WO2003023043A1 - Laccase activity enhancers - Google Patents
Laccase activity enhancers Download PDFInfo
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- WO2003023043A1 WO2003023043A1 PCT/US2002/018540 US0218540W WO03023043A1 WO 2003023043 A1 WO2003023043 A1 WO 2003023043A1 US 0218540 W US0218540 W US 0218540W WO 03023043 A1 WO03023043 A1 WO 03023043A1
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- Prior art keywords
- enzyme
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- monomer
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- 108010029541 Laccase Proteins 0.000 title claims abstract description 57
- 230000000694 effects Effects 0.000 title claims abstract description 45
- 239000003623 enhancer Substances 0.000 title description 2
- 102000004190 Enzymes Human genes 0.000 claims abstract description 81
- 108090000790 Enzymes Proteins 0.000 claims abstract description 81
- 230000002708 enhancing effect Effects 0.000 claims abstract description 29
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 28
- 238000000034 method Methods 0.000 claims abstract description 28
- 230000008569 process Effects 0.000 claims abstract description 28
- 230000001747 exhibiting effect Effects 0.000 claims abstract description 20
- 239000000203 mixture Substances 0.000 claims abstract description 14
- 239000000758 substrate Substances 0.000 claims abstract description 12
- 230000001590 oxidative effect Effects 0.000 claims abstract description 5
- 125000000956 methoxy group Chemical group [H]C([H])([H])O* 0.000 claims description 32
- 239000000178 monomer Substances 0.000 claims description 26
- MIYKHJXFICMPOJ-UHFFFAOYSA-N n-benzyl-1-phenylmethanimine Chemical compound C=1C=CC=CC=1CN=CC1=CC=CC=C1 MIYKHJXFICMPOJ-UHFFFAOYSA-N 0.000 claims description 22
- ROSDSFDQCJNGOL-UHFFFAOYSA-N Dimethylamine Chemical compound CNC ROSDSFDQCJNGOL-UHFFFAOYSA-N 0.000 claims description 20
- PCYGLFXKCBFGPC-UHFFFAOYSA-N 4-(hydroxymethyl)benzene-1,2-diol Chemical compound OCC1=CC=C(O)C(O)=C1 PCYGLFXKCBFGPC-UHFFFAOYSA-N 0.000 claims description 18
- 239000000539 dimer Substances 0.000 claims description 18
- YGSDEFSMJLZEOE-UHFFFAOYSA-N salicylic acid Chemical compound OC(=O)C1=CC=CC=C1O YGSDEFSMJLZEOE-UHFFFAOYSA-N 0.000 claims description 16
- 125000003118 aryl group Chemical group 0.000 claims description 14
- 125000001931 aliphatic group Chemical group 0.000 claims description 13
- 238000004061 bleaching Methods 0.000 claims description 13
- 239000000463 material Substances 0.000 claims description 13
- 239000011121 hardwood Substances 0.000 claims description 11
- 229920005610 lignin Polymers 0.000 claims description 11
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims description 10
- 150000001851 cinnamic acid derivatives Chemical class 0.000 claims description 10
- 239000011122 softwood Substances 0.000 claims description 10
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 claims description 9
- 108010015428 Bilirubin oxidase Proteins 0.000 claims description 8
- 108010031396 Catechol oxidase Proteins 0.000 claims description 8
- 102000030523 Catechol oxidase Human genes 0.000 claims description 8
- 239000007800 oxidant agent Substances 0.000 claims description 8
- FJKROLUGYXJWQN-UHFFFAOYSA-N papa-hydroxy-benzoic acid Natural products OC(=O)C1=CC=C(O)C=C1 FJKROLUGYXJWQN-UHFFFAOYSA-N 0.000 claims description 8
- 229960004889 salicylic acid Drugs 0.000 claims description 8
- WMBWREPUVVBILR-WIYYLYMNSA-N (-)-Epigallocatechin-3-o-gallate Chemical compound O([C@@H]1CC2=C(O)C=C(C=C2O[C@@H]1C=1C=C(O)C(O)=C(O)C=1)O)C(=O)C1=CC(O)=C(O)C(O)=C1 WMBWREPUVVBILR-WIYYLYMNSA-N 0.000 claims description 7
- WMBWREPUVVBILR-UHFFFAOYSA-N GCG Natural products C=1C(O)=C(O)C(O)=CC=1C1OC2=CC(O)=CC(O)=C2CC1OC(=O)C1=CC(O)=C(O)C(O)=C1 WMBWREPUVVBILR-UHFFFAOYSA-N 0.000 claims description 7
- 229910006069 SO3H Inorganic materials 0.000 claims description 7
- 229940030275 epigallocatechin gallate Drugs 0.000 claims description 7
- 125000000325 methylidene group Chemical group [H]C([H])=* 0.000 claims description 7
- 125000000020 sulfo group Chemical group O=S(=O)([*])O[H] 0.000 claims description 7
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 claims description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 6
- 229920000877 Melamine resin Polymers 0.000 claims description 6
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 claims description 6
- JDSHMPZPIAZGSV-UHFFFAOYSA-N melamine Chemical compound NC1=NC(N)=NC(N)=N1 JDSHMPZPIAZGSV-UHFFFAOYSA-N 0.000 claims description 6
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- 239000001301 oxygen Substances 0.000 claims description 6
- JOLPMPPNHIACPD-ZZXKWVIFSA-N (e)-3-(4-aminophenyl)prop-2-enoic acid Chemical compound NC1=CC=C(\C=C\C(O)=O)C=C1 JOLPMPPNHIACPD-ZZXKWVIFSA-N 0.000 claims description 5
- CQNPVMCASGWEHM-VMPITWQZSA-N (e)-3-[4-(dimethylamino)phenyl]prop-2-enoic acid Chemical compound CN(C)C1=CC=C(\C=C\C(O)=O)C=C1 CQNPVMCASGWEHM-VMPITWQZSA-N 0.000 claims description 5
- GXLIFJYFGMHYDY-ZZXKWVIFSA-N 4-chlorocinnamic acid Chemical compound OC(=O)\C=C\C1=CC=C(Cl)C=C1 GXLIFJYFGMHYDY-ZZXKWVIFSA-N 0.000 claims description 5
- 239000002253 acid Substances 0.000 claims description 5
- 239000003570 air Substances 0.000 claims description 5
- 108010024957 Ascorbate Oxidase Proteins 0.000 claims description 4
- 229920001732 Lignosulfonate Polymers 0.000 claims description 4
- 102000004005 Prostaglandin-endoperoxide synthases Human genes 0.000 claims description 4
- 108090000459 Prostaglandin-endoperoxide synthases Proteins 0.000 claims description 4
- WBYWAXJHAXSJNI-VOTSOKGWSA-M .beta-Phenylacrylic acid Natural products [O-]C(=O)\C=C\C1=CC=CC=C1 WBYWAXJHAXSJNI-VOTSOKGWSA-M 0.000 claims description 3
- WBYWAXJHAXSJNI-SREVYHEPSA-N Cinnamic acid Chemical compound OC(=O)\C=C/C1=CC=CC=C1 WBYWAXJHAXSJNI-SREVYHEPSA-N 0.000 claims description 3
- 229920001131 Pulp (paper) Polymers 0.000 claims description 3
- 102000003425 Tyrosinase Human genes 0.000 claims description 3
- 108060008724 Tyrosinase Proteins 0.000 claims description 3
- 235000013985 cinnamic acid Nutrition 0.000 claims description 3
- 229930016911 cinnamic acid Natural products 0.000 claims description 3
- WBYWAXJHAXSJNI-UHFFFAOYSA-N methyl p-hydroxycinnamate Natural products OC(=O)C=CC1=CC=CC=C1 WBYWAXJHAXSJNI-UHFFFAOYSA-N 0.000 claims description 3
- 229920002678 cellulose Polymers 0.000 claims 2
- 239000001913 cellulose Substances 0.000 claims 2
- 102000008109 Mixed Function Oxygenases Human genes 0.000 claims 1
- 108010074633 Mixed Function Oxygenases Proteins 0.000 claims 1
- 239000002994 raw material Substances 0.000 claims 1
- 150000001875 compounds Chemical class 0.000 abstract description 8
- 230000003213 activating effect Effects 0.000 abstract description 4
- 238000006116 polymerization reaction Methods 0.000 abstract description 4
- 239000007844 bleaching agent Substances 0.000 abstract description 3
- 125000000391 vinyl group Chemical group [H]C([*])=C([H])[H] 0.000 abstract description 3
- 229920002554 vinyl polymer Polymers 0.000 abstract description 3
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- 238000002835 absorbance Methods 0.000 description 10
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- 238000003556 assay Methods 0.000 description 5
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- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
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- 239000000975 dye Substances 0.000 description 3
- QURCVMIEKCOAJU-UHFFFAOYSA-N trans-isoferulic acid Natural products COC1=CC=C(C=CC(O)=O)C=C1O QURCVMIEKCOAJU-UHFFFAOYSA-N 0.000 description 3
- 239000002351 wastewater Substances 0.000 description 3
- OEGPRYNGFWGMMV-UHFFFAOYSA-N (3,4-dimethoxyphenyl)methanol Chemical compound COC1=CC=C(CO)C=C1OC OEGPRYNGFWGMMV-UHFFFAOYSA-N 0.000 description 2
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- KSEBMYQBYZTDHS-UHFFFAOYSA-N ferulic acid Natural products COC1=CC(C=CC(O)=O)=CC=C1O KSEBMYQBYZTDHS-UHFFFAOYSA-N 0.000 description 2
- 230000002538 fungal effect Effects 0.000 description 2
- JXDYKVIHCLTXOP-UHFFFAOYSA-N isatin Chemical compound C1=CC=C2C(=O)C(=O)NC2=C1 JXDYKVIHCLTXOP-UHFFFAOYSA-N 0.000 description 2
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- 238000004076 pulp bleaching Methods 0.000 description 2
- PCMORTLOPMLEFB-UHFFFAOYSA-N sinapic acid Chemical compound COC1=CC(C=CC(O)=O)=CC(OC)=C1O PCMORTLOPMLEFB-UHFFFAOYSA-N 0.000 description 2
- 125000001424 substituent group Chemical group 0.000 description 2
- AFDXODALSZRGIH-QPJJXVBHSA-N (E)-3-(4-methoxyphenyl)prop-2-enoic acid Chemical compound COC1=CC=C(\C=C\C(O)=O)C=C1 AFDXODALSZRGIH-QPJJXVBHSA-N 0.000 description 1
- KSEBMYQBYZTDHS-HWKANZROSA-M (E)-Ferulic acid Natural products COC1=CC(\C=C\C([O-])=O)=CC=C1O KSEBMYQBYZTDHS-HWKANZROSA-M 0.000 description 1
- KJRRTHHNKJBVBO-AATRIKPKSA-N (e)-3-(2-chlorophenyl)prop-2-enoic acid Chemical compound OC(=O)\C=C\C1=CC=CC=C1Cl KJRRTHHNKJBVBO-AATRIKPKSA-N 0.000 description 1
- ASOKPJOREAFHNY-UHFFFAOYSA-N 1-Hydroxybenzotriazole Chemical compound C1=CC=C2N(O)N=NC2=C1 ASOKPJOREAFHNY-UHFFFAOYSA-N 0.000 description 1
- BOBATFKNMFWLFG-UHFFFAOYSA-N 2-amino-2-cyano-n-methylacetamide Chemical compound CNC(=O)C(N)C#N BOBATFKNMFWLFG-UHFFFAOYSA-N 0.000 description 1
- YTFVRYKNXDADBI-SNAWJCMRSA-N 3,4,5-trimethoxycinnamic acid Chemical compound COC1=CC(\C=C\C(O)=O)=CC(OC)=C1OC YTFVRYKNXDADBI-SNAWJCMRSA-N 0.000 description 1
- HJBWJAPEBGSQPR-GQCTYLIASA-N 3,4-dimethoxycinnamic acid Chemical compound COC1=CC=C(\C=C\C(O)=O)C=C1OC HJBWJAPEBGSQPR-GQCTYLIASA-N 0.000 description 1
- SCJHPUGWYHCYAZ-UHFFFAOYSA-N 3,5-diethyl-2-propylpyridine Chemical compound CCCC1=NC=C(CC)C=C1CC SCJHPUGWYHCYAZ-UHFFFAOYSA-N 0.000 description 1
- FOGYNLXERPKEGN-UHFFFAOYSA-N 3-(2-hydroxy-3-methoxyphenyl)-2-[2-methoxy-4-(3-sulfopropyl)phenoxy]propane-1-sulfonic acid Chemical compound COC1=CC=CC(CC(CS(O)(=O)=O)OC=2C(=CC(CCCS(O)(=O)=O)=CC=2)OC)=C1O FOGYNLXERPKEGN-UHFFFAOYSA-N 0.000 description 1
- FFKGOJWPSXRALK-UHFFFAOYSA-N 3-(3-chlorophenyl)prop-2-enoic acid Chemical compound OC(=O)C=CC1=CC=CC(Cl)=C1 FFKGOJWPSXRALK-UHFFFAOYSA-N 0.000 description 1
- LZPNXAULYJPXEH-AATRIKPKSA-N 3-Methoxycinnamic acid Chemical compound COC1=CC=CC(\C=C\C(O)=O)=C1 LZPNXAULYJPXEH-AATRIKPKSA-N 0.000 description 1
- HRRVLSKRYVIEPR-UHFFFAOYSA-N 6-hydroxy-5-nitroso-1H-pyrimidine-2,4-dione Chemical compound OC1=NC(O)=C(N=O)C(O)=N1 HRRVLSKRYVIEPR-UHFFFAOYSA-N 0.000 description 1
- 0 CC(C)(C1)C(*)=CC=C1C=CC(O)=O Chemical compound CC(C)(C1)C(*)=CC=C1C=CC(O)=O 0.000 description 1
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- GYCKQBWUSACYIF-UHFFFAOYSA-N Ethyl salicylate Chemical compound CCOC(=O)C1=CC=CC=C1O GYCKQBWUSACYIF-UHFFFAOYSA-N 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical group ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 1
- LSDPWZHWYPCBBB-UHFFFAOYSA-N Methanethiol Chemical group SC LSDPWZHWYPCBBB-UHFFFAOYSA-N 0.000 description 1
- YTFVRYKNXDADBI-UHFFFAOYSA-N O-Methylsinapic acid Natural products COC1=CC(C=CC(O)=O)=CC(OC)=C1OC YTFVRYKNXDADBI-UHFFFAOYSA-N 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 150000001336 alkenes Chemical group 0.000 description 1
- 150000001491 aromatic compounds Chemical class 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- BPHHNXJPFPEJOF-UHFFFAOYSA-J chembl296966 Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]S(=O)(=O)C1=CC(S([O-])(=O)=O)=C(N)C2=C(O)C(N=NC3=CC=C(C=C3OC)C=3C=C(C(=CC=3)N=NC=3C(=C4C(N)=C(C=C(C4=CC=3)S([O-])(=O)=O)S([O-])(=O)=O)O)OC)=CC=C21 BPHHNXJPFPEJOF-UHFFFAOYSA-J 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 238000004042 decolorization Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 1
- 229940005667 ethyl salicylate Drugs 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- KSEBMYQBYZTDHS-HWKANZROSA-N ferulic acid Chemical compound COC1=CC(\C=C\C(O)=O)=CC=C1O KSEBMYQBYZTDHS-HWKANZROSA-N 0.000 description 1
- 235000001785 ferulic acid Nutrition 0.000 description 1
- 229940114124 ferulic acid Drugs 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 231100001261 hazardous Toxicity 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- -1 i.e. Proteins 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- KKSDGJDHHZEWEP-UHFFFAOYSA-N m-hydroxycinnamic acid Natural products OC(=O)C=CC1=CC=CC(O)=C1 KKSDGJDHHZEWEP-UHFFFAOYSA-N 0.000 description 1
- 150000004702 methyl esters Chemical class 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- PMOWTIHVNWZYFI-UHFFFAOYSA-N o-Coumaric acid Natural products OC(=O)C=CC1=CC=CC=C1O PMOWTIHVNWZYFI-UHFFFAOYSA-N 0.000 description 1
- JRZJOMJEPLMPRA-UHFFFAOYSA-N olefin Chemical group CCCCCCCC=C JRZJOMJEPLMPRA-UHFFFAOYSA-N 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- AFDXODALSZRGIH-UHFFFAOYSA-N p-coumaric acid methyl ether Natural products COC1=CC=C(C=CC(O)=O)C=C1 AFDXODALSZRGIH-UHFFFAOYSA-N 0.000 description 1
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- 229920001221 xylan Polymers 0.000 description 1
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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
- D21C3/00—Pulping cellulose-containing materials
- D21C3/22—Other features of pulping processes
- D21C3/222—Use of compounds accelerating the pulping processes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P1/00—Preparation of compounds or compositions, not provided for in groups C12P3/00 - C12P39/00, by using microorganisms or enzymes
-
- D—TEXTILES; PAPER
- D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
- D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
- D21C9/00—After-treatment of cellulose pulp, e.g. of wood pulp, or cotton linters ; Treatment of dilute or dewatered pulp or process improvement taking place after obtaining the raw cellulosic material and not provided for elsewhere
- D21C9/10—Bleaching ; Apparatus therefor
- D21C9/1026—Other features in bleaching processes
- D21C9/1036—Use of compounds accelerating or improving the efficiency of the processes
-
- D—TEXTILES; PAPER
- D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
- D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
- D21C5/00—Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
- D21C5/005—Treatment of cellulose-containing material with microorganisms or enzymes
Abstract
New mediators for use in laccase-mediator systems (LMS) are disclosed. The mediators enhance the activity of enzymes exhibiting laccase activity and can be used, for example, to bleach a dye in solution, to oxidize an appropriate compound, or to initiate vinyl or phenol polymerizations. A composition comprising an enzyme exhibiting laccase activity and an enzyme enhancing agent (also referred to as a mediator or an activating agent) is also disclosed. A process for oxidizing a substrate that comprises treating the substrate with a composition comprising an enzyme exhibiting laccase activity and an enzyme enhancing agent is also disclosed.
Description
LACCASE ACTIVITY ENHANCERS
. CROSS REFERENCE TO RELATED APPLICATIONS
FIELD OF THE INVENTION
The present invention relates to the enhancement of enzyme activity and the activation of enzymes. More specifically, the present invention relates to mediators, enhancing agents, or activating agents that are useful in enhancing the activity of enzymes having laccase activity.
BACKGROUND OF THE INVENTION
Laccases are copper-containing enzymes that are known to be good oxidizing agents in the presence of oxygen. Laccases are found in microbes, fungi, and higher organisms. Laccase enzymes are used for many applications, including pulp bleaching, treatment of pulp waste water, de-inking, industrial color removal, bleaching laundry detergents, oral care teeth whiteners, and as catalysts or facilitators for polymerization and oxidation reactions. Commercial enzymes are often produced from fungal sources.
For many applications, the oxidizing efficiency of a laccase can be improved through the use of a mediator, also known as an enhancing agent. Systems that include a laccase and a mediator are known in the art as laccase-mediator systems (LMS). The same compounds can also be used to activate or initiate the action of laccase.
There are several known mediators for use in a laccase-mediator system. These include
HBT (1-hydroxybenzotriazole), ABTS [2,2'-azmobis(3-ethylbenzothiazoline-6-sulfmic acid)], NHA (N-hydroxyacetinilide), NHAA (N-acetyl-N-phenymydroxylamine), HBTO (3-hydroxy- l,2,3-benzotriazin-4(3H)-one), and VIO (violuric acid). In addition, there are several compounds containing NH-OH or N-O that have been found to be useful as mediators.
Functional groups and substituents have large effects on mediator efficiency. Even within the same class of compounds, a substituent can change the laccase specificity towards a substrate, thereby increasing or decreasing mediator efficiency greatly. In addition, a mediator may be effective for one particular application but unsuitable for another application. Thus, there is a need to discover efficient mediators for specific applications. One such application is the bleaching of pulp, wherein it is also important that the mediators are not unduly expensive or hazardous. Other applications of the laccase-mediator system are given below.
Thus, there is a need to identify additional mediators that activate laccase, and/or enhance the activity of enzymes that exhibit laccase activity.
SUMMARY OF THE INVENTION
The present invention provides mediators for use in laccase-mediator systems (LMS). The mediators of the invention enhance the activity of enzymes exhibiting laccase activity and can be used, for example, to bleach a dye in solution, to oxidize an appropriate compound, or to initiate vinyl or phenol polymerizations.
The invention provides a composition comprising an enzyme exhibiting laccase activity and an enzyme enhancing agent (also referred to as a mediator or an activating agent). The enzyme enhancing or activating agent is selected from: (i) a monomer, dimer, or oligomer of at least one of:
R4 is an OH or methylene that connects to another monomer; and R5 is SO3H or H;
(ii) N-benzylidene benzylamine (NBBA) or a substituted NBBA having the structure:
wherein:
R6 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; and R7 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group;
(iii) a derivative of cinnamic acid having the structure:
wherein: R8 is OCH3, NH2, Cl, NH(CH3)2; and
(iv) salicylic acid;
(v) epigallocatechin gallate;
(vi) mela nine; (vii) 3,4-dihydroxybenzyl alcohol (DHBA) or a substituted DHBA;
(viii) a hardwood black liquor;
(ix) a hardwood black liquor that comprises the monomer, dimer, or oligomer of group
Q;
(x) a softwood black liquor; and (xi) a softwood black liquor that comprises monomer, dimer, or oligomer under group (i).
The invention also provides a process for oxidizing a substrate that comprises treating the substrate with a composition comprising an enzyme exhibiting laccase activity and an enzyme enhancing agent.
The invention further provides a process for bleaching a lignin-containing material that comprises treating the material with an enzyme exhibiting laccase activity and an enzyme enhancing agent.
In addition, the invention provides a process for enhancing the activity of an enzyme exhibiting laccase activity that comprises adding an enzyme enhancing agent to the enzyme.
The process of the invention can further include the step of adding an oxidizing agent, such as at least one of air, oxygen, and hydrogen peroxide.
BRIEF DESCRIPTION OF THE DRAWING
Figure 1 illustrates the bleaching of the Chicago Blue Dye (DB1) in the presence and absence of the mediator ABTS.
DETAILED DESCRIPTION OF THE INVENTION
The invention provides newly identified enzyme enhancing agents (also referred to as mediators) that enhance the activity of enzymes exhibiting laccase activity.
The mediators of this invention are capable of enhancing the activities of laccase and laccase-related enzymes, i.e., enzymes exhibiting laccase activity. The enzymes exhibiting laccase enzyme activity include the laccase enzymes of enzyme classification EC 1.10.3.2, the catechol oxidase enzymes of enzyme classification EC 1.10.3.1, the monophenol
monooxygenase enzymes of enzyme classification EC 1.14.99.1, the bilirubin oxidase enzymes of enzyme classification EC 1.3.3.5, and the ascorbate oxidase enzymes of enzyme classification EC 1.10.3.3. The EC (Enzyme Commission) number is based upon the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB).
The enzymes exhibiting laccase activity may be derived from microbial, fungal, or other sources. These enzymes can also be produced by recombinant methods that are well known to those skilled in the art, such as cultivating a host cell transformed with a recombinant DNA vector that includes a DNA sequence encoding a laccase (and, optionally, DNA sequences that permit the expression of the laccase DNA sequence) in a culture medium under conditions that permit the expression of the laccase, and recovering the enzyme from the culture. The composition of the invention can further include a hydrolase, such as xylanase.
The enzyme enhancing agents of the invention are selected from: (i) a monomer, dimer, or oligomer of at least one of:
Rj is OCH3, H, or another moiety; R2 is OCH3, H, or another moiety; R3 is OH, sulfonate, or another moiety;
R4 is an OH or methylene that connects to another monomer; and R5 is SO3H orH; (ii) N-benzylidene benzylamine (NBBA) or a substituted NBBA having the structure:
wherein:
R6 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; and R7 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; (iii) a derivative of cinnamic acid having the structure:
wherein:
R8 is OCH3, NH2, Cl, NH(CH3)2; and
R9 is OH or H; (vi) salicylic acid;
(v) epigallocatechin gallate;
(vi) melamine;
(vii) 3,4-dihydroxybenzyl alcohol (DHBA) or a substituted DHBA;
(viii) a hardwood black liquor; (ix) a hardwood black liquor that comprises the monomer, dimer, or oligomer of group
(i);
(x) a softwood black liquor; and
(xi) a softwood black liquor that comprises monomer, dimer, or oligomer under group (i).
Without limiting the scope of the invention, the enzyme enhancing agents of the invention can be classified into four categories:
I. Lignin-like Materials a. Organic soluble fraction of lignin (lignin organosolv) b. Lignin sulfonate c. Hardwood black liquor and softwood black liquor
Each of these three materials is a mixture comprising monomers, dimers, and oligomers with the following structures.
II. N-benzylidene benzylamine (NBBA and substituted NBBA.
In this structure, R6 and R7 are H or OCH3, NH(CH3)2, Cl, Br, aliphatic or aromatic groups, substituted at the 2 and 4 positions.
III. Derivatives of cinnamic acid a. 4-(dimethylamino)cinnamic acid b. 3 -hydroxy-4-methyoxy cinnamic acid c. 4-aminocinnamic acid d. 4-chlorocinnamic acid
In this structure, R8 is OCH3, NH2, Cl, NH(CH3)2, and Rg is OH or H.
IV. Other Aromatic Compounds a. salicylic acid b. epigallocatechin gallate c. melarnine d. 3,4-dihydroxybenzyl alcohol (DHBA), and substituted DHBA.
The mediators of the invention can be used, for example, for pulp delignification and bleaching. Laccase itself can bleach pulp only to a limited extent. The use of the mediators as disclosed herein enhances the activity of laccase in pulp bleaching through delignification. Other applications that may use the present invention include: polymerization of vinyl monomers or phenolic compounds; oxidation of materials containing hydroxy, amine, mercaptan, olefin, and aromatic moieties; microbial control in personal care products; bleaching of hair; treatment of waste water, particularly waste water in pulp mills; and bleaching in laundry detergents.
Another aspect of the invention provides a process for oxidizing a substrate that comprises treating the substrate with a composition comprising an enzyme exliibiting laccase activity and an enzyme enhancing agent. The enzyme enhancing agent can be selected from one or the above described enzyme enhancing agents.
The enhancing agent may be present in concentrations of from about 0.01 micromolar to 1000 micromolar, more preferably from about 0.1 micromolar to about 250 micromolar and most preferably from about 0.5 to about 100 micromolar.
The enzyme is used in amounts of from 0.001 to 50 units (defined in the Examples using ABTS as substrate) in 1 ml of the reaction solution , preferably from about 0.01 to 20 units and even more preferably from 0.1 to 10 units and most preferably from 2 to -3 units
The process of the invention can further include the step of adding an oxidizing agent, such as at least one of air, oxygen, and hydrogen peroxide.
One aspect of the invention provides a process for bleaching a lignin-containing material that comprises treating the material with an enzyme exhibiting laccase activity and an enzyme enhancing agent. In this aspect of the invention, the enhancing agent may be present in an amount of from about 0.1% to about 15% based on the weight of the dry lignin containing material, more preferably from about 0.1 % to about 10% and even more preferably from about 0.5% to about 5% and most preferably from about 1% to about 4 %. One example of a lignin containing material is wood pulp. The process for bleaching a lignin-containing material can further include the step of adding an oxidizing agent, such as at least one of air, oxygen, and hydrogen peroxide.
EXAMPLES
The following examples are illustrative of the present invention, and are not intended to be construed in any way as limiting the scope of the invention.
The specific activity was determined using ABTS (0.5 mM) as substrate. One unit of activity is equal to the umol of the oxidized product from ABTS per min per mg protein at pH 6.0 at 23 °C. The extinction coefficient of the oxidized ABTS is: ε(max) at 420 nm=36,000M-lcm-l.)
Alternatively, the activity of laccase (NS51003) was determined using syringaldazine as substrate. In this case, one unit of activity is equal to the change of 0.001 UV absorbance at A530nm per minute per ug protein in 2 ml of 100 mM, pH 5.5 potassium phosphate buffer, and 0.5 ml of 0.25 mM syringaldazine in methanol at 23 °C.
The assay results for three samples of laccase enzyme are shown in the following table. Samples NS 51002 and NS51003 were obtained from Novozymes A/S (Denmark). Unless otherwise stated, the results given in the examples were based on the enzyme NS51003.
Name Source Density Activity Protein Specific activity
(umol/mi con. (umol/min. n.ml) (mg/ml) mg protein)
NS51002 Aspergillus sp., 1.08 895 25 36 Novozymes
NS51003 Aspergillus sp., 1.04 750 20 38 Novozymes
Example 1 -Use of the Chicago Blue assay.
In the following example, several compounds were tested to identify enzyme enhancing agents that enhance the activity of an enzyme that exhibits laccase activity. The Chicago Blue Dye, also known as Direct Blue 1 or DB1, was used to identify these compounds. The Chicago Blue Dye is fully described by Schneider et al. in U.S. Patent No. 5,885,304, which is hereby incorporated by reference, and has the following formula.
Each of the test compounds (i.e., potential mediators) was dissolved in water, or in ethanol if the potential mediator was not water soluble, and then mixed with a phosphate buffer and a Chicago Blue solution. A solution of a laccase was added to make up 1 ml of the final solution, containing 20 uM mediator, 20 mM buffer at pH 5.5 or 7.0, 0.1-1% laccase (v/v) and Chicago Blue solution, with absorbance at A610 nm between 0.6 to 0.8. The change in the absorbance at A610 nm was measured immediately using a UV-VIS spectrophotometer (UV- 1201, Shimadzu Scientific Instruments) after the enzyme was added. The decrease in absorbance was recorded at 30-second intervals for 5 minutes and was used to estimate the efficiency of the mediator.
As a reference point, the decrease in absorbance for the Chicago Blue dye in the presence and the absence of the ABTS mediator is shown in Figure 1.
Example 2 - Screening for potential mediators using the Chicago Blue dye.
Experiments were conducted at pH levels of 5.5 and 7.0. The results of the Chicago Blue Assay at pH 5.5 and pH 7.0 are provided in the following tables below. The last column gives the decrease in absorbance at 610 nm. The larger the decrease in absorbance at 610 nm, the better is the ability to discolor the dye.
Table 1 - Results of the Chicago Blue Assay at pH 5.5
Potential Mediator (0.1 micromole/ml Appearance ΔmA610 in water (3 mih)
None clear 0
4-(Dimethylamino)cinnamic acid clear, yellow 519
3,5-Dimethoxy-4-hydroxycinnamic acid clear 491
4-Hydroxy-3-methoxy cinnamic acid (ferulic acid) clear 441
Hardwood black liquor (150 ul, 12%) yellow 425
Lignin, organosolv. (20ug/ml) clear, brown 390
Melamine cloudy 128
3 -Hydroxy-4-methoxy cinnamic acid clear 94
4-Aminocinnamic acid clear 43
4-Hydroxycinnamic acid clear 42
N-benzylidene benzylamine clear 28
Lignosulfonic acid. (25ug/ml) Light brown 24
4-Chlorocinnamic acid cloudy 13
Salicylic acid clear 11
Softwood black liquor (150 ul, 12%) yellow 10
2-Chlorocinnamic acid cloudy 9
3-Chlorocinnamic acid cloudy 8
3-Hydroxycinnamic acid clear 7
4-Methoxycinnamic acid cloudy 6
Isatin clear 6
2-Hydroxycinnamic acid clear 5
3,4,5-Trimethoxycinnamic acid cloudy 5
3-Methoxycinnamic acid clear 4
Cinnamic acid clear 3
2-Aminopyridine light brown 3
Veratryl alcohol clear 3
Ethyl Salicylate cloudy 2
3, 4-Dimethoxy cinnamic acid clear 0
4-Nitrocinnamic acid cloudy 0
Table 2 - Results of the Chicago Blue Assay at pH 7.0
Potential Mediator (0.1 micromole/ml Appearance ΔmA610 in water (3 min
None clear 0
Hardwood black liquor (150 ul, 12%) yellow 358
Lignin, organosolv (20ug/ml) clear, yellow 218
Ligninsulfonic acid (20ug/ml) clear 18
2-Aminopyridine light brown 2
N-Benzylidenebenzylamine clear 2
Example 3 - Combination of laccases and xylanases using N-benzylidenebenzylamine to enhance the bleaching of Chicago Blue at pH 7.0.
In the following example, the enzyme enhancing agent N-benzylidenebenzylamine was used as a mediator for a laccase to enhance the bleaching of Chicago Blue at pH 7.0 in the presence of a laccase and a xylanase.
The activity of the xylanase (Pulpzyme HC, Novozymes A/S) is 1000 units per ml enzyme solution. One xylanase unit is defined as the amount of enzyme which, under standard conditions (pH 9.0, 50°C, 30 minutes of incubation), release one micromole of the dye from a dyed RBB xylan.
N-Benzylidenebenzylamine was dissolved in ethanol and then mixed with a phosphate buffer and a Chicago Blue solution. A solution of laccase (NS51003, Novozymes A S) and xylanase (Pulpzyme HC, Novozymes A/S) was added to make 1 ml of the final solution,
containing 20 uM of the mediator, 20 mM buffer at pH 7.0 and Chicago Blue solution, with absorbance at A610 nm between 0.6 to 0.8. After the enzyme was added, the change in the absorbance was measured immediately using a UV spectrophotometer (UV-1201, Shimadzu Scientific Instruments). The decrease in absorbance was recorded after 3 minutes and was used to estimate the results of bleaching. The results are shown below.
It is to be understood that the above described embodiments are illustrative only and that modification throughout may occur to one skilled in the art. For example, a person of skill in the art will recognize that the mediators of the invention also include mediators which are functionally equivalent to the mediators specifically recited herein, such equivalents having minor structural variations such as the addition of a methyl or ethyl substituent or the formation of a methyl ester from a carboxyhc acid. Accordingly, this invention is not to be regarded as limited to the embodiments disclosed herein.
Claims
CLAIMS:
What is claimed is:
L A composition comprising an enzyme exhibiting laccase activity and an enzyme enhancing agent selected from:
(i) a monomer, dimer, or oligomer of at least one of:
R][ is OCH3, H, or another moiety; R2 is OCH3, H, or another moiety; R3 is OH, sulfonate, or another moiety;
R4 is an OH or methylene that connects to another monomer; and R5 is SO3H or H;
(ii) N-benzylidene benzylamine or a substituted N-benzylidene benzylamine having the structure:
wherein:
R6 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; and R7 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; (iii) a derivative of cinnamic acid having the structure: 
wherein: R8 is OCH3, NH2, Cl, NH(CH3)2; and 
(vi) salicylic acid; (v) epigallocatechin gallate; (vi) melamine; and (vii) 3,4-dihydroxybenzyl alcohol or a substituted 3, 4-dihydroxybenzyl alcohol.
2. The composition of claim 1 wherein said enzyme exhibiting laccase activity is selected from a laccase enzyme of enzyme classification EC 1.10.3.2, a catechol oxidase enzyme of enzyme classification EC 1.10.3.1, a monophenol monooxygenase enzyme of enzyme classification EC 1.14.99.1, a bilirubin oxidase enzyme of enzyme classification EC 1.3.3.5, and an ascorbate oxidase enzyme of enzyme classification EC 1.10.3.3.
3. The composition of claim 1 that further comprises a hydrolase.
4. The composition of claim 3 wherein said hydrolase is a xylanase.
5. The composition of claim 1 wherein said monomer, dimer, or oligomer is an organic soluble fraction of lignin or a lignin sulfonate.
6. The composition of claim 1 wherein said derivative of cinnamic acid is selected from:
4-(dimethylamino)cinnamic acid; 3 -hydroxy-4-methyoxy cinnamic acid; 4-aminocinnamic acid; and 4-chlorocinnamic acid.
7. A process for oxidizing a substrate, comprising treating the substrate with a composition comprising an enzyme exhibiting laccase activity and an enzyme enhancing agent selected from: (i) a monomer, dimer, or oligomer of at least one of:
Rj is OCH3, H, or another moiety; R2 is OCH3, H, or another moiety;
R3 is OH, sulfonate, or another moiety;
R4 is an OH or methylene that connects to another monomer; and
R5 is SO3H or H;
(ii) N-benzylidene benzylamine or a substituted N-benzylidene benzylamine having the structure:
wherein:
R6 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; and R7 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; (iii) a derivative of cinnamic acid having the structure:
R8 is OCH3, NH2, Cl, NH(CH3)2; and 
(vi) salicylic acid;
(v) epigallocatechin gallate;
(vi) melamine; and
(vii) 3,4-dihydroxybenzyl alcohol or a substituted 3, 4-dihydroxybenzyl alcohol.
8. The process of claim 7 wherein said enzyme exhibiting laccase activity is selected from a laccase enzyme of enzyme classification EC 1.10.3.2, a catechol oxidase enzyme of enzyme classification EC 1.10.3.1, a monophenol monooxygenase enzyme of enzyme classification EC 1.14.99.1, a bilirubin oxidase enzyme of enzyme classification EC 1.3.3.5, and an ascorbate oxidase enzyme of enzyme classification EC 1.10.3.3.
9. The process of claim 7 wherein said treating further includes a hydrolase.
10. The process of claim 9 wherein said hydrolase is a xylanase.
11. The process of claim 7 wherein said monomer, dimer, or oligomer is an organic soluble fraction of lignin or a lignin sulfonate.
12. The process of claim 7 wherein said derivative of cinnamic acid is selected from: 4- (dimethylamino)cinnamic acid; 3-hydroxy-4-methyoxycinnamic acid; 4-aminocinnamic acid; and 4-chlorocinnamic acid.
13. The process of claim 7 that further comprises adding an oxidizing agent.
14. The process of claim 13 wherein said oxidizing agent is at least one of air, oxygen, and hydrogen peroxide.
15. A process for bleaching a lignin-containing material, comprising treating the material with an enzyme exhibiting laccase activity and an enzyme enhancing agent selected from:
(i) a monomer, dimer, or oligomer of at least one of:
R2 is OCH3, H, or another moiety; R3 is OH, sulfonate, or another moiety;
R4 is an OH or methylene that connects to another monomer; and R5 is SO3H or H; (ii) N-benzylidene benzylamine or a substituted N-benzylidene benzylamine having the structure:
wherein:
R6 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; and R7 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; (iii) a derivative of cinnamic acid having the structure:
R8 is OCH3, NH2, Cl, NH(CH3)2; and Rj is OH or H; (vi) salicylic acid;
(v) epigallocatechin gallate; (vi) melamine;
(vii) 3,4-dihydroxybenzyl alcohol or a substituted 3.4-dihydroxybenzyl alcohol; (viii) a hardwood black liquor; (ix) a hardwood black liquor that comprises (i) said monomer, dimer, or oligomer;
(x) a softwood black liquor; and (xi) a softwood black liquor that comprises (i) said monomer, dimer, or oligomer.
16. The process of claim 15 wherein said enzyme exhibiting laccase activity is selected from a laccase enzyme of enzyme classification EC 1.10.3.2, a catechol oxidase enzyme of enzyme classification EC 1.10.3.1, amonophenol monooxygenase enzyme of enzyme classification EC 1.14.99.1, a bilirubin oxidase enzyme of enzyme classification EC 1.3.3.5, and an ascorbate oxidase enzyme of enzyme classification EC 1.10.3.3.
17. The process of claim 15 wherein said treating further includes a hydrolase.
18. The process of claim 17 wherein said hydrolase is a xylanase.
19. The process of claim 15 wherein said monomer, dimer, or oligomer is an organic soluble fraction of lignin or a lignin sulfonate.
20. The process of claim 15 wherein said derivative of cinnamic acid is selected from: 4- (dimethylamino)cinnamic acid; 3-hydroxy-4-methyoxycinnamic acid; 4-aminocinnamic acid; and 4-chlorocinnamic acid.
21. The process of claim 15 that further comprises adding an oxidizing agent.
22. The process of claim 21 wherein said oxidizing agent is at least one of air, oxygen, and hydrogen peroxide.
23. The process of claim 15 wherein said material is a wood pulp.
24. The process of claim 23 wherein said wood pulp is a raw material used to form a cellulose or a cellulose derivative.
25. A process for enhancing the activity of an enzyme exhibiting laccase activity, comprising adding an enzyme enhancing agent to said enzyme, wherein said enzyme enhancing agent is selected from: (i) a monomer, dimer, or oligomer of at least one of:
Ri is OCH3, H, or another moiety; R2 is OCHj, H, or another moiety;
R3 is OH, sulfonate, or another moiety;
R4 is an OH or methylene that connects to another monomer; and
R5 is SO3H or H;
(ii) N-benzylidene benzylamine or a substituted N-benzylidene benzylamine having the structure: 
wherein:
R6 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; and R7 is H, OCH3, NH(CH3)2, Cl, Br, an aliphatic group, or an aromatic group; (iii) a derivative of cinnamic acid having the structure:
wherein:
R8 is OCH3, NH2, Cl, NH(CH3)2; and 
(vi) salicylic acid;
(v) epigallocatechin gallate;
(vi) melamine;
(vii) 3,4-dihydroxybenzyl alcohol or a substituted 3.4-dihydroxylbenzyl alcohol; (viii) a hardwood black liquor;
(ix) a hardwood black liquor that comprises (i) said monomer, dimer, or oligomer;
(x) a softwood black liquor; and
(xi) a softwood black liquor that comprises (i) said monomer, dimer, or oligomer.
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US31829101P | 2001-09-10 | 2001-09-10 | |
| US60/318,291 | 2001-09-10 | ||
| US10/027,166 US20030096394A1 (en) | 2001-09-10 | 2001-12-20 | Laccase activity enhancers |
| US10/027,166 | 2001-12-20 |
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| Publication Number | Publication Date |
|---|---|
| WO2003023043A1 true WO2003023043A1 (en) | 2003-03-20 |
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| PCT/US2002/018540 WO2003023043A1 (en) | 2001-09-10 | 2002-06-07 | Laccase activity enhancers |
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| WO (1) | WO2003023043A1 (en) |
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| USRE45660E1 (en) | 2006-02-14 | 2015-09-01 | Bp Corporation North America Inc. | Xylanases, nucleic acids encoding them and methods for making and using them |
| BRPI0817811A2 (en) | 2007-10-03 | 2014-10-14 | Verenium Corp | Xylanases, nucleic acids that encode the same and methods for the manufacture and use of the same. |
| PL2238242T3 (en) | 2008-01-03 | 2015-06-30 | Basf Enzymes Llc | Transferases and oxidoreductases, nucleic acids encoding them and methods for making and using them |
| CN101957315B (en) * | 2010-09-11 | 2012-02-15 | 大连工业大学 | Method for measuring lignin content in black liquor |
| US9663899B2 (en) * | 2015-08-26 | 2017-05-30 | Solenis Technologies, L.P. | Method for making lignocellulosic paper and paper product |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5885304A (en) * | 1993-06-29 | 1999-03-23 | Novo Nordisk A/S | Enhancement of laccase reactions |
| US5912405A (en) * | 1994-09-27 | 1999-06-15 | Novo Nordisk A/S | Enhancers such as acetosyringone |
| US6200786B1 (en) * | 1999-09-08 | 2001-03-13 | Givaudan S.A. | Process for the preparation of nootkatone by laccase catalysis |
| US6242245B1 (en) * | 1997-09-26 | 2001-06-05 | Consortium für elektrochemische Industrie GmbH | Multicomponent system for modifying, degrading or bleaching lignin or lignin-containing materials, and processes for its use |
-
2001
- 2001-12-20 US US10/027,166 patent/US20030096394A1/en not_active Abandoned
-
2002
- 2002-06-07 WO PCT/US2002/018540 patent/WO2003023043A1/en not_active Application Discontinuation
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5885304A (en) * | 1993-06-29 | 1999-03-23 | Novo Nordisk A/S | Enhancement of laccase reactions |
| US5912405A (en) * | 1994-09-27 | 1999-06-15 | Novo Nordisk A/S | Enhancers such as acetosyringone |
| US6242245B1 (en) * | 1997-09-26 | 2001-06-05 | Consortium für elektrochemische Industrie GmbH | Multicomponent system for modifying, degrading or bleaching lignin or lignin-containing materials, and processes for its use |
| US6200786B1 (en) * | 1999-09-08 | 2001-03-13 | Givaudan S.A. | Process for the preparation of nootkatone by laccase catalysis |
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