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Volumn 67, Issue 2, 2005, Pages 160-169

Production and applications of esterases

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANTS; DEGRADATION; ESTERS; INDUSTRIAL EMISSIONS; PLASTICS; POLLUTION; SYNTHESIS (CHEMICAL); TOXIC MATERIALS;

EID: 17944374832     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-004-1840-y     Document Type: Article
Times cited : (243)

References (118)
  • 1
    • 17944363192 scopus 로고    scopus 로고
    • Update on antiviral agents, California
    • Abbott JC (2001) Update on antiviral agents, California. J Health Syst Pharmacy July/August 6
    • (2001) J Health Syst Pharmacy , vol.JULY-AUGUST 6
    • Abbott, J.C.1
  • 2
    • 0029294737 scopus 로고
    • Characterization of salivary gland-specific esterase in the vector mosquito, Aedes aegypti
    • Argentine JA, James AA (1995) Characterization of salivary gland-specific esterase in the vector mosquito, Aedes aegypti. Insect Biochem Mol Biol 25:621-630
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 621-630
    • Argentine, J.A.1    James, A.A.2
  • 4
    • 0001548913 scopus 로고
    • Purification et properties de la pectinesterase produite par Aspergillus niger
    • Baron A, Rombouts F, Drilleau JF, Pilnik W (1980) Purification et properties de la pectinesterase produite par Aspergillus niger. Lebensm Wiss Technol 13:330-333
    • (1980) Lebensm Wiss Technol , vol.13 , pp. 330-333
    • Baron, A.1    Rombouts, F.2    Drilleau, J.F.3    Pilnik, W.4
  • 5
    • 0034453325 scopus 로고    scopus 로고
    • Rapid screening of hydrolases for the enantioselective conversion of difficult-to-resolve substrates
    • Baumann M, Hauer H, Bornscheuer UT (2000) Rapid screening of hydrolases for the enantioselective conversion of difficult-to-resolve substrates. Tetrahedron Asymm 11:4781-4790
    • (2000) Tetrahedron Asymm , vol.11 , pp. 4781-4790
    • Baumann, M.1    Hauer, H.2    Bornscheuer, U.T.3
  • 7
    • 0141425540 scopus 로고    scopus 로고
    • Mapping and sequencing of acetylcholinesterase genes from the platyhelminth blood fluke Schistosoma
    • Bentley GN, Jones AK, Agnew A (2003) Mapping and sequencing of acetylcholinesterase genes from the platyhelminth blood fluke Schistosoma. Gene 314:103-112
    • (2003) Gene , vol.314 , pp. 103-112
    • Bentley, G.N.1    Jones, A.K.2    Agnew, A.3
  • 8
    • 0030569312 scopus 로고    scopus 로고
    • Substrate specificity and mode of action of acetyl-xylan esterase from Streptomyces lividans
    • Biely P, Cote GL, Kremnieky L, Greene RV, Dupont C, Kluepfel D (1996) Substrate specificity and mode of action of acetyl-xylan esterase from Streptomyces lividans. FEBS Lett 396:257-260
    • (1996) FEBS Lett , vol.396 , pp. 257-260
    • Biely, P.1    Cote, G.L.2    Kremnieky, L.3    Greene, R.V.4    Dupont, C.5    Kluepfel, D.6
  • 9
    • 0037421326 scopus 로고    scopus 로고
    • Enzymatic desymmetrization of a centrosymmetric diacetate
    • Bohm C, Austin WF, Trauner D (2003) Enzymatic desymmetrization of a centrosymmetric diacetate. Tetrahedron Assym 14:71-74
    • (2003) Tetrahedron Assym , vol.14 , pp. 71-74
    • Bohm, C.1    Austin, W.F.2    Trauner, D.3
  • 10
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxylesterases: Classification, properties and application in biocatalyses
    • Bornscheuer UT (2002) Microbial carboxylesterases: classification, properties and application in biocatalyses. FEMS Microbiol Rev 26:73-81
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 73-81
    • Bornscheuer, U.T.1
  • 12
    • 0028904919 scopus 로고
    • Characterization of uptake and hydrolysis of fluorescein diacetate and carboxyfluorescein diacetate by intracellular esterases in Saccharomyces cerevisiae, which result in accumulation of fluorescent product
    • Breeuwer P, Drocourt JL, Bunschoten N, Zwietering MH, Rombouts FM, Abee T (1995) Characterization of uptake and hydrolysis of fluorescein diacetate and carboxyfluorescein diacetate by intracellular esterases in Saccharomyces cerevisiae, which result in accumulation of fluorescent product. Appl Environ Microbiol 61:1614-1619
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1614-1619
    • Breeuwer, P.1    Drocourt, J.L.2    Bunschoten, N.3    Zwietering, M.H.4    Rombouts, F.M.5    Abee, T.6
  • 13
    • 0142199918 scopus 로고    scopus 로고
    • Characterisation of choline esterases and their tissue and subcellular distribution in mussel (Mytilus edulis)
    • Brown M, Davies IM, Moffat CF, Redshaw J, Craft JA (2004) Characterisation of choline esterases and their tissue and subcellular distribution in mussel (Mytilus edulis). Marine Environ Res 57:155-169
    • (2004) Marine Environ Res , vol.57 , pp. 155-169
    • Brown, M.1    Davies, I.M.2    Moffat, C.F.3    Redshaw, J.4    Craft, J.A.5
  • 15
    • 0021753566 scopus 로고
    • Preparative production of optically active esters and alcohols using esterase-catalysed stereospecific transesterification in organic media
    • Campon B, Kilbanon AM (1984) Preparative production of optically active esters and alcohols using esterase-catalysed stereospecific transesterification in organic media. J Am Chem Soc 106:2687-2692
    • (1984) J Am Chem Soc , vol.106 , pp. 2687-2692
    • Campon, B.1    Kilbanon, A.M.2
  • 16
    • 0029782799 scopus 로고    scopus 로고
    • Enzymatic synthesis of geraniol esters in a solvent free system by lipases
    • Chaabouni MK, Pulvin S, Touraud D, Thomas D (1996) Enzymatic synthesis of geraniol esters in a solvent free system by lipases. Biotechnol Lett 18:1083-1088
    • (1996) Biotechnol Lett , vol.18 , pp. 1083-1088
    • Chaabouni, M.K.1    Pulvin, S.2    Touraud, D.3    Thomas, D.4
  • 18
    • 17944362071 scopus 로고    scopus 로고
    • Neural pathways transducing pain, non-narcotic analgesics
    • Chavkin C (2004) Neural pathways transducing pain, non-narcotic analgesics. Pharmacology 402/512:153-154
    • (2004) Pharmacology , vol.402-512 , pp. 153-154
    • Chavkin, C.1
  • 19
    • 0034786380 scopus 로고    scopus 로고
    • Culture conditions for the production of esterase from Lactobacillus casei CL 96
    • Choi YJ, Lee BH (2001) Culture conditions for the production of esterase from Lactobacillus casei CL 96. Bioprocess Biosyst Eng 24:59-63
    • (2001) Bioprocess Biosyst Eng , vol.24 , pp. 59-63
    • Choi, Y.J.1    Lee, B.H.2
  • 21
    • 0033179577 scopus 로고    scopus 로고
    • The same aminoacid substitution in orthologous esterases confers organophosphate resistance on the house fly and a blowfly
    • Claudianos C, Russell R, Oakeshott JG (1999) The same aminoacid substitution in orthologous esterases confers organophosphate resistance on the house fly and a blowfly. Insect Biochem Mol Biol 29:675-686
    • (1999) Insect Biochem Mol Biol , vol.29 , pp. 675-686
    • Claudianos, C.1    Russell, R.2    Oakeshott, J.G.3
  • 23
    • 12244270398 scopus 로고    scopus 로고
    • Engineering of the metabolism of Saccharomyces cerevisae for anaerobic production of mannitol
    • Costenoble R, Adler L, Nikiasson C, Lideh G (2003) Engineering of the metabolism of Saccharomyces cerevisae for anaerobic production of mannitol. FEMS Yeast Res 3:17-325
    • (2003) FEMS Yeast Res , vol.3 , pp. 17-325
    • Costenoble, R.1    Adler, L.2    Nikiasson, C.3    Lideh, G.4
  • 24
    • 0033910674 scopus 로고    scopus 로고
    • The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity
    • Degrassi G, Kojic M, Ljubijankic G, Venturi V (2000) The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity. Microbiology 146:1585-1591
    • (2000) Microbiology , vol.146 , pp. 1585-1591
    • Degrassi, G.1    Kojic, M.2    Ljubijankic, G.3    Venturi, V.4
  • 25
    • 0024655878 scopus 로고
    • Enzymatic catalysis in monophasic solvent
    • Dodrick JS (1989) Enzymatic catalysis in monophasic solvent. Enzyme Microbiol Technol 11:194-211
    • (1989) Enzyme Microbiol Technol , vol.11 , pp. 194-211
    • Dodrick, J.S.1
  • 26
    • 17944362374 scopus 로고    scopus 로고
    • Influence of yeast strain and fermentation conditions on yeast esterase activities
    • Dufour JP, Bing Y (2001) Influence of yeast strain and fermentation conditions on yeast esterase activities. Brew Dig 76:44
    • (2001) Brew Dig , vol.76 , pp. 44
    • Dufour, J.P.1    Bing, Y.2
  • 27
    • 17944380577 scopus 로고
    • Stereospecific hetero-bicyclic alcohol enantiomer preparation. European Patent 605033
    • Duphar-Int Res (1994) Stereospecific hetero-bicyclic alcohol enantiomer preparation. European Patent 605033
    • (1994)
  • 29
    • 1642411072 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two thermostable carboxylesterases from Geobacillus stearothermophillus
    • Ewis HE, Abdelal AT, Lu C-D (2004) Molecular cloning and characterization of two thermostable carboxylesterases from Geobacillus stearothermophillus. Gene 329:187-195
    • (2004) Gene , vol.329 , pp. 187-195
    • Ewis, H.E.1    Abdelal, A.T.2    Lu, C.-D.3
  • 30
    • 0031710284 scopus 로고    scopus 로고
    • Balance of activities of alcohol acetyltransferase and esterase in Saccharomyces cerevisiae is important for production of isoamyl acetate
    • Fakuda K, Yamamoto N, Kiyokawa Y, Yanagiuchi T, Wakai Y, Kitamoto K, Inoue Y, Kimura A (1998) Balance of activities of alcohol acetyltransferase and esterase in Saccharomyces cerevisiae is important for production of isoamyl acetate. Appl Environ Microbiol 64:4076-4078
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4076-4078
    • Fakuda, K.1    Yamamoto, N.2    Kiyokawa, Y.3    Yanagiuchi, T.4    Wakai, Y.5    Kitamoto, K.6    Inoue, Y.7    Kimura, A.8
  • 31
    • 0035992170 scopus 로고    scopus 로고
    • Cholinesterase activity and effects of its inhibition by neurotoxic drugs in Dicotyostelium discoideum
    • Falugi C, Amaroli A, Evangelisti V, Viarengo A, Corrado MUD (2002) Cholinesterase activity and effects of its inhibition by neurotoxic drugs in Dicotyostelium discoideum. Chemosphere 48:407-414
    • (2002) Chemosphere , vol.48 , pp. 407-414
    • Falugi, C.1    Amaroli, A.2    Evangelisti, V.3    Viarengo, A.4    Corrado, M.U.D.5
  • 33
    • 0742288326 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular tributyrin esterase produced by a cheese isolate, Micrococcus sp. INIA 528
    • Fernandez J, Mohedano AF, Fernandez-Garcia E, Medina M, Nunez M (2004) Purification and characterization of an extracellular tributyrin esterase produced by a cheese isolate, Micrococcus sp. INIA 528. Int Dairy J 14:135-142
    • (2004) Int Dairy J , vol.14 , pp. 135-142
    • Fernandez, J.1    Mohedano, A.F.2    Fernandez-Garcia, E.3    Medina, M.4    Nunez, M.5
  • 34
    • 0033214507 scopus 로고    scopus 로고
    • A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose binding cellulase- Hemi-cellulase complex
    • Fillingham IJ, Kroon PA, Williamson G, Gilbert HJ, Hazlewood GP (1999) A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose binding cellulase- hemi-cellulase complex. Biochem J 343:215-224
    • (1999) Biochem J , vol.343 , pp. 215-224
    • Fillingham, I.J.1    Kroon, P.A.2    Williamson, G.3    Gilbert, H.J.4    Hazlewood, G.P.5
  • 35
    • 0347761353 scopus 로고    scopus 로고
    • Mutual influence of cholesterol esterase and pseudocholinesterase on the biodegradation of dental composites
    • Finer Y, Jaffer F, Santerre JP (2004) Mutual influence of cholesterol esterase and pseudocholinesterase on the biodegradation of dental composites. Biomaterials 25:1787-1793
    • (2004) Biomaterials , vol.25 , pp. 1787-1793
    • Finer, Y.1    Jaffer, F.2    Santerre, J.P.3
  • 37
    • 17644432629 scopus 로고    scopus 로고
    • Cloning, purification and properties of a hyperthermophilic esterase from archaeon Aerophyrum pernix KL
    • Gao R, Feng Y, Ishikana K, Ishida H, Ando S, Kosugi Y, Cao S (2003) Cloning, purification and properties of a hyperthermophilic esterase from archaeon Aerophyrum pernix KL. J Mol Catal B 24-25:1-8
    • (2003) J Mol Catal B , vol.24-25 , pp. 1-8
    • Gao, R.1    Feng, Y.2    Ishikana, K.3    Ishida, H.4    Ando, S.5    Kosugi, Y.6    Cao, S.7
  • 39
    • 0025874845 scopus 로고
    • Crystallization and preliminary diffraction analysis of cholesterol esterase from Candida cylindrcea
    • Ghosh D, Erman M, Duax WL (1991) Crystallization and preliminary diffraction analysis of cholesterol esterase from Candida cylindrcea. J Steroid Biochem Mol Biol 38:663-666
    • (1991) J Steroid Biochem Mol Biol , vol.38 , pp. 663-666
    • Ghosh, D.1    Erman, M.2    Duax, W.L.3
  • 42
  • 43
    • 3042543369 scopus 로고    scopus 로고
    • Characterizations of general esterases in relation to malathion susceptibility in two field populations of the oriental migratory locust, Locusta migratoria manilensis (Meyen)
    • He YP, Ma EB, Zhu KY (2004) Characterizations of general esterases in relation to malathion susceptibility in two field populations of the oriental migratory locust, Locusta migratoria manilensis (Meyen). Pesticide Biochem Physiol 78:103-113
    • (2004) Pesticide Biochem Physiol , vol.78 , pp. 103-113
    • He, Y.P.1    Ma, E.B.2    Zhu, K.Y.3
  • 46
    • 0037210701 scopus 로고    scopus 로고
    • Esterases from B. subtilis and B. stearothermophilis share high sequence homology but differ substantially in their properties
    • Henke E, Bornscheuer UT (2002) Esterases from B. subtilis and B. stearothermophilis share high sequence homology but differ substantially in their properties. Appl Microbiol Biotechnol 60:320-326
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 320-326
    • Henke, E.1    Bornscheuer, U.T.2
  • 47
    • 0038236305 scopus 로고    scopus 로고
    • A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases
    • Henke E, Bornscheuer UT, Schmit RD, Pleiss J (2003) A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases. Chembiochem 6:485-493
    • (2003) Chembiochem , vol.6 , pp. 485-493
    • Henke, E.1    Bornscheuer, U.T.2    Schmit, R.D.3    Pleiss, J.4
  • 49
    • 0038814072 scopus 로고    scopus 로고
    • Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3-bromo-2-methylpropanoate and ethyl 3-phenylbutyrate
    • Horsman GP, Liu AM, Henke E, Bornscheuer UT, Kazlauskas RJ (2003) Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3-bromo-2-methylpropanoate and ethyl 3-phenylbutyrate. Chemistry 9:1933-1939
    • (2003) Chemistry , vol.9 , pp. 1933-1939
    • Horsman, G.P.1    Liu, A.M.2    Henke, E.3    Bornscheuer, U.T.4    Kazlauskas, R.J.5
  • 50
    • 0010510562 scopus 로고    scopus 로고
    • Cloning, nucleotide, sequencing and characterization of a polyurethanase gene (pueB) from Pseudomonas chlororaphis
    • Howard GT, Crother B, Vicknair J (2001) Cloning, nucleotide, sequencing and characterization of a polyurethanase gene (pueB) from Pseudomonas chlororaphis. Int Biodeterior Biodegrad 47:141-149
    • (2001) Int Biodeterior Biodegrad , vol.47 , pp. 141-149
    • Howard, G.T.1    Crother, B.2    Vicknair, J.3
  • 51
    • 0037450115 scopus 로고    scopus 로고
    • Ferulic acid esterase from Humicola insolens catalyses enantioselective transesterification of secondary alcohols
    • Htzakis NS, Daphnomili D, Smonou L (2003) Ferulic acid esterase from Humicola insolens catalyses enantioselective transesterification of secondary alcohols. J Mol Catal B 21:309-311
    • (2003) J Mol Catal B , vol.21 , pp. 309-311
    • Htzakis, N.S.1    Daphnomili, D.2    Smonou, L.3
  • 53
    • 0037209912 scopus 로고    scopus 로고
    • The influence of protein adsorption and surface modifying macromolecules on the hydrolytic degradation of a poly (ether-urethane) by cholesterol esterase
    • Jahangir R, Mc Closkey CB, Mc Clung WG, Labow RS, Brash JL, Santerre JP (2003) The influence of protein adsorption and surface modifying macromolecules on the hydrolytic degradation of a poly (ether-urethane) by cholesterol esterase. Biomaterials 24:121-130
    • (2003) Biomaterials , vol.24 , pp. 121-130
    • Jahangir, R.1    Mc Closkey, C.B.2    Mc Clung, W.G.3    Labow, R.S.4    Brash, J.L.5    Santerre, J.P.6
  • 54
    • 0035916872 scopus 로고    scopus 로고
    • Quantitative screening method for hydrolases in microplates using pH indicators: Determination of kinetic parameters by dynamic monitoring
    • John GT, Heinzle E (2000) Quantitative screening method for hydrolases in microplates using pH indicators: Determination of kinetic parameters by dynamic monitoring. Biotechnol Bioeng 72:620-627
    • (2000) Biotechnol Bioeng , vol.72 , pp. 620-627
    • John, G.T.1    Heinzle, E.2
  • 55
    • 0035735155 scopus 로고    scopus 로고
    • High-level production of recombinant Aspergillus niger cinnamoyal esterase (FAEA) in the methylotrophic yeast Pichia pastoris
    • Juge N, Williamson G, Puuigserver A, Cummings NJ, Connerton IF, Faulds CB (2001) High-level production of recombinant Aspergillus niger cinnamoyal esterase (FAEA) in the methylotrophic yeast Pichia pastoris. FEMS Yeast Res 1:127-132
    • (2001) FEMS Yeast Res , vol.1 , pp. 127-132
    • Juge, N.1    Williamson, G.2    Puuigserver, A.3    Cummings, N.J.4    Connerton, I.F.5    Faulds, C.B.6
  • 56
    • 0242575084 scopus 로고    scopus 로고
    • Nonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1
    • Jung YJ, Lee JK, Sung CG, Oh TK, Kim HK (2003) Nonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1. J Mol Catal B 26:223-229
    • (2003) J Mol Catal B , vol.26 , pp. 223-229
    • Jung, Y.J.1    Lee, J.K.2    Sung, C.G.3    Oh, T.K.4    Kim, H.K.5
  • 57
    • 0342646950 scopus 로고    scopus 로고
    • Characterization of a new thermo stable esterase from the moderate thermophilic bacterium Bacillus circulans
    • Kademi A, Abdelkader NA, Fakhreddine L, Baratti JC (2000) Characterization of a new thermo stable esterase from the moderate thermophilic bacterium Bacillus circulans. J Mol Catal B 10:395-401
    • (2000) J Mol Catal B , vol.10 , pp. 395-401
    • Kademi, A.1    Abdelkader, N.A.2    Fakhreddine, L.3    Baratti, J.C.4
  • 58
    • 17944364756 scopus 로고
    • New stereospecific 5-acyloxymethyl-oxazolidin-2-one derivative. Patent J03108498
    • Kanegafuchi Chem (1991) New stereospecific 5-acyloxymethyl-oxazolidin-2- one derivative. Patent J03108498
    • (1991)
  • 60
    • 0033869460 scopus 로고    scopus 로고
    • The effect of physical and chemical treatments on the esterase activity from Pseudomonas fragi CRDA 037
    • Kermasha S, Bisakowski B, Ismail S, Morin A (2000) The effect of physical and chemical treatments on the esterase activity from Pseudomonas fragi CRDA 037. Food Res Int 33:767-774
    • (2000) Food Res Int , vol.33 , pp. 767-774
    • Kermasha, S.1    Bisakowski, B.2    Ismail, S.3    Morin, A.4
  • 61
    • 0037034738 scopus 로고    scopus 로고
    • Screening, production and properties of a stereo specific esterase from pseudomonas species-34 with high selectivity to (S)-ketoprofen ethyl ester
    • Kim GJ, Choi GS, Kim JY, Lee JB, Jo DH, Ryu YW (2002a) Screening, production and properties of a stereo specific esterase from pseudomonas species-34 with high selectivity to (S)-ketoprofen ethyl ester. J Mol Catal B 17:29-38
    • (2002) J Mol Catal B , vol.17 , pp. 29-38
    • Kim, G.J.1    Choi, G.S.2    Kim, J.Y.3    Lee, J.B.4    Jo, D.H.5    Ryu, Y.W.6
  • 62
    • 0037035419 scopus 로고    scopus 로고
    • Purification and characterization of an erythromycin resistant Pseudomonas sp. GD 100
    • Kim YH, Cha CJ, Cerniglia CE (2002b) Purification and characterization of an erythromycin resistant Pseudomonas sp. GD 100. FEMS Microbiol Lett 210:239-244
    • (2002) FEMS Microbiol Lett , vol.210 , pp. 239-244
    • Kim, Y.H.1    Cha, C.J.2    Cerniglia, C.E.3
  • 63
    • 1242315610 scopus 로고    scopus 로고
    • Occurrence of ofloxacin ester hydrolyzing esterase from Bacillus niacini EM001
    • Kim HK, Na HS, Park MS, Oh TK, Lee TS (2004) Occurrence of ofloxacin ester hydrolyzing esterase from Bacillus niacini EM001. J Mol Catal B 27:237-241
    • (2004) J Mol Catal B , vol.27 , pp. 237-241
    • Kim, H.K.1    Na, H.S.2    Park, M.S.3    Oh, T.K.4    Lee, T.S.5
  • 65
    • 0032524178 scopus 로고    scopus 로고
    • Characterization and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens
    • Krebsfanger N, Zocher F, Altenbuchner J, Bornscheuer UT (1998) Characterization and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens. Enzyme Microb Technol 22:641-646
    • (1998) Enzyme Microb Technol , vol.22 , pp. 641-646
    • Krebsfanger, N.1    Zocher, F.2    Altenbuchner, J.3    Bornscheuer, U.T.4
  • 66
    • 0033679102 scopus 로고    scopus 로고
    • A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate biding module
    • Kroon PA, Williamson G, Fish NM, Archer DB, Belshaw NJ (2000) A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate biding module. Eur J Biochem 267:6740-6752
    • (2000) Eur J Biochem , vol.267 , pp. 6740-6752
    • Kroon, P.A.1    Williamson, G.2    Fish, N.M.3    Archer, D.B.4    Belshaw, N.J.5
  • 67
    • 1242284208 scopus 로고    scopus 로고
    • Cold-active esterase from Psychrobacter sp. Ant300: Gene cloning, characterization and the effects of Gly → Pro substitution near the active site on its catalytic activity and stability
    • Kulakova L, Galkin A, Nakayama T, Nishino T, Esaki N (2004) Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization and the effects of Gly → Pro substitution near the active site on its catalytic activity and stability. Biochim Biophys Acta 1696:59-65
    • (2004) Biochim Biophys Acta , vol.1696 , pp. 59-65
    • Kulakova, L.1    Galkin, A.2    Nakayama, T.3    Nishino, T.4    Esaki, N.5
  • 68
    • 0346094143 scopus 로고    scopus 로고
    • Effects of caffeine and used coffee grounds on biological features of Aedes aegypti (Diptera, Culicidae) and their possible use in alternative control
    • Laranja AT, Manzatto AJ, de C Bicudo HEM (2003) Effects of caffeine and used coffee grounds on biological features of Aedes aegypti (Diptera, Culicidae) and their possible use in alternative control. Genetics Mol Biol 26:419-429
    • (2003) Genetics Mol Biol , vol.26 , pp. 419-429
    • Laranja, A.T.1    Manzatto, A.J.2    De C Bicudo, H.E.M.3
  • 70
    • 3543112653 scopus 로고    scopus 로고
    • Homologous expression of the feruloyl esterase B gene from Aspergillus niger and the characterization of the recombinant enzyme
    • Levassenr A, Benoit I, Asther M, Record E (2004) Homologous expression of the feruloyl esterase B gene from Aspergillus niger and the characterization of the recombinant enzyme. Purification 37:126-133
    • (2004) Purification , vol.37 , pp. 126-133
    • Levassenr, A.1    Benoit, I.2    Asther, M.3    Record, E.4
  • 71
    • 0035911359 scopus 로고    scopus 로고
    • Mapping the substrate selectivity of new hydrolases using colorimetric screening: Lipases from Bacillus thermocatenulatus and Ophiostoma piliferum, esterases from Pseudomonas fluorescens and Streptomyces diastatochromogenes
    • Liu AMF, Somers NA, Kazlauskas RJ, Brush TS, Zocher F, Enzelberger MM, Bornscheuer UT, Horsman GP, Mezzetti A, Schmidt-Dannert C, Schmid RD (2001) Mapping the substrate selectivity of new hydrolases using colorimetric screening: lipases from Bacillus thermocatenulatus and Ophiostoma piliferum, esterases from Pseudomonas fluorescens and Streptomyces diastatochromogenes. Tetrahedron Asymm 12:545-556
    • (2001) Tetrahedron Asymm , vol.12 , pp. 545-556
    • Liu, A.M.F.1    Somers, N.A.2    Kazlauskas, R.J.3    Brush, T.S.4    Zocher, F.5    Enzelberger, M.M.6    Bornscheuer, U.T.7    Horsman, G.P.8    Mezzetti, A.9    Schmidt-Dannert, C.10    Schmid, R.D.11
  • 72
    • 1242332877 scopus 로고    scopus 로고
    • Cell vitality and esterase activity of Saccharomyces cerevisiae is affected by increasing calcium concentration
    • Lomolino G, Rizzi C, Spettoli P, Curioni A, Lante A (2003) Cell vitality and esterase activity of Saccharomyces cerevisiae is affected by increasing calcium concentration. Biotechnology (Nov/Dec):32-35
    • (2003) Biotechnology , vol.NOV-DEC , pp. 32-35
    • Lomolino, G.1    Rizzi, C.2    Spettoli, P.3    Curioni, A.4    Lante, A.5
  • 74
    • 0033754307 scopus 로고    scopus 로고
    • Recombinant, catalytically inactive juvenile hormone esterase enhances efficacy of Baculovirus insecticides
    • Meer MMM van, Bonning BC, Ward VK, Vlak JM, Hammock BD (2000) Recombinant, catalytically inactive juvenile hormone esterase enhances efficacy of Baculovirus insecticides. Biol Control 19:191-199
    • (2000) Biol Control , vol.19 , pp. 191-199
    • Van Meer, M.M.M.1    Bonning, B.C.2    Ward, V.K.3    Vlak, J.M.4    Hammock, B.D.5
  • 75
    • 0030589108 scopus 로고    scopus 로고
    • Isolation of a novel carboxylesterase from Bacillus coagulans with high enantioselectivity toward racemic esters of 1,2-O-isopropylideneglycerol
    • Molinavi F, Brenna O, Valenti M, Aragozzini F (1996) Isolation of a novel carboxylesterase from Bacillus coagulans with high enantioselectivity toward racemic esters of 1,2-O-isopropylideneglycerol. Enzyme Microb Technol 19:551-556
    • (1996) Enzyme Microb Technol , vol.19 , pp. 551-556
    • Molinavi, F.1    Brenna, O.2    Valenti, M.3    Aragozzini, F.4
  • 76
    • 0037160540 scopus 로고    scopus 로고
    • A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: Cloning of the gene, characterization of the protein
    • Morana A, Prizito ND, Aurilia V, Rossi M, Cannio R (2002) A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: cloning of the gene, characterization of the protein. Gene 283:107-115
    • (2002) Gene , vol.283 , pp. 107-115
    • Morana, A.1    Prizito, N.D.2    Aurilia, V.3    Rossi, M.4    Cannio, R.5
  • 77
    • 1442335000 scopus 로고    scopus 로고
    • Recombinant porcine intestinal carboxylesterase: Cloning from the pig liver esterase gene by site-directed mutagenesis, functional expression and characterization
    • Musidlowska-Persson A, Bornscheuer UT (2003) Recombinant porcine intestinal carboxylesterase: cloning from the pig liver esterase gene by site-directed mutagenesis, functional expression and characterization. Protein Eng 16:1139-1145
    • (2003) Protein Eng , vol.16 , pp. 1139-1145
    • Musidlowska-Persson, A.1    Bornscheuer, U.T.2
  • 78
    • 0034319281 scopus 로고    scopus 로고
    • Inhibitory effects of carbohydrates on cholesterol esterase biosynthesis in Streptomyces lavendulae H646-SY2
    • Nishimura M, Inouye S (2000) Inhibitory effects of carbohydrates on cholesterol esterase biosynthesis in Streptomyces lavendulae H646-SY2. J Biosci Bioeng 90:564-566
    • (2000) J Biosci Bioeng , vol.90 , pp. 564-566
    • Nishimura, M.1    Inouye, S.2
  • 79
    • 0033486287 scopus 로고    scopus 로고
    • Carboxyl/cholinesterases: A case study of the evolution of a successful multigene family
    • Oakeshott JG, Claudianos C, Russell RJ, Robin GC (1999) Carboxyl/cholinesterases: a case study of the evolution of a successful multigene family. Bioessays 21:1031-1042
    • (1999) Bioessays , vol.21 , pp. 1031-1042
    • Oakeshott, J.G.1    Claudianos, C.2    Russell, R.J.3    Robin, G.C.4
  • 80
    • 0030525322 scopus 로고    scopus 로고
    • Production, isolation and partial characterization of lipase-esterase from Pediococcus pentosaceus SV61
    • Ostdal H, Baron CP, Blom H, Andersen HJ (1996) Production, isolation and partial characterization of lipase-esterase from Pediococcus pentosaceus SV61. Lebensm Wiss Technol 29:542-546
    • (1996) Lebensm Wiss Technol , vol.29 , pp. 542-546
    • Ostdal, H.1    Baron, C.P.2    Blom, H.3    Andersen, H.J.4
  • 81
    • 0031531659 scopus 로고    scopus 로고
    • Esterase catalysed region- and enantioselective hydrolysis of substituted carboxylases
    • Ozaki E, Sakashita K (1997) Esterase catalysed region- and enantioselective hydrolysis of substituted carboxylases. Chem Lett 8:741-742
    • (1997) Chem Lett , vol.8 , pp. 741-742
    • Ozaki, E.1    Sakashita, K.2
  • 82
    • 0028504610 scopus 로고
    • Cloning and expression of Pseudomonas putida esterase gene in Escherichia coli and its use in enzymatic production of D-β-acetylthioisobutyric acid
    • Ozaki E, Sakimae A, Numazawa R (1994) Cloning and expression of Pseudomonas putida esterase gene in Escherichia coli and its use in enzymatic production of D-β-acetylthioisobutyric acid. Biosci Biotechnol Biochem 58:1745-1746
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 1745-1746
    • Ozaki, E.1    Sakimae, A.2    Numazawa, R.3
  • 83
    • 0842308021 scopus 로고    scopus 로고
    • Recovery of acetylcholine esterase activity of Drawida willsi (Oligochaeta) following application of three pesticides to soil
    • Panda S, Sahu SK (2004) Recovery of acetylcholine esterase activity of Drawida willsi (Oligochaeta) following application of three pesticides to soil. Chemosphere 55:283-290
    • (2004) Chemosphere , vol.55 , pp. 283-290
    • Panda, S.1    Sahu, S.K.2
  • 85
    • 0035954552 scopus 로고    scopus 로고
    • A novel esterase from Burkholderia gladioli which shows high deacetylation activity on Cephalosporins is related to β-lactamases and DD-peptidases
    • Peterson EI, Valinger G, Solkner B, Stubenrauch G, Schwab H (2001) A novel esterase from Burkholderia gladioli which shows high deacetylation activity on Cephalosporins is related to β-lactamases and DD-peptidases. J Biotechnol 89:11-25
    • (2001) J Biotechnol , vol.89 , pp. 11-25
    • Peterson, E.I.1    Valinger, G.2    Solkner, B.3    Stubenrauch, G.4    Schwab, H.5
  • 86
    • 0034265029 scopus 로고    scopus 로고
    • Resistance to insecticides and effect of synergists on permethrin toxicity in Pediculus capitis (Anoplura: Pediculidae) from Buenos Aires
    • Picollo MI, Vassena CV, Cueto GAM, Vernetti M, Zerba EN (2000) Resistance to insecticides and effect of synergists on permethrin toxicity in Pediculus capitis (Anoplura: Pediculidae) from Buenos Aires. J Med Entomol 37:721-725
    • (2000) J Med Entomol , vol.37 , pp. 721-725
    • Picollo, M.I.1    Vassena, C.V.2    Cueto, G.A.M.3    Vernetti, M.4    Zerba, E.N.5
  • 87
    • 0032103791 scopus 로고    scopus 로고
    • Anatomy of lipase binding sites: The scissile fatty acid binding site
    • Pleiss J, Fischer M, Schmid RD (1998) Anatomy of lipase binding sites: the scissile fatty acid binding site. Chem Phys Lipids 93:67-80
    • (1998) Chem Phys Lipids , vol.93 , pp. 67-80
    • Pleiss, J.1    Fischer, M.2    Schmid, R.D.3
  • 89
    • 0030981938 scopus 로고    scopus 로고
    • Molecular characterization of Pseudomonas strain HR199 involved in bioconversion of vanillin to protocatechnate
    • Priefart H, Rabenhorst J, Steinbuechel A (1997) Molecular characterization of Pseudomonas strain HR199 involved in bioconversion of vanillin to protocatechnate. J Bacteriol 179:2595-2607
    • (1997) J Bacteriol , vol.179 , pp. 2595-2607
    • Priefart, H.1    Rabenhorst, J.2    Steinbuechel, A.3
  • 90
    • 1642567275 scopus 로고    scopus 로고
    • Purification of ENOD8 proteins from Medicago sativa root nodules and their characterization as esterases
    • Pringle D, Dickstein R (2004) Purification of ENOD8 proteins from Medicago sativa root nodules and their characterization as esterases. Plant Physiol Biochem 42:73-79
    • (2004) Plant Physiol Biochem , vol.42 , pp. 73-79
    • Pringle, D.1    Dickstein, R.2
  • 92
    • 0018136104 scopus 로고
    • Nonspecific esterase activity in human lymphocytes: Histochemical characterization and distribution among major lymphocyte subclasses
    • Ranki A (1978) Nonspecific esterase activity in human lymphocytes: histochemical characterization and distribution among major lymphocyte subclasses. Clin Immunol Immunopathol 10:47-58
    • (1978) Clin Immunol Immunopathol , vol.10 , pp. 47-58
    • Ranki, A.1
  • 93
    • 0034583247 scopus 로고    scopus 로고
    • Application of directed evolution in the development of enantioselective enzymes
    • Reetz MT (2000) Application of directed evolution in the development of enantioselective enzymes. Pure Appl Chem 72:1615-1622
    • (2000) Pure Appl Chem , vol.72 , pp. 1615-1622
    • Reetz, M.T.1
  • 94
    • 17944367572 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of cyclic oligomers of poly(ethylene terephthlate). WO 9727237
    • Riegels M, Koch R, Pedersen LS, Lund H (1997) Enzymatic hydrolysis of cyclic oligomers of poly(ethylene terephthlate). WO 9727237
    • (1997)
    • Riegels, M.1    Koch, R.2    Pedersen, L.S.3    Lund, H.4
  • 95
    • 0025357167 scopus 로고
    • Pancreatic cholesterol esterases. Purification and characterization of human pancreatic fatty acid ethyl ester synthase
    • Riley DJ, Kyger EM, Spilburg CA, Lange LG (1990) Pancreatic cholesterol esterases. Purification and characterization of human pancreatic fatty acid ethyl ester synthase. Biochemistry 29:3848-3852
    • (1990) Biochemistry , vol.29 , pp. 3848-3852
    • Riley, D.J.1    Kyger, E.M.2    Spilburg, C.A.3    Lange, L.G.4
  • 96
    • 20444440414 scopus 로고    scopus 로고
    • Non-steroidal anti-inflammatory drugs (NSAIDS)
    • Ruiter J de (2002) Non-steroidal anti-inflammatory drugs (NSAIDS). Principles Drug Action 2:1-8
    • (2002) Principles Drug Action , vol.2 , pp. 1-8
    • De Ruiter, J.1
  • 98
    • 17944374273 scopus 로고    scopus 로고
    • Enantiomeric chroman carboxylic acid derivative production DE 4430089
    • Schutt H (1996) Enantiomeric chroman carboxylic acid derivative production DE 4430089
    • (1996)
    • Schutt, H.1
  • 99
    • 0141942562 scopus 로고    scopus 로고
    • Strategic selection of hyperthermophilic esterases for resolution of 2-arylpropionic esters
    • Sehegal AC, Kelly RM (2003) Strategic selection of hyperthermophilic esterases for resolution of 2-arylpropionic esters. Biotechnol Prog 19:1410-1416
    • (2003) Biotechnol Prog , vol.19 , pp. 1410-1416
    • Sehegal, A.C.1    Kelly, R.M.2
  • 100
    • 0003076197 scopus 로고
    • Idiosyncrasies of solid-state fermentation systems in the biosynthesis of metabolites by some bacterial and fungal cultures
    • Shankaranand VS, Ramesh MV, Lonsane BK (1992) Idiosyncrasies of solid-state fermentation systems in the biosynthesis of metabolites by some bacterial and fungal cultures. Process Biochem 27:33-36
    • (1992) Process Biochem , vol.27 , pp. 33-36
    • Shankaranand, V.S.1    Ramesh, M.V.2    Lonsane, B.K.3
  • 101
    • 0028869651 scopus 로고
    • Purification and characterization of two thermostable acetyl xylan esterases from Thermoanaerobacterium sp. Strain JW/SL-Y485
    • Shao W, Wiegel J (1995) Purification and characterization of two thermostable acetyl xylan esterases from Thermoanaerobacterium sp. Strain JW/SL-Y485. Appl Environ Microbiol 61:729-733
    • (1995) Appl Environ Microbiol , vol.61 , pp. 729-733
    • Shao, W.1    Wiegel, J.2
  • 102
    • 0037164165 scopus 로고    scopus 로고
    • Significantly improved esterase activity of Trichosporun brassicae cells for ketoprofen resolution by 2-propanol treatment
    • Shen D, Xu JH, Wu HY, Liu YY (2002) Significantly improved esterase activity of Trichosporun brassicae cells for ketoprofen resolution by 2-propanol treatment. J Mol Catal B 18:219-224
    • (2002) J Mol Catal B , vol.18 , pp. 219-224
    • Shen, D.1    Xu, J.H.2    Wu, H.Y.3    Liu, Y.Y.4
  • 103
    • 17944370767 scopus 로고
    • Enzymatic resolution of taxane side chain intermediate. European Patent 552041
    • Squibb (1993) Enzymatic resolution of taxane side chain intermediate. European Patent 552041
    • (1993)
  • 104
    • 0037030806 scopus 로고    scopus 로고
    • Purification and partial amino acid sequences of an esterase from tomato
    • Stuhlfelder C, Lottspeich F, Mueller MJ (2002) Purification and partial amino acid sequences of an esterase from tomato. Phytochemistry 60:233-240
    • (2002) Phytochemistry , vol.60 , pp. 233-240
    • Stuhlfelder, C.1    Lottspeich, F.2    Mueller, M.J.3
  • 105
    • 2942746205 scopus 로고    scopus 로고
    • A novel thermostable esterase from the thermo-acidophilic archaeon Sulfololeus tokodaii strain 7
    • Suzuki Y, Miyamoto K, Ohta H (2004) A novel thermostable esterase from the thermo-acidophilic archaeon Sulfololeus tokodaii strain 7. FEMS Microbiol Lett 236:97-102
    • (2004) FEMS Microbiol Lett , vol.236 , pp. 97-102
    • Suzuki, Y.1    Miyamoto, K.2    Ohta, H.3
  • 106
    • 0031014580 scopus 로고    scopus 로고
    • Application of macromolecular additives to reduce the hydrolytic degradation of polyurethanes by lysosomal enzymes
    • Tang YW, Santerre JP, Labow RS, Taylor DG (1997) Application of macromolecular additives to reduce the hydrolytic degradation of polyurethanes by lysosomal enzymes. Biomaterials 18:37-45
    • (1997) Biomaterials , vol.18 , pp. 37-45
    • Tang, Y.W.1    Santerre, J.P.2    Labow, R.S.3    Taylor, D.G.4
  • 107
    • 0028862433 scopus 로고
    • An acetylglucomannan esterase of Aspergillus oryzae: Purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan
    • Tenkanen M, Thornton J, Viikari L (1995) An acetylglucomannan esterase of Aspergillus oryzae: purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan. J Biotechnol 42:197-206
    • (1995) J Biotechnol , vol.42 , pp. 197-206
    • Tenkanen, M.1    Thornton, J.2    Viikari, L.3
  • 108
    • 0037626454 scopus 로고    scopus 로고
    • Production and partial characterization of feruloyl esterase by Sporotrichum thermophile in solid-state fermentation
    • Topakas E, Kalogeris E, Kekos D, Macris BJ, Christakopoulos P (2003) Production and partial characterization of feruloyl esterase by Sporotrichum thermophile in solid-state fermentation. Process Biochem 38:1539-1543
    • (2003) Process Biochem , vol.38 , pp. 1539-1543
    • Topakas, E.1    Kalogeris, E.2    Kekos, D.3    Macris, B.J.4    Christakopoulos, P.5
  • 109
    • 0027404437 scopus 로고
    • Efficient kinetic resolution of organosilicon compounds by stereoselective esterification with hydrolases in organic solvent
    • Uejima A, Fukni T, Fuknsaki E, Omata T, Kawamoto T, Tanaka A (1993) Efficient kinetic resolution of organosilicon compounds by stereoselective esterification with hydrolases in organic solvent. Appl Microbiol Biotechnol 38:426-486
    • (1993) Appl Microbiol Biotechnol , vol.38 , pp. 426-486
    • Uejima, A.1    Fukni, T.2    Fuknsaki, E.3    Omata, T.4    Kawamoto, T.5    Tanaka, A.6
  • 111
    • 0034364866 scopus 로고    scopus 로고
    • Directed evolution: From a staphylococcal lipase to a phospholipase
    • Van Kampen MD, Egmond MR (2000) Directed evolution: from a staphylococcal lipase to a phospholipase. Eur J Lipid Sci Technol 102:717-728
    • (2000) Eur J Lipid Sci Technol , vol.102 , pp. 717-728
    • Van Kampen, M.D.1    Egmond, M.R.2
  • 112
    • 0019619706 scopus 로고
    • Identification of aspirinase with one of the carboxylesterase requiring a thiol group
    • Vincent D, Lagreu R (1981) Identification of aspirinase with one of the carboxylesterase requiring a thiol group. Biochem J 197:771-773
    • (1981) Biochem J , vol.197 , pp. 771-773
    • Vincent, D.1    Lagreu, R.2
  • 113
    • 0032731963 scopus 로고    scopus 로고
    • Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger
    • Vries RP de, Visser J (1999) Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger. Appl Environ Microbiol 65:5500-5503
    • (1999) Appl Environ Microbiol , vol.65 , pp. 5500-5503
    • De Vries, R.P.1    Visser, J.2
  • 114
    • 0035711459 scopus 로고    scopus 로고
    • High-throughput screening for biocatalysts
    • Wahler D, Reymond Jean-Louis (2001) High-throughput screening for biocatalysts. Curr Opin Biotechnol 12:535-544
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 535-544
    • Wahler, D.1    Jean-Louis, R.2
  • 116
    • 0015513558 scopus 로고
    • Cholinesterase activities in subcellular fractions of rat liver
    • Wheeler GE, Coleman R, Finean JB (1972) Cholinesterase activities in subcellular fractions of rat liver. Biochim Biophys Acta 255:917-930
    • (1972) Biochim Biophys Acta , vol.255 , pp. 917-930
    • Wheeler, G.E.1    Coleman, R.2    Finean, J.B.3
  • 118
    • 3042686950 scopus 로고    scopus 로고
    • Partial purification and characterization of a methyl-parathion resistance-associated general esterase in Diabrotica virgifera (Coleoptera: Chrysomelidae)
    • Zhou X, Scharf ME, Sarath G, Meinke LJ, Chandler LD, Siegfried BD (2004) Partial purification and characterization of a methyl-parathion resistance-associated general esterase in Diabrotica virgifera (Coleoptera: chrysomelidae). Pesticide Biochem Physiol 78:114-125
    • (2004) Pesticide Biochem Physiol , vol.78 , pp. 114-125
    • Zhou, X.1    Scharf, M.E.2    Sarath, G.3    Meinke, L.J.4    Chandler, L.D.5    Siegfried, B.D.6


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