AU2007214449A1 - Chemical pulp treatment compositions and methods - Google Patents
Chemical pulp treatment compositions and methods Download PDFInfo
- Publication number
- AU2007214449A1 AU2007214449A1 AU2007214449A AU2007214449A AU2007214449A1 AU 2007214449 A1 AU2007214449 A1 AU 2007214449A1 AU 2007214449 A AU2007214449 A AU 2007214449A AU 2007214449 A AU2007214449 A AU 2007214449A AU 2007214449 A1 AU2007214449 A1 AU 2007214449A1
- Authority
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- Australia
- Prior art keywords
- strain
- pulp
- lipase
- chemical pulp
- peroxide
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 238000000034 method Methods 0.000 title claims description 72
- 229920001131 Pulp (paper) Polymers 0.000 title claims description 27
- 239000000203 mixture Substances 0.000 title description 9
- 102000004190 Enzymes Human genes 0.000 claims description 44
- 108090000790 Enzymes Proteins 0.000 claims description 44
- 108090001060 Lipase Proteins 0.000 claims description 35
- 102000004882 Lipase Human genes 0.000 claims description 34
- 239000004367 Lipase Substances 0.000 claims description 33
- 235000019421 lipase Nutrition 0.000 claims description 33
- 150000002978 peroxides Chemical class 0.000 claims description 30
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical group OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims description 24
- 239000002655 kraft paper Substances 0.000 claims description 23
- 239000000123 paper Substances 0.000 claims description 22
- 108010031797 Candida antarctica lipase B Proteins 0.000 claims description 7
- 241000235527 Rhizopus Species 0.000 claims description 6
- 150000007524 organic acids Chemical class 0.000 claims description 6
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 5
- 241000222120 Candida <Saccharomycetales> Species 0.000 claims description 5
- 241000223198 Humicola Species 0.000 claims description 5
- 241000589516 Pseudomonas Species 0.000 claims description 4
- 241000235402 Rhizomucor Species 0.000 claims description 4
- LSNNMFCWUKXFEE-UHFFFAOYSA-N Sulfurous acid Chemical compound OS(O)=O LSNNMFCWUKXFEE-UHFFFAOYSA-N 0.000 claims description 4
- 241000228212 Aspergillus Species 0.000 claims description 3
- 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
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 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
- 229910001882 dioxygen Inorganic materials 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
- 229960003903 oxygen Drugs 0.000 claims 1
- 230000008569 process Effects 0.000 description 47
- 229940088598 enzyme Drugs 0.000 description 41
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 18
- 239000011347 resin Chemical class 0.000 description 10
- 229920005989 resin Chemical class 0.000 description 10
- -1 triglycerdies Chemical class 0.000 description 10
- 239000000126 substance Substances 0.000 description 9
- 108090000854 Oxidoreductases Proteins 0.000 description 8
- 102000004316 Oxidoreductases Human genes 0.000 description 8
- 238000004519 manufacturing process Methods 0.000 description 8
- 108010029541 Laccase Proteins 0.000 description 7
- 239000002253 acid Substances 0.000 description 7
- 230000002255 enzymatic effect Effects 0.000 description 7
- 150000007513 acids Chemical class 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 239000004094 surface-active agent Substances 0.000 description 6
- 102100035687 Bile salt-activated lipase Human genes 0.000 description 5
- 108091005804 Peptidases Proteins 0.000 description 5
- 102000003992 Peroxidases Human genes 0.000 description 5
- 239000004365 Protease Substances 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
- 239000000463 material Substances 0.000 description 5
- 241000590020 Achromobacter Species 0.000 description 4
- 108010055297 Sterol Esterase Proteins 0.000 description 4
- 238000010411 cooking Methods 0.000 description 4
- 230000008021 deposition Effects 0.000 description 4
- 150000004665 fatty acids Chemical class 0.000 description 4
- 229920000642 polymer Polymers 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 238000004537 pulping 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
- 240000000972 Agathis dammara Species 0.000 description 3
- 108010065511 Amylases Proteins 0.000 description 3
- 102000013142 Amylases Human genes 0.000 description 3
- 102100032487 Beta-mannosidase Human genes 0.000 description 3
- 108010059892 Cellulase Proteins 0.000 description 3
- 229920002871 Dammar gum Polymers 0.000 description 3
- 108090000371 Esterases Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108700020962 Peroxidase Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 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 3
- 239000000654 additive Substances 0.000 description 3
- 239000002671 adjuvant Substances 0.000 description 3
- 235000019418 amylase Nutrition 0.000 description 3
- 108010055059 beta-Mannosidase Proteins 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 108010005400 cutinase Proteins 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 150000002148 esters Chemical class 0.000 description 3
- 239000000523 sample Substances 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
- 241000235389 Absidia Species 0.000 description 2
- 239000004382 Amylase Substances 0.000 description 2
- 241000223651 Aureobasidium Species 0.000 description 2
- 241000589513 Burkholderia cepacia Species 0.000 description 2
- FERIUCNNQQJTOY-UHFFFAOYSA-N Butyric acid Chemical compound CCCC(O)=O FERIUCNNQQJTOY-UHFFFAOYSA-N 0.000 description 2
- ROSDSFDQCJNGOL-UHFFFAOYSA-N Dimethylamine Chemical compound CNC ROSDSFDQCJNGOL-UHFFFAOYSA-N 0.000 description 2
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 2
- 244000286779 Hansenula anomala Species 0.000 description 2
- 101001091385 Homo sapiens Kallikrein-6 Proteins 0.000 description 2
- 241001480714 Humicola insolens Species 0.000 description 2
- 102100034866 Kallikrein-6 Human genes 0.000 description 2
- 241001661345 Moesziomyces antarcticus Species 0.000 description 2
- 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
- 241000813090 Rhizoctonia solani Species 0.000 description 2
- 229930182558 Sterol Natural products 0.000 description 2
- 108010056079 Subtilisins Proteins 0.000 description 2
- 102000005158 Subtilisins Human genes 0.000 description 2
- 241000223258 Thermomyces lanuginosus Species 0.000 description 2
- 239000000370 acceptor Substances 0.000 description 2
- 239000012190 activator Substances 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000007844 bleaching agent Substances 0.000 description 2
- 229940079919 digestives enzyme preparation Drugs 0.000 description 2
- 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 2
- 239000002270 dispersing agent Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000011121 hardwood Substances 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
- 150000004965 peroxy acids Chemical class 0.000 description 2
- 230000035484 reaction time Effects 0.000 description 2
- 238000010188 recombinant method Methods 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
- 235000021122 unsaturated fatty acids Nutrition 0.000 description 2
- 150000004670 unsaturated fatty acids Chemical class 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
- 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 1
- 108010025188 Alcohol oxidase Proteins 0.000 description 1
- 241000228245 Aspergillus niger Species 0.000 description 1
- 241000194106 Bacillus mycoides Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 241000223679 Beauveria Species 0.000 description 1
- 108010089254 Cholesterol oxidase Proteins 0.000 description 1
- 241000511343 Chondrostoma nasus Species 0.000 description 1
- 241000222511 Coprinus Species 0.000 description 1
- 241000222175 Diutina rugosa Species 0.000 description 1
- 108010083608 Durazym 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
- 241000223218 Fusarium Species 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
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 235000014683 Hansenula anomala Nutrition 0.000 description 1
- 229920002488 Hemicellulose Polymers 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 241001148466 Janthinobacterium lividum Species 0.000 description 1
- 241000144128 Lichtheimia corymbifera Species 0.000 description 1
- OYHQOLUKZRVURQ-HZJYTTRNSA-N Linoleic acid Chemical compound CCCCC\C=C/C\C=C/CCCCCCCC(O)=O OYHQOLUKZRVURQ-HZJYTTRNSA-N 0.000 description 1
- 101710084385 Lipase 8 Proteins 0.000 description 1
- 239000006091 Macor Substances 0.000 description 1
- 241000203622 Nocardiopsis Species 0.000 description 1
- 241001221335 Nocardiopsis sp. Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 1
- 241000168225 Pseudomonas alcaligenes Species 0.000 description 1
- 241000589540 Pseudomonas fluorescens Species 0.000 description 1
- 241000589538 Pseudomonas fragi Species 0.000 description 1
- 241000589755 Pseudomonas mendocina Species 0.000 description 1
- 241000589776 Pseudomonas putida Species 0.000 description 1
- 241000577556 Pseudomonas wisconsinensis Species 0.000 description 1
- 241000593344 Rhizopus microsporus Species 0.000 description 1
- 241000223252 Rhodotorula Species 0.000 description 1
- 241000221523 Rhodotorula toruloides Species 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- UCKMPCXJQFINFW-UHFFFAOYSA-N Sulphide Chemical compound [S-2] UCKMPCXJQFINFW-UHFFFAOYSA-N 0.000 description 1
- 241000223257 Thermomyces Species 0.000 description 1
- 241000222354 Trametes Species 0.000 description 1
- 241000223259 Trichoderma 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
- 125000005599 alkyl carboxylate group Chemical group 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
- 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
- 150000007942 carboxylates Chemical class 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
- 239000003093 cationic surfactant Substances 0.000 description 1
- 229940106157 cellulase Drugs 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229940106135 cellulose Drugs 0.000 description 1
- 235000010980 cellulose Nutrition 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
- 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
- 150000002314 glycerols Chemical class 0.000 description 1
- 229940059442 hemicellulase Drugs 0.000 description 1
- 108010002430 hemicellulase Proteins 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 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
- OYHQOLUKZRVURQ-IXWMQOLASA-N linoleic acid Natural products CCCCC\C=C/C\C=C\CCCCCCCC(O)=O OYHQOLUKZRVURQ-IXWMQOLASA-N 0.000 description 1
- 235000020778 linoleic acid Nutrition 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
- 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
- 229920000371 poly(diallyldimethylammonium chloride) polymer Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 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
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000243 solution Substances 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
- 125000001273 sulfonato group Chemical group [O-]S(*)(=O)=O 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 0.000 description 1
- 108010075550 termamyl Proteins 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
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
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Paper (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Compositions Of Macromolecular Compounds (AREA)
- Enzymes And Modification Thereof (AREA)
Description
WO 2007/095575 PCT/US2007/062136 CHEMICAL PULP TREATMENT COMPOSITIONS AND METHODS FIELD OF THE INVENTION The present invention relates to enzymatic compositions and methods for treating pitch 5 problems in chemical pulp. BACKGROUND OF THE INVENTION Wood contains about 1 to 10% of pitch or extractives in addition to its main components cel lulose, hemicullose and lignin. Major components of pitch are fatty acids, triglycerdies, sterols, 10 steryl esters and resin acids, 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. Various enzymatic processes have been used to treat pitch problems. WO 00/53843 dis closes steryl esterase enzyme preparations and their use in the manufacture of paper to hydrolyze the steryl ester part of pitch. 15 U.S. Pat, No. 6,066,486 discloses an enzyme preparation comprising a cholesterol esterase derived from Pseudomionas 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. X, Zhang; Pulp & Paper Canada, 101:3 (2000), page 59-62, discloses studies of the ability 20 of laccase to remove dissolved and colloidal substances. Karlsson et al: Reactivity of Trametes laccases with fatty and resin acids; Appi. Microbiol. Biotechnol. (2001) 55:317-320 discloses experiments in which laccases were used to treat pitch. U.S. Patent application 20030124710 discloses a process for manufacturing a paper mate rial by treating a papermaking pulp process water with a fatty acid oxidizing enzyme. 25 U.S. Patent No, 5,356,517 discloses the use of lipases to hydrolyze tryglycerides during peroxy bleaching in the preparation of chemithermomechanical pulp, SUMMARY OF THE INVENTION The present invention relates to compositions and methods for treating pitch problems in 30 chemical pulp by treating chemical pulp process waterwith a combination of a lipase and a perox ide source. Although not limited to any one theory of operation, it is believed that the addition of a lipase and peroxide leads to the formation of peracids which in turn oxidize unsaturated fatty acids and resin acids through an expoxidation reaction. The resulting products are hydrophilic and are readily washed from the pulp, thereby reducing pitch problems associated with chemical pulp. 35 In another embodiment, the present invention relates to compositions and methods for
I
WO 2007/095575 PCT/US2007/062136 treating pitch problems in chemical pulp by treating chemical pulp process water with a lipase, a peroxide source and an organic acid. DETAILED DESCRIPTION OF THE INVENTION 5 A "paper-making process" refers to a process wherein a chemical pulp is suspended in wa ter, mixed with various additives and then passed to equipment for further processing, e.g, in which the paper, cardboard, tissue, towel etc. is formed, pressed and dried. The term "paper material" refers to products which can be made out of pulp, such as pa per, linerboard, corrugated paperboard, tissue, towels, corrugated containers or boxes. 10 The term "a papermaking pulp" or "pulp" means any chemical pulp which can be used for the production of a paper material, A "chemical pulp" refers to chemical pulp (such as Kraft pulp or suffite pulp) or semichemical pulp (SCP), Chemical pulp is usually manufactured by alkaline cooking whereby most of the lignin and some hemicellulose components are removed. In Kraft pulping or sulphate cooking, sodium 15 sulphide or sodium hydroxide are generally used as principal cooking chemicals. In such pulp, as a result of the alkaline cooking, the triglyceride part of pitch will be hydrolyzed into fatty acids and glycerol. In a particular embodiment of the use and the process of the invention, the chemical pulp is a Kraft pulp or a sulfite pulp, In particular embodiments, the Kralt pulp is bleached Kraft pulp, for 20 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 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 25 Kraft (HWBK, also called LBKP (Laub Holz Bleached Kraft Pulp and)) or a mixture of these 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 80%, at least 90%, at least 95%, or 100% of chemical pulp (such as Kraft pulp or sulfite pulp), The percentage of chemical 30 pulp lies within the range of 1-100%. In particular embodiments, the percentage of chemical pulp (such as Kraft pulp or sulfite pulp) ies within the range of 1-99%, 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%. In accordance with the present invention, chemical pulp process water is treated with a combination of a lipase and a peroxide source. Such chemical pulp process water contains pitch 35 causing components, such as, fatty acids, triglycerdies. sterols, steryl esters and/or resin acids (for 2 WO 2007/095575 PCT/US2007/062136 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. Any suitable lipase may be used. Lipases include the enzymes classified by EC 3.1.1.3, Ref 5 erence is made to the Recommendations (1992) of the Nomenclature Committee of the Intemational Union of Biochemistry and Molecular Biology, Academic Press Inc., 1992 In a preferred embodiment of the present invention, the lipase is preferably of microbial ori gin, in particular of bacterial, fungal or yeast origin, The lipase may be derived from any source, in cluding, for example, a strain of Absidia, in particular Absidia blakesteena and Absidia corymbifera, a 10 strain of Achromobacter, in particular Achromobacter /ophagus, a strain of Aemmonas, a strain of Atemaia, in particular Altemaria brassicioa, a strain of Aspergiluas, in particular Aspergillus niger and Aspergilus flavus, a strain of Achromobacter, in particular Achrtomobacter iophagus, a strain of Aureobasidium, in particular Aureobasidium pululans, a strain of Bacillus, in particular Bacillus purnius, Bacillus strearothermophilus and Bacillus subilis, a strain of Beauveria, a strain of Bro 15 chothrix, in particular Brochothr/x thermosohata, a strain of Candida, in particular Candidea cyl indracea (Candida rugosa), Candda paralpolytica, and Candida antarctica, a strain of ChromObac ter. in particular Chrornobacter viscosum, a strain of Coprinus, in particular Coprnus c/nerius, a strain of Fusariun, in particular Fusarium oxysporum, Fusarium solani, Fusarum solani pisi, and Fusar/um roseum culmorum, a strain of Geotricum, in particular Geotdcun penicillatum, a strain of Hansenua, 20 in particular Hansenula anomala. a strain of Humicola, in particular Humicola brevispora, Humicola brevis var. thermoidea, and Humicola insolens, a strain of Hyphozyma, a strain of Lactobacilus, in particular Lactobacilius curatus, a strain of Meteraiium, a strain of Macor, a strain of Paec//omyces, a strain of Penilc/ium, in particular Penicilium cyclopium, Penicil/um crustosum and Penicilium exa pansum, a strain of Pseudoornans in particular Pseudomonas aeruginosa, Pseudornonas alcai 25 genes, Pseudomonas cepacia (syn. Burkholderia cepacia), Pseudomonas fluorescens, Pseudomo nas fragi, Pseudon7onas matophilia, Pseudomonas mendocina, Pseudomonas mephitica lipolytica, Pseudomonas alcaligenes, Pseudononas plantar, Pseudomonas pseudoalcaigenes, Pseudomonas putida, Pseudomonas stutzed, and Pseudomonas wisconsinensis, a strain of Rhizoctonia, in particu lar Rhizoctonia solani, a strain of Rhizomucor, in particular Rhizomucor rniehel, a strain of Rhizopus, 30 in particular Rhizopus japoncus, Rhizopus microsporus and Rhizopus nodosus, a strain of Rhodosporidium, in particular Rhodosporidium toruloides, a strain of Rhodotorua, in particular Rhadotorula glut/ns, a strain of Sparobolomyces, in particular Sporoboomyces shibatanus, a strain of Thermonmyces, in particular Thermomyces lanuginosus (formerly Humicola lanuginosa). a strain of Thiarnsparella, in particular Thiarosporela phaseolina, a strain of Tdfchoderma, in particular Tricho 35 derma hrzianurn, and Trichoderma reesel, and/or a strain of Verticilium. 3 WO 2007/095575 PCT/US2007/062136 in a preferred embodiment, the lipase is derived from a strain of Aspergillus, a strain of Achromobacter, a strain of Bacillus, a strain of Candida, a strain of Chromobacter, a strain of Fusa Aium, a strain of Humicola, a strain of Hyphozyma, a strain of Pseudomonas, a strain of Rhizomucor, a strain of Rhizopus, or a strain of Thermomyces. 5 Preferred lipases include the lipases described in U,, Patent No, 6,074,863 and WO 02/055679, Preferred commercial lipases include Resinase A2X and Resinase HT (Novozymes AIS). In another preferred embodiment, the lipase is the Candida antarctica lipase A (CALA) or the Candida antarctica lipase B (CALB) (available from Novozymes A/S) As used herein, a "peroxide source" or "hydrogen peroxide source" refers to hydrogen per 10 oxide itself 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 15 ganic substrate into hydrogen peroxide and the oxidized substrate, respectively. These enzymes produce only low levels of hydrogen peroxide. Examples of 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, Although not limited to any one theory of operation, it is believed that the addition of a Ii 20 pase and peroxide leads to the formation of peracids which in turn oxidize unsaturated fatty acids, resin acids and other pitch components through an epoxidation reaction. The resulting products are hydrophilic and are readily washed from the pulp, thereby reducing or eliminating pitch prob lems, Organic acid(s) may also be added to the pulp, e.g., to enhance the pitch treatment. Or 25 ganic acids refer to any organic substance which contains at least one acidic group. Examples of organic acids are acetic acid, butyric acid, and linoleic acid. The concentration of organic acid is preferably between 0.001-500 mM. In the case of paper and pulp processing, 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 30 pulp 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. 35 In the present context, the term "process water' can include water added as a raw material to 4 WO 2007/095575 PCT/US2007/062136 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, In a particular embodiment, the process water is, has been, is being, or is intended for being circulated or re-circulated, iLe, re-used in another step of the process. The term "water" in turn means 5 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%, 5%, 4%, 3%, 20% or below 1% dry matter, The process of the invention may be carded out at conventional conditions in the paper and 10 pulp processing. The process conditions will be a function of the enzyme(s) applied, the reaction time and the conditions given. The enzyme and peroxide should be added in an effective amount. By the term "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 15 readily removed from the pulp or pulp process water. In a particular embodiment, 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., 0.5-10 % dry substance, In particular embodiments, the consistency is within the range of 0,5-45; 0,5-40; 0,5-35; 0,5-30; 0,5 20 25; 0.5-20; 0.5-15; 0,5-10; 0,5-8; 0,5-5; or 0,5-5% dry substance. The enzymatic treatment may be carried out at a temperature of from about 10 to about 100C0. Further examples of temperature ranges (all "from about" and "to about") are the following: 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*-C, as well as any combination of the upper and lower values here indicated. The temperature 25 may be from about 20 to 90*C, or 20 to 9500, preferably from about 40 to 7Q*C, or 40 to 754C. The enzymatic treatment may be carried out at a pH of from about 2 to about 12. Further examples of pH ranges (all tfrom about" and *to about") 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 arid lower values here indicated. The pH range may be from about 2 to 11, preferably within the range from 30 about 3-9. 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 I 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 35 hour, or from about 1 minute to about 30 minutes. The reaction time may be from about 10 minutes to 5 WO 2007/095575 PCT/US2007/062136 3 hours, 10 minutes to 10 hours, preferably 15 minutes to 1 hour, or 15 minutes to 2 hours, Various additives over and above the enzyme and peroxide treatment can be used in the process or use of the invention. Surfactants and/or dispersants are often present in, and/or added to a papermaking pulp, Thus the process and use of the present invention may be carried out in the 5 presence of an anionic, non-ionic., cationic and/or zwilterionic surfactant and/or dispersant conventionally used in a papermaking pulp, Examples of anionic surfactants are carboxylates, sulphates, sulphonates or phosphates of alkyl, substituted alkyl or aryl Fatty acids are examples of alkyl-carboxylates. Examples of non-ionic surfactants are polyoxyethylene compounds, such as alcohol ethoxylates, propoxylates or mixed ethoxy-/propoxylates, poly-glycerols and other polyols, as 10 well as certain block-copolymers. Examples of cationic surfactants are water-soluble cationic polymers, such as quartenary ammonium sulphates and certain amines, e.g. epichlorohydrin/dimethylamine polymers (EPI-OMA) 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. 5,681,862; and 5,575,993. Examples of zwitterionic or 15 amphoteric surfactants are betains, glycinates, amino propionates, imino propionates and various imidazolin-derivatives. Also the polymers disclosed in US patent no. 5,258,252 may be used. Also according to the invention, 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 to from about 8 to about 40% (wiw) of the composition. In particular embodiments the 20 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/v). It is to be understood that the term enzyme, as well as the various enzymes and enzyme 25 classes mentioned herein, 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. In a particular embodiment the enzyme in question is well-defined, meaning that only one 30 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, The term "applied together with" (or "used together with") means that the additional en zyme may be applied in the same, or in another step of the process of the invention. The other 35 process step may be upstream or downstream in the paper manufacturing process, as compared 6 WO 2007/095575 PCT/US2007/062136 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 lanase, cufinase, oxidoreductase, cellulase, endoglucanase, amylase, mannanase, steryl es 5 terase, and/or cholesterol esterase activity. Examples of oxidoreductase enzymes are enzymes with laccase, and/or peroxidase activity. The term "a step" of a process means at least one step, and it could be one, two, three, four, five or even more process steps. Thus, 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 10 step, which may be the same or a different process step as compared to the step where the lipase and peroxide source is used. The term "enzyme preparation" means a product containing at least one flpase enzyme, In addition to the enzymatic activity such a preparation preferably contains at least one adjuvant. Examples of adjuvants, which are used in enzyme preparations for the paper and pulp industry, 15 are buffers, polymers, surfactants and stabilizing agents. Any enzyme having protease, xylanase, cutinase, oxidoreductase, cellulase endogluca nase, 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 20 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. Examples of 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 p/si (WO 90/09446; WO 25 94/14964, WO 94/03578). The cutinase may also be derived from a strain of Rhizoctonia, e,g. R. solani, or a strain of Atemarfia, e.g. A, brassicicola (WO 94/03578), or variants thereof such as those described in WO 00/34450, or Wa 01/92502. Examples of proteases are the ALCALASE, ESPERASE, SAVINASE, NEUTRASE and DURAZYM proteases. Other proteases are derived from Nocardopsis, Aspergillus, Rhizopus, Ba 30 c/ilus alcalophilus, B. cereas, B. natto, B, vulgatus, B. mycoide, and subtilisins from Bacilius, es pecially proteases from the species Nocardiopsis sp. and Nocardiopsis dassonviliei such as those disclosed in WA 88/03947, and mutants thereof, e.g. those disclosed in WO 91/00345 and EP 415296, Examples of amylases are the BAN, AQUAZYM, TERMAMYL, and AQUAZYM Ultra amy 35 lases. An example of a xylanase is the PULPZYME HC hemicellulase. Examples of endogluca 7 WO 2007/095575 PCT/US2007/062136 nases are the NOVOZYM 613, 342, and 476 enzyme products. Examples of mannanases are the Tichoderma reeses endo-beta-mannanases described in Stuhlbrand et alt J. Biotechnol. 29 (1993), 229-242, Examples of steryl esterases, peroxidases, laccases, and cholesterol esterases are dis 5 closed in the references mentioned in the background art section hereof. Further examples of oxi doreductases 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, enhancers, mediators and/or activators, such compounds should be considered to be included if 10 not already present, Examples of enhancers and mediators are disclosed in EP 705327; WO 98/58899; EP 677102; EP 781328; and EP 707637, If desired a distinction could be made by de fining 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. 15 These are particular embodiments of the present invention: Use of a lipase and peroxide source for reducing the deposition of pitch in the paper making process. A process for reducing deposition of pitch in the paper making process, wherein the process comprises treating the pulp and/or process water with a lipase and peroxide source. Use of a lipase, peroxide source and or ganic acid for reducing the deposition of pitch in the paper making process, A process for reducing 20 deposition of pitch in the paper making process, wherein the process comprises treating the pulp and/or process water with a lipase, a peroxide source and organic acid. The invention described and claimed herein is not to be limited in scope by the specific embodiments herein disclosed, since these embodiments are intended as illustrations of several aspects of the invention. Any equivalent embodiments are intended to be within the scope of this 25 invention, Indeed, various modifications of the invention in addition to those shown and described herein will become apparent to those skilled in the art from the foregoing description. Such modi fications are also intended to fall within the scope of the appended claims, In the case of conflict, the present disclosure including definitions will control. Various references are cited herein, the disclosures of which are incorporated by refer 30 ence in their entireties. EXAMPLES Example 1. Deresination of Kraft pulp pitch by Candide antarctica lipase 8 (CALB) 35 Dammar resin was obtained from Fluka and used as a model pitch to simulate Kraft pulp pitch. 8 WO 2007/095575 PCT/US2007/062136 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. Sample ID Chemical/Enzyme Dose per beaker 600nm 1 Control 0.043 2 CALB 50 mg 0.222 3 Peroxide 25 mg 0.084 4 CALB and peroxide 50 mg/25 rg 0.847 5 Peroxide and TAED 25 mg/360 mg 0.501 5 After mixing the samples overnight, it was observed that the lipase (CALB) and peroxide treated sample turned into milky emulsion whereas the control sample was still as clear as water with the resins deposited either at the bottom on the wall of the of the flask. The turbidity results clearly showed that a combination of peroxide with lipase could lead to better emulsification of dammar 10 resin. Peracetic acid generated in situ by peroxide and a bleach activator (TAED) was also fairly effective, but not as effective as peroxide and lipase combination. Example 2, Deresination of Kraft pulp pitch by Resinase A2X and Resinase HT. The experiment was carried out in the same manner as illustrated in Example I except that the 15 flasks were stirred overnight at 40*C. The lipases used in this study were Resinase@ A2X and Resinase@ HT (available from Novozymes AiS). Sample ID Chemical/Enzyme Dose er beaker 60Onm 6 Control 0.104 8 Resinase@ HT 50 mgf2S Mg 0.219 9 Resinase@ A2X and 50 mg/25 mg 0.535 H202 10 Resinase® HT and 50 mg/25 mg 0.614
H
2
O
2 it is evident that both Resinase@ A2X and Resinase® HT worked to emulsify the Kraft model 20 pitch. 9
Claims (11)
1. A method for reducing pitch problems in a chemical pulp, comprising treating a chemical pulp with a lipase and a peroxide source in amount effective to reduce pitch problems. 5
2. The method of claim I, wherein said treating is performed before. after or in between bleaching stages.
3. The method of claim 1, wherein said chemical pulp is a Kraft pulp. 10
4. The method of claim 1, wherein said chemical pulp is a sulfite pulp.
5. The method of claim 1, wherein said chemical pulp is bleached Kraft pulp. 15 6. The method of claim 1, further comprising the step of preparing paper, linerboard, corru gated paperboard, tissue, towels, corrugated containers or boxes from said pulp.
7. The method of claim 1, wherein said lipase is derived from a strain of Aspergillus, a strain of Achrmobacter, a strain of Bacillus, a strain of Candida, a strain of Chromobacter, a strain of Fusa 20 rium, a strain of Humicola, a strain of Hyphozyma, a strain of Pseudomonas, a strain of Rhizomucor, a strain of Rhizo pus, or a strain of Thennomyces. 8, The method of claim 1, wherein said lipase is derived from a strain of Candida, 25 9. The method of claim 1, wherein said lipase is derived from a strain of Candida antarica lipase A or the Candida antarctica lipase B.
10. The method of claim 1, comprising treating a chemical pulp with a lipase, a peroxide source and an organic acid, 30 1M The method of claim 1, wherein peroxide source is hydrogen peroxide,
12. The method of claim 1, wherein peroxide source is a precursor of hydrogen peroxide, 35 13. The method of claim 12, wherein the precursor of hydrogen peroxide is perborate or a 10 WO 2007/095575 PCT/US2007/062136 percarbonate.
14. The method of claim 1, wherein the peroxide source is an enzyme that converts molecu lar oxygen and an organic or inorganic substrate into hydrogen peroxide. 5
15. Use of a lipase and a peroxide source for reducing pitch problems,
16. Use of a lipase and a peroxide source for reducing pitch problems in chemical pulp. 11
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| US60/773,242 | 2006-02-14 | ||
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| US20030051836A1 (en) * | 2001-05-21 | 2003-03-20 | Novozymes A/S | Enzymatic hydrolysis of a polymer comprising vinyl acetate monomer |
| CA2607827C (en) * | 2005-05-04 | 2013-11-19 | Novozymes North America, Inc. | Chlorine dioxide treatment compositions and processes |
| EP2534254A4 (en) * | 2010-02-08 | 2014-01-22 | Iogen Energy Corp | Method for scale removal during a lignocellulosic conversion process |
| JP5833643B2 (en) * | 2010-06-08 | 2015-12-16 | バックマン・ラボラトリーズ・インターナショナル・インコーポレーテッドBuckman Laboratories International Incorporated | Method for decomposing sludge from pulp and paper manufacture |
| AU2012328637B2 (en) * | 2011-10-27 | 2016-06-02 | Buckman Laboratories International, Inc. | Method and composition for enzymatic treatment of fiber for papermaking, and paper products made therewith |
| NZ702937A (en) | 2012-06-22 | 2016-07-29 | Buckman Lab Int Inc | Methods of using combinations of a lipase and an oxidant for pitch control in paper making processes and products thereof |
| 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 |
| CN106436417B (en) * | 2016-10-19 | 2019-03-05 | 瑞辰星生物技术(广州)有限公司 | Composition and papermaking method for controlling deposition of organic pollutants in pulp and paper 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 |
| WO2025230818A1 (en) | 2024-05-03 | 2025-11-06 | Buckman Laboratories International, Inc. | Methods for dehairing animal skins and hides and formulations related to same |
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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 |
| NZ235983A (en) * | 1989-11-08 | 1993-01-27 | Novo Nordisk As | Process for hydrolysis of resins in lignocellulosic pulp using enzymes simultaneously with peroxy bleaching; ctmp fluff-pulp and absorbent articles produced therefrom |
| US5256252A (en) * | 1992-07-15 | 1993-10-26 | Nalco Chemical Company | Method for controlling pitch deposits using lipase and cationic polymer |
| DK39593D0 (en) * | 1993-04-02 | 1993-04-02 | Novo Nordisk As | ENZYME |
| JP3589870B2 (en) * | 1998-09-02 | 2004-11-17 | 日本製紙株式会社 | Pitch trouble prevention method by enzyme |
| FI990501L (en) * | 1999-03-08 | 2000-09-09 | Valtion Teknillinen | A new enzymatic process to control pitch problems in papermaking |
| US20030124710A1 (en) * | 2001-10-23 | 2003-07-03 | Novozymes A/S | Oxidizing enzymes in the manufacture of paper materials |
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| CN101384769A (en) | 2009-03-11 |
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