQACOLQNOUYJCE-FYZZASKESA-N 0.000 description 3
- RSWGJHLUYNHPMX-UHFFFAOYSA-N Abietic-Saeure Natural products C12CCC(C(C)C)=CC2=CCC2C1(C)CCCC2(C)C(O)=O RSWGJHLUYNHPMX-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
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- 229920002871 Dammar gum Polymers 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 101000898082 Homo sapiens Calbindin Proteins 0.000 description 3
- 108010029541 Laccase Proteins 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108700020962 Peroxidase Proteins 0.000 description 3
- 101001021643 Pseudozyma antarctica Lipase B Proteins 0.000 description 3
- 108010055297 Sterol Esterase Proteins 0.000 description 3
- 102000000019 Sterol Esterase Human genes 0.000 description 3
- 239000000654 additive Substances 0.000 description 3
- 239000002671 adjuvant Substances 0.000 description 3
- 235000019418 amylase Nutrition 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 150000002148 esters Chemical class 0.000 description 3
- 238000004537 pulping Methods 0.000 description 3
- LTMQZVLXCLQPCT-UHFFFAOYSA-N 1,1,6-trimethyltetralin Chemical compound C1CCC(C)(C)C=2C1=CC(C)=CC=2 LTMQZVLXCLQPCT-UHFFFAOYSA-N 0.000 description 2
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 2
- 241000235389 Absidia Species 0.000 description 2
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- 241000223651 Aureobasidium Species 0.000 description 2
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- 241000206605 Brochothrix Species 0.000 description 2
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- 108010059892 Cellulase Proteins 0.000 description 2
- 241000511343 Chondrostoma nasus Species 0.000 description 2
- 241000223218 Fusarium Species 0.000 description 2
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- KFSLWBXXFJQRDL-UHFFFAOYSA-N Peracetic acid Chemical compound CC(=O)OO KFSLWBXXFJQRDL-UHFFFAOYSA-N 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 241001361634 Rhizoctonia Species 0.000 description 2
- 241000223252 Rhodotorula Species 0.000 description 2
- 229930182558 Sterol Natural products 0.000 description 2
- BGRWYDHXPHLNKA-UHFFFAOYSA-N Tetraacetylethylenediamine Chemical compound CC(=O)N(C(C)=O)CCN(C(C)=O)C(C)=O BGRWYDHXPHLNKA-UHFFFAOYSA-N 0.000 description 2
- 241000223259 Trichoderma Species 0.000 description 2
- 241000607632 Vibrio alginolyticus chemovar iophagus Species 0.000 description 2
- 239000000370 acceptor Substances 0.000 description 2
- 239000012190 activator Substances 0.000 description 2
- 108010055059 beta-Mannosidase Proteins 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000007844 bleaching agent Substances 0.000 description 2
- 229940106157 cellulase Drugs 0.000 description 2
- 229940079919 digestives enzyme preparation Drugs 0.000 description 2
- 239000002270 dispersing agent Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000011121 hardwood Substances 0.000 description 2
- 229940039696 lactobacillus Drugs 0.000 description 2
- 229920005610 lignin Polymers 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 230000035484 reaction time Effects 0.000 description 2
- 238000010188 recombinant method Methods 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 239000011122 softwood Substances 0.000 description 2
- 150000003432 sterols Chemical class 0.000 description 2
- 235000003702 sterols Nutrition 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 239000008399 tap water Substances 0.000 description 2
- 235000020679 tap water Nutrition 0.000 description 2
- 150000004670 unsaturated fatty acids Chemical class 0.000 description 2
- 235000021122 unsaturated fatty acids Nutrition 0.000 description 2
- LJCNDNBULVLKSG-UHFFFAOYSA-N 2-aminoacetic acid;butane Chemical compound CCCC.CCCC.NCC(O)=O LJCNDNBULVLKSG-UHFFFAOYSA-N 0.000 description 1
- 241000607534 Aeromonas Species 0.000 description 1
- 108010025188 Alcohol oxidase Proteins 0.000 description 1
- 241001237431 Anomala Species 0.000 description 1
- 240000008791 Antiaris toxicaria Species 0.000 description 1
- 241000228197 Aspergillus flavus Species 0.000 description 1
- 241000228245 Aspergillus niger Species 0.000 description 1
- 241000194103 Bacillus pumilus Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000223679 Beauveria Species 0.000 description 1
- 108010031797 Candida antarctica lipase B Proteins 0.000 description 1
- 108010089254 Cholesterol oxidase Proteins 0.000 description 1
- 241000222511 Coprinus Species 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 108010083608 Durazym Proteins 0.000 description 1
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 1
- BRLQWZUYTZBJKN-UHFFFAOYSA-N Epichlorohydrin Chemical compound ClCC1CO1 BRLQWZUYTZBJKN-UHFFFAOYSA-N 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 241000223221 Fusarium oxysporum Species 0.000 description 1
- 241000221779 Fusarium sambucinum Species 0.000 description 1
- 241000427940 Fusarium solani Species 0.000 description 1
- 108010015133 Galactose oxidase Proteins 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 101001091385 Homo sapiens Kallikrein-6 Proteins 0.000 description 1
- 241001480714 Humicola insolens Species 0.000 description 1
- 241001148466 Janthinobacterium lividum Species 0.000 description 1
- 102100034866 Kallikrein-6 Human genes 0.000 description 1
- 241000144128 Lichtheimia corymbifera Species 0.000 description 1
- 101710084385 Lipase 8 Proteins 0.000 description 1
- 241000223201 Metarhizium Species 0.000 description 1
- 241001661345 Moesziomyces antarcticus Species 0.000 description 1
- 241000203622 Nocardiopsis Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241001236817 Paecilomyces <Clavicipitaceae> Species 0.000 description 1
- 241001507662 Penicillium crustosum Species 0.000 description 1
- 241000235648 Pichia Species 0.000 description 1
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 1
- 241000168225 Pseudomonas alcaligenes Species 0.000 description 1
- 241000589755 Pseudomonas mendocina Species 0.000 description 1
- 241000589630 Pseudomonas pseudoalcaligenes Species 0.000 description 1
- 241000589776 Pseudomonas putida Species 0.000 description 1
- 241000589614 Pseudomonas stutzeri Species 0.000 description 1
- 241000577556 Pseudomonas wisconsinensis Species 0.000 description 1
- 241000235403 Rhizomucor miehei Species 0.000 description 1
- 241000593344 Rhizopus microsporus Species 0.000 description 1
- 240000005384 Rhizopus oryzae Species 0.000 description 1
- 241000223253 Rhodotorula glutinis Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 241000222068 Sporobolomyces <Sporidiobolaceae> Species 0.000 description 1
- 241000122973 Stenotrophomonas maltophilia Species 0.000 description 1
- 108010056079 Subtilisins Proteins 0.000 description 1
- 102000005158 Subtilisins Human genes 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 241000223257 Thermomyces Species 0.000 description 1
- 241000222354 Trametes Species 0.000 description 1
- 241000223260 Trichoderma harzianum Species 0.000 description 1
- 108010092464 Urate Oxidase Proteins 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 229920006322 acrylamide copolymer Polymers 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- KTYVHLCLTPLSGC-UHFFFAOYSA-N amino propanoate Chemical class CCC(=O)ON KTYVHLCLTPLSGC-UHFFFAOYSA-N 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical class N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 239000002280 amphoteric surfactant Substances 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 229920001400 block copolymer Polymers 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 239000011111 cardboard Substances 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 229920006317 cationic polymer Polymers 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000013068 control sample Substances 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- GQOKIYDTHHZSCJ-UHFFFAOYSA-M dimethyl-bis(prop-2-enyl)azanium;chloride Chemical compound [Cl-].C=CC[N+](C)(C)CC=C GQOKIYDTHHZSCJ-UHFFFAOYSA-M 0.000 description 1
- 229910001882 dioxygen Inorganic materials 0.000 description 1
- 238000004945 emulsification Methods 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 238000006735 epoxidation reaction Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-M hydroxide Chemical compound [OH-] XLYOFNOQVPJJNP-UHFFFAOYSA-M 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 108010009355 microbial metalloproteinases Proteins 0.000 description 1
- 108010020132 microbial serine proteinases Proteins 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 150000004965 peroxy acids Chemical class 0.000 description 1
- 125000000864 peroxy group Chemical group O(O*)* 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 125000002572 propoxy group Chemical group [*]OC([H])([H])C(C([H])([H])[H])([H])[H] 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000004076 pulp bleaching Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- GRVFOGOEDUUMBP-UHFFFAOYSA-N sodium sulfide (anhydrous) Chemical compound [Na+].[Na+].[S-2] GRVFOGOEDUUMBP-UHFFFAOYSA-N 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 125000000547 substituted alkyl group Chemical group 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 0.000 description 1
- 125000005457 triglyceride group Chemical group 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 229940005267 urate oxidase Drugs 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000002351 wastewater Substances 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
- 239000002888 zwitterionic surfactant Substances 0.000 description 1
Classifications
-
- D—TEXTILES; PAPER
- D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
- D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
- 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
- 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
Definitions
- the present invention relates to enzymatic compositions and methods for treating pitch problems in chemical pulp
- Wood contains about 1 to 10% of pitcn or extractives in addition to its main components cellulose, hemicull ⁇ se and lignin.
- Major components of pitch are fatty acids, triglycerdies, sterols, steryi esters and resirs adds, such as, for example, abietic acid.
- Pitch causes problems in paper machines by sticking to the rollers and causing spots or holes in the paper material.
- WO 00/53843 discloses steryl esterase enzyme preparations and their use in the manufacture of paper to hydroiyze the steryi ester part of pitch.
- U.S. Pat Ho. 6,066.486 discloses an enzyme preparation comprising a cholesteroi esterase derived from Pseudomo ⁇ as fragi > and its use to hydrolyze pulp resin.
- JP 2000080581 discloses the use of certain peroxidases for the decomposition of abietic acid during pulping or paper making processes.
- the present invention relates to compositions and methods for treating pitch problems in chemical pulp by treating chemical pulp process water with a combination of a lipase and a peroxide source.
- a lipase and peroxide leads to the formation of perac ⁇ ds which in turn oxidize unsaturated fatty acids and resin acids through an expoxidation reaction.
- the resuiting products are hydrophiiic and are readily washed from the pulp, thereby reducing pitch problems associated with chemical pulp.
- the present invention relates to compositions and methods for treating pitch problems in chemical pulp by treating chemical pulp process water with a lipase, a peroxide source and an organic add.
- a "paper-making process” refers to a process wherein a chemical pulp is suspended in water, mixed wrth various additives and then passed to equipment for further processing, e.g., in which frte paper, cardboard, tissue, towel etc. is formed, pressed and dried.
- paper material refers to products which can be made out of pulp, such as pa- per, lirserboard, corrugated paperboard , tissue, towels, corrugated containers or boxes.
- a papermaksng pulp or “pulp” means any chemical pulp which can be used for the production of a paper materia).
- a “chemical pulp” refers to chemical pulp (such as Kraft pulp or sulfite pulp) or seroichemical pulp (SCP).
- Chemicai pulp is usually manufactured by alkaline cooking whereby most of the lignin and some hem ⁇ cellulo ⁇ e components are removed.
- Jn Kraft pulpmg or sulphate cooking, sodium sulphide or s ⁇ drum hydroxide are generally used as principal cooking Chemicals.
- Jn such pulp as a result of the alkaline cooking, the triglyceride part of pitch wfll be hydrolyzed ⁇ nto fatty acids and glycerol.
- the chemical pulp is a Kraft pulp or a sulfite pulp
- the Kraft pulp is bleached Kraft pulp, for example softwood bleached Kraft (SWBK. also called NSKP (Nadef Note Bleached Kraft PuIp)), hardwood bleached Kraft (HWBK, also called LBKP (Laub HoIz Bleached Kraft Pulp and)) or a mixture thereof.
- SWBK softwood bleached Kraft
- HWBK also called LBKP (Laub HoIz Bleached Kraft Pulp and)
- the Kraft pulp to be tmaie ⁇ may be a bleached Kraft pulp, which may consist of softwood bleached Kraft (SWBK 1 also called NBKP (Nadel HoIz Bleached Kraft PuIp)), hardwood bleached Kraft (HWSK, also called LBKP (Laub HoIz Bleached Kraft Pulp and)) or a mixture of these softwood bleached Kraft (SWBK 1 also called NBKP (Nadel HoIz Bleached Kraft PuIp)), hardwood bleached Kraft (HWSK, also called LBKP (Laub HoIz Bleached Kraft Pulp and)) or a mixture of these softwood bleached Kraft (SWBK 1 also called NBKP (Nadel HoIz Bleached Kraft PuIp)), hardwood bleached Kraft (HWSK, also called LBKP (Laub HoIz Bleached Kraft Pulp and)) or a mixture of these softwood bleached Kraft (SWBK 1 also called NBKP (Nadel
- the pulp to be used in the process of the invention is a suspension of chemical pulp.
- the pulp to be used in the process of the invention may comprise at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least S0%, at least 90%, at least 95%, or 100% of chemical pulp (such as Kraft pulp or sulfite pulp),
- chemical pulp such as Kraft pulp or sulfite pulp
- the percentage of chemical pulp lies within the range of 1 -100%. in particular embodiments, the percentage of chemical pulp (such as Kraft pulp or s ⁇ ime pulp) lies within the range of 1-99%, 2-98%, 3-97%, 4-96%, 5-85%, 8- 94%, 7-93%. 8-92%. 9-91%, 10-90%, 15-85%, 20-80%, 25-75%, 30-70%, 40-60%, or 45-55%.
- chemical pulp process water is treated with a combination of a lipase and a peroxide source.
- Such chemical pulp process water contains pitch causing components, such as, fatty acids, triglycerdies.. sterols, steryl esters and/or resin acids (for example, abietic acid).
- the process of the invention is particularly applicable to the reduction of compounds constituting the pitch during a pulping or paper-making process, e.g. to avoid pitch troubles.
- Lipases include the enzymes classified by EC 3.1.1 ,3, Ref- erence is made to the Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, Academic Press Inc., 1992
- the lipase is preferably of microbial ori- gin, in particular of bacterial, fungal or yeast origin
- the iipase may be derived from any source, in- cluding, for example, a strain of Absidia, in particular Absidia blakesleena and Absidia corymbifera, a strain of Achromobacter, in particular Achromobacter iophagus, a strain of Aeromonas, a strain of Altemaria, in particular Altemaria brassiciola, a strain of Aspergillus, in particular Aspergillus niger and Aspergillus flavus, a strain of Achromobrcter, in particular Achromobacter iophagus, a strain of Aureobasidium, in particular Aureobasidium p ⁇ llulans, a strain of Bacillus, in particular Bacillus pumilus, Bacillus sttearothermophilus and Bacillus subtilis,
- a strain of HumiGola. in particular Humicola brevispora. Humicola brevls var. thermoidea, and Humicola insofens a strain of Hyphozyma, a strain of Lactobacillus, in particular Lactobacillus curvat ⁇ s, a strain of Metarhizium, a strain M ⁇ cor, a strain of Paecilomyces, a strain of Penscilttum.
- Penic ⁇ llium cydopium Penicillium crustosum and Penidliium ex- pansum
- Pseudomonas in particular Pseudomonas aeruginosa, Pseudomonas afc&li- genes, Pseudomonas Gapa ⁇ a (syrt. Burkboldeiia cepacia), Pseudomonas ft ⁇ orescens, Pseudomo- nas tragi.
- Pseudomonas maltophilia Pseudomonas mendocina, Pseudomonas mephitica lipolyfica, Pseudomonas alcaligenes, Pseudomonas plantari. Pseudomonas pseudoalcaligenes.
- Rhizoctonia in particu- lar Rhizoctonia soiani
- Rhlzomucor in particular Rhizomucor miehei
- Rhizopus in particular Rhizopus japonicus
- Rhizopus microsporus Rhizopus nodosus
- Rhodosporidium in particular Rhodosporidlum tor ⁇ loides
- Rhodotorula in particular Rhodotorula glutinis
- Sporobolomyces in particular Sporobobmyces shibatanus
- Themomyces in particular Viermomyces lanuglnosus (formerly Humicoia lanuginosa)
- Thiamsporella in particular Thiarosporeil
- the lipase is derived from a strain of Aspergillus, a strain of Achromohacter, a strain of Bacillus, a strain of Candida, a strain of Chromobacter, a strain of Fusa- rium, a strain of Humicola, a strain of Hyphozyma, a strain of Pse ⁇ domonas, a strain of Rhizomucor, 3 strain of Rhizopus, or a strain of Thermomyces.
- Preferred lipases indude the upases described in U.S. Patent No, 6,074.863 and WO
- Preferred commercial lipases include Resinase A2X and Resinase HT (Novozymes A/S).
- the lipase is the Candida antarctioa lipase A (CALA) or the Candida antarctica lipase 8 (CALB) (available from Novozymes A/S)
- a "peroxide source” or “hydrogen peroxide source” refers to hydrogen per- oxide itseif or components which can generate peroxide.
- the hydrogen peroxide source may be added at the beginning or during the lipase treatment process, e.g., at a concentration of about 0.001-100 mM, particularly 0,01-50 mM.
- One source of hydrogen peroxide includes precursors of hydrogen peroxide, such as, e.g., a perborate or a percarbonate.
- Another source of hydrogen peroxide includes enzymes which are able to convert molecular oxygen and an organic or inor- ganic substrate into hydrogen peroxide and the oxidized substrate, respectively.
- enzymes which are capable of produc- ing hydrogen peroxide include, but are not limited to, glucose oxidase, urate oxidase, galactose oxidase, alcohol oxidase, amine oxidase, amino acid oxidase and cholesterol oxidase.
- Organic acid ⁇ s may aiso be added to the pulp, e.g., to enhance the pitch treatment.
- Or- ganic acids refer to any organic substance which contains at least one acidic group. Examples of organic acids are acetic acid, butyric acid, and linoieic acid. The concentration of organic acid is preferably between 0.001-500 mM.
- 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 promisp storing container (storage chest), storage tower, mixing chest or metering chest.
- the enzyme treatment is preferably applied before or after pulp bleach process or in between the pulp bleaching stages.
- the enzyme can be added to the circulated process water (white water) originating from bleaching. In a particular embodiment of a Kraft pulping process, the enzyme is added during the brown-stock washing.
- process water can include water added as a raw material to the paper manufacturing process; intermediate water products resulting from any step of the process for manufacturing the paper material: as well as waste water as an output or by-product of the process,
- the process water is, has keen, is being, or is intended for being circulated or 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, in a particular embodiment the process water has a low content of solid (dry) matter, e.g,, below 20%, 18%, 16% : 14%, 12%, 10%, 8%, 7%, 6%, S%, 4%, 3%. 20% or below 1% dry matter.
- dry matter e.g, below 20%, 18%, 16% : 14%, 12%, 10%, 8%, 7%, 6%, S%, 4%, 3%. 20% or below 1% dry matter.
- the process of t ⁇ e invention may be carried out at conventional conditions in the paper and puSp processing.
- the process conditions wiii be a function of the enzyrne(s) applied, the reaction time and the conditions given.
- the enzyme m ⁇ peroxide should be added sn an effective amount.
- effective amount is meant the amount sufficient to achieve the desired effect of reducing or inhibiting pitch components, such as, by degrading or converting such components into a form which can be more readily removed from the pulp or pulp process water.
- the dosage of the lipase enzyme Is from about 0,1 mg enzyme protein to about 100.000 mg enzyme protein (of each enzyme) per ton of paper pulp.
- the enzymatic treatment can be done at consistency, e.g. t 0,5-10 % dry substance, in particular embodiments, the consistency is within the range of 0.5-45; 0.540; 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
- the temperature may be from about 20 to 9G 15 C, or 20 to 95 0 C. preferably from about 40 to 7O 0 C 1 or 40 to 75°C.
- the enzymatic treatment may be carried out at a pH of from about 2 to about 12. Further examples of pH ranges (all "from about” and “to about”) are the following: 3-12, 4-12, 5-12, 6-12, 1-
- the pH range may be from about 2 to 11 , preferably within the range from about 3- ⁇ .
- 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 16 hours, or from about 1 minute to about 12 hours, or from Bboui 1 minute to S 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.
- the reaction time may be from about 10 minutes to 3 hours, 10 minutes to 10 hours, preferably 15 minutes to 1 hour, or 15 minutes to 2 hours,
- Surfactants and/or dispersants are often present in, and/or added to a papermaking p ⁇ ip.
- the process and use of the present invention may be carried out in the presence of an anionic, non-ionic, cationic and/or zwilterionic surfactant and/or dispersant conventionally used m a papermaking pulp.
- anionic surfactants are carboxyiates, sulphates, suiphonates or phosphates of alkyl, substituted alkyl or aryl.
- Fatty acids are examples of alkykarboxyiates.
- non-ionic surfactants are poiyoxyethyiene compounds, such as alcohol ethoxyiates, propoxylates or mixed ethoxy-/propoxy Sates, poly-giyeerois and other polyols, as well as certain block-copolymers.
- cafionic surfactants are wafer-soluble cationic polymers, such as quartenary ammonium sulphates and certain amines, e.g.
- epichlorohydrin/dimethylamine polymers EPI-DMA
- cross-linked solutions thereof polydiallyl dimethyl ammonium chioride (DADMAO), DADMAC/Acrylamide co-polymers, and ionene polymers, such as those disclosed in US patents nos. 5,681,862; and 5,575.993.
- DADMAO polydiallyl dimethyl ammonium chioride
- DADMAC/Acrylamide co-polymers such as those disclosed in US patents nos. 5,681,862; and 5,575.993.
- Examples of zwitterionic or amphoteric surfactants are Detains, glycinaies, amino propionates, imino propionates and various imidazolin-derivatives.
- 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.
- the amount of each surfactant in such composition may amount io from about 8 to about 40% (w/w) of the composition, in particular embodiments 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 23 to about 32% ⁇ w/w ⁇ -
- enzyme encompass wild-type enzymes, as well as any variant thereof that re- tains 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 purifica- tion 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 weii-deftned, 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.
- 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 lipase and peroxide source, in particular embodiments the additional enzyme is an enzyme which has protease, xy- larsase, cutinase, oxidoreductase, cellulase, endogiucanase, amylase, mannartase, steryl es- terase, and/or cholesterol esterase activity.
- oxidoreductase enzymes are enzymes with Iaccase, and/or peroxidase activity.
- 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 lipase and peroxide source 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 lipase an ⁇ peroxide source is used.
- enzyme preparation means a product containing at ieast one lipase enzyme.
- 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, xylanase, cutinase, oxidoreductase, cellulase endogiuca- nase, amylase, mannanase, steryl esterase, and/or cholesterol esterase activity can be used as additional enzymes in the use and process of the invention. Selow some non ⁇ iimiting examples are listed of sued 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 en- zyme in question, including the methods mentioned in the references cited.
- cutinases are those derived from Humicola insolens (US 5,627,71 S); from a strain of FuSBnUm 1 e.g. F. roseum cutmorum, or particularly F. s ⁇ lani pisi (WO 80/09446; WO 94/14964, WO 94/03578).
- the cutinase may also be derived from a strain of Fthizoctonia, e.g. R. sol ⁇ nh or a strain of Attemaria, e.g. A, hrassicicola (WO 94/03578), or variants thereof such as those described in WO 00/34450, or WO 01/92502,
- proteases are the ALCALASE, ESPERASE, SAVINASE, NEUTRASE and DURAZYM proteases.
- Other proteases are derived from Nocardiopsis, Aspergillus, Rhlzopus, Ba- citkis afcafophiius, B. oereus, B. natto, B, vulgatus, B. myoolde, and subtHisins from Bacillus, es- pecially proteases from the species Nooardiopsis sp, and Nocar ⁇ ' opsis dessertvillei such as those disclosed in WO 88/03947, and mutants thereof, e.g. those disclosed in WO 91/00345 and SP 415286.
- amylases are the BAN, AQUAZYM, TERMAiVIYL, and AQUAZYM Ultra amy- fases.
- Art example of a xyianase is the PULPZYME HC hemscelluiase.
- Examples of endogluca- nases are the NOVOZYM 613, 342, and 476 enzyme products.
- mannanases examples include the Tnchoderma reesei endo-foeta-mannanases described in St ⁇ hlbrand et ai. J. Biotechnoi. 29 (1893), 229-242.
- steryl esterases examples include steryl esterases, peroxidases, laccases, and cholesterol esterases.
- oxi- doreducfases are the peroxidases and laccases disclosed In EP 730641; WO 01/98469; EF 719337; EP 765394; EP 767 ⁇ 3Q; EP 763115; and EP 7S8547, in the present context, whenever an oxtdoreductase enzyme is mentioned that requires or benefits from the presence of acceptors, enhancers., mediators and/or activators, such compounds should foe considered to be included if not already present Examples of enhancers and mediators are disclosed in EP 705327; WQ 98/56899; EP 677102; SP 7S1326: and EP 707637.
- an ⁇ xidoreductase enzyme system ⁇ e.g. a laccase, or a peroxidase enzyme system
- an ⁇ xidoreductase enzyme system ⁇ e.g. a laccase, or a peroxidase enzyme system
- an enhancer and/or mediator for the enzyme in question ⁇ its acceptor, and optionally also an enhancer and/or mediator for the enzyme in question.
- a process for reducing deposition of pitch in t ⁇ e paper making process wherein the process comprises treating the pulp and/or process water with a lipase, a peroxide source and organic acid.
- Dammar resin was obtained from Fluka and used as a model pitch to simulate Kraft pulp pitch.
- TAED was also obtained from Fluka. Put 75 mg of Dammar resin in a flask and add 75 mL of Dl water. Add chemicals or enzymes according to the conditions shown in Table 1. Stir at ambient temperature overnight. Turbidity of the solutions was determined by UV-vis at 600 nm.
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Abstract
Description
Claims
Priority Applications (7)
Application Number | Priority Date | Filing Date | Title |
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JP2008554548A JP2009526919A (en) | 2006-02-14 | 2007-02-14 | Chemical pulp treatment composition and method |
EP07717616A EP1994219A1 (en) | 2006-02-14 | 2007-02-14 | Chemical pulp treatment compositions and methods |
CA002637691A CA2637691A1 (en) | 2006-02-14 | 2007-02-14 | Chemical pulp treatment compositions and methods |
BRPI0707656-8A BRPI0707656A2 (en) | 2006-02-14 | 2007-02-14 | Method for reducing pitch problems in a chemical pulp, and, use of a lipase and peroxide source |
AU2007214449A AU2007214449A1 (en) | 2006-02-14 | 2007-02-14 | Chemical pulp treatment compositions and methods |
US12/160,898 US20090065159A1 (en) | 2006-02-14 | 2007-02-14 | Chemical pulp treatment compositions and methods |
NO20083436A NO20083436L (en) | 2006-02-14 | 2008-08-05 | Chemical pulp treatment, composition and methods |
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US77324206P | 2006-02-14 | 2006-02-14 | |
US60/773,242 | 2006-02-14 |
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PCT/US2007/062136 WO2007095575A1 (en) | 2006-02-14 | 2007-02-14 | Chemical pulp treatment compositions and methods |
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US (1) | US20090065159A1 (en) |
EP (1) | EP1994219A1 (en) |
JP (1) | JP2009526919A (en) |
CN (1) | CN101384769A (en) |
AU (1) | AU2007214449A1 (en) |
BR (1) | BRPI0707656A2 (en) |
CA (1) | CA2637691A1 (en) |
NO (1) | NO20083436L (en) |
WO (1) | WO2007095575A1 (en) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US7951267B2 (en) * | 2001-05-21 | 2011-05-31 | Kim Borch | Enzymatic hydrolysis of a polymer comprising vinyl acetate monomer |
EP2534254A1 (en) * | 2010-02-08 | 2012-12-19 | Iogen Energy Corporation | Method for scale removal during a lignocellulosic conversion process |
CN103998680A (en) * | 2011-10-27 | 2014-08-20 | 巴科曼实验室国际公司 | Method and composition for enzymatic treatment of fiber for papermaking, and paper products made therewith |
Families Citing this family (8)
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PT1880053T (en) * | 2005-05-04 | 2019-11-04 | Novozymes As | Chlorine dioxide treatment compositions and processes |
PT2580388T (en) * | 2010-06-08 | 2018-02-21 | Buckman Laboratories Int Inc | Methods to degrade sludge from pulp and paper manufacturing |
BR112014031811A2 (en) | 2012-06-22 | 2017-06-27 | Buckman Laboratories Int Inc | method for controlling deposition of organic fiber contaminants in papermaking and papermaking systems |
CN103243601A (en) * | 2013-04-27 | 2013-08-14 | 陕西科技大学 | Method for treating masson pine thermo-mechanical pulp resin by using combination of lipase, NaOH and talc powder |
CN104088184B (en) * | 2014-06-26 | 2017-01-11 | 孔慧 | Pulp washing auxiliary agent and pulping process |
CN109610217A (en) * | 2016-10-19 | 2019-04-12 | 瑞辰星生物技术(广州)有限公司 | The composition of organic pollutant deposition is controlled in pulping and paper-making production |
CN106480771B (en) * | 2016-12-23 | 2018-12-04 | 江南大学 | A method of utilizing cutin enzymatic treatment mthod of white water from paper making |
CN109722422A (en) * | 2018-12-31 | 2019-05-07 | 苏州埃斯腾特生物科技有限公司 | High temperature resistant lipase and application thereof |
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US3486969A (en) * | 1965-07-20 | 1969-12-30 | Mo Och Domsjoe Ab | Process for the treating of wood chips with fungi to enhance enzymatic hydrolysis of the resinous components |
US5256252A (en) * | 1992-07-15 | 1993-10-26 | Nalco Chemical Company | Method for controlling pitch deposits using lipase and cationic polymer |
US5356517A (en) * | 1989-11-08 | 1994-10-18 | Novo Nordisk A/S | Hydrolysis of resin in pulp with an enzyme and a peroxide |
JP2000080581A (en) * | 1998-09-02 | 2000-03-21 | Nippon Paper Industries Co Ltd | Pitch trouble prevention with enzyme |
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 |
US20030124710A1 (en) * | 2001-10-23 | 2003-07-03 | Novozymes A/S | Oxidizing enzymes in the manufacture of paper materials |
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DK39593D0 (en) * | 1993-04-02 | 1993-04-02 | Novo Nordisk As | ENZYME |
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2007
- 2007-02-14 EP EP07717616A patent/EP1994219A1/en not_active Withdrawn
- 2007-02-14 CA CA002637691A patent/CA2637691A1/en not_active Abandoned
- 2007-02-14 WO PCT/US2007/062136 patent/WO2007095575A1/en active Application Filing
- 2007-02-14 BR BRPI0707656-8A patent/BRPI0707656A2/en not_active Application Discontinuation
- 2007-02-14 AU AU2007214449A patent/AU2007214449A1/en not_active Abandoned
- 2007-02-14 CN CNA2007800054194A patent/CN101384769A/en active Pending
- 2007-02-14 JP JP2008554548A patent/JP2009526919A/en active Pending
- 2007-02-14 US US12/160,898 patent/US20090065159A1/en not_active Abandoned
-
2008
- 2008-08-05 NO NO20083436A patent/NO20083436L/en not_active Application Discontinuation
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US3486969A (en) * | 1965-07-20 | 1969-12-30 | Mo Och Domsjoe Ab | Process for the treating of wood chips with fungi to enhance enzymatic hydrolysis of the resinous components |
US5356517A (en) * | 1989-11-08 | 1994-10-18 | Novo Nordisk A/S | Hydrolysis of resin in pulp with an enzyme and a peroxide |
US5256252A (en) * | 1992-07-15 | 1993-10-26 | Nalco Chemical Company | Method for controlling pitch deposits using lipase and cationic polymer |
JP2000080581A (en) * | 1998-09-02 | 2000-03-21 | Nippon Paper Industries Co Ltd | Pitch trouble prevention with enzyme |
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 |
US20030124710A1 (en) * | 2001-10-23 | 2003-07-03 | Novozymes A/S | Oxidizing enzymes in the manufacture of paper materials |
Cited By (5)
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US7951267B2 (en) * | 2001-05-21 | 2011-05-31 | Kim Borch | Enzymatic hydrolysis of a polymer comprising vinyl acetate monomer |
EP2534254A1 (en) * | 2010-02-08 | 2012-12-19 | Iogen Energy Corporation | Method for scale removal during a lignocellulosic conversion process |
EP2534254A4 (en) * | 2010-02-08 | 2014-01-22 | Iogen Energy Corp | Method for scale removal during a lignocellulosic conversion process |
US8882925B2 (en) | 2010-02-08 | 2014-11-11 | Iogen Energy Corporation | Method for scale removal during a lignocellulosic conversion process |
CN103998680A (en) * | 2011-10-27 | 2014-08-20 | 巴科曼实验室国际公司 | Method and composition for enzymatic treatment of fiber for papermaking, and paper products made therewith |
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BRPI0707656A2 (en) | 2011-05-10 |
EP1994219A1 (en) | 2008-11-26 |
JP2009526919A (en) | 2009-07-23 |
US20090065159A1 (en) | 2009-03-12 |
AU2007214449A1 (en) | 2007-08-23 |
CN101384769A (en) | 2009-03-11 |
NO20083436L (en) | 2008-08-26 |
CA2637691A1 (en) | 2007-08-23 |
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