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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleA novel and enantioselective epoxide hydrolase from Aspergillus brasiliensis CCT 1435: Purification and characterizationpt_BR
dc.contributor.authorBeloti, LLpt_BR
dc.contributor.authorCosta, BZpt_BR
dc.contributor.authorToledo, MASpt_BR
dc.contributor.authorSantos, CApt_BR
dc.contributor.authorCrucello, Apt_BR
dc.contributor.authorFavaro, MTPpt_BR
dc.contributor.authorSantiago, ASpt_BR
dc.contributor.authorMendes, JSpt_BR
dc.contributor.authorMarsaioli, AJpt_BR
dc.contributor.authorSouza, APpt_BR
unicamp.authorBeloti, Lilian L. Toledo, Marcelo A. S. Santos, Clelton A. Crucello, Aline Favaro, Marianna T. P. Santiago, Andre S. Mendes, Juliano S. Souza, Anete P. Univ Estadual Campinas, Ctr Biol Mol & Engn Genet, BR-13083875 Campinas, SP, Brazilpt_BR
unicamp.authorCosta, Bruna Z. Marsaioli, Anita J. Univ Estadual Campinas, Inst Quim, Sao Paulo, Brazilpt_BR
unicamp.authorSouza, Anete P. Univ Estadual Campinas, Dept Biol Vegetal, Inst Biol, Sao Paulo, Brazilpt_BR
dc.subject.wosSecondary Structure Analysespt_BR
dc.subject.wosMicrobiological Transformationspt_BR
dc.subject.wosKinetic Resolutionpt_BR
dc.subject.wosStyrene Oxidept_BR
dc.subject.wosAsymmetric Catalysispt_BR
dc.description.abstractA novel epoxide hydrolase from Aspergillus brasiliensis CCT1435 (AbEH) was cloned and overexpressed in Escherichia call cells with a 6xHis-tag and purified by nickel affinity chromatography. Gel filtration analysis and circular dichroism measurements indicated that this novel AbEH is a homodimer in aqueous solution and contains the typical secondary structure of an alpha/beta hydrolase fold. The activity of AbEH was initially assessed using the fluorogenic probe O-(3,4-epoxybutyl) umbelliferone and was active in a broad range of pH (6-9) and temperature (25-45 degrees C); showing optimum performance at pH 6.0 and 30 degrees C. The Michaelis constant (K-M) and maximum rate (V-max) values were 495 mu M and 0.24 mu M/s, respectively. Racemic styrene oxide (SO) was used as a substrate to assess the AbEH activity and enantioselectivity, and 66% of the SO was hydrolyzed after only 5 min of reaction, with the remaining (S)-SO ee exceeding 99% in a typical kinetic resolution behavior. The AbEH-catalyzed hydrolysis of SO was also evaluated in a biphasic system of water:isooctane; (R)-diol in 84% ee and unreacted (S)-SO in 36% ee were produced, with 43% conversion in 24 h, indicating a discrete enantioconvergent behavior for AbEH. This novel epoxide hydrolase has biotechnological potential for the preparation of enantiopure epoxides or vicinal diols. (C) 2013 Elsevier Inc. All right S
dc.relation.ispartofProtein Expression And Purificationpt_BR
dc.relation.ispartofabbreviationProtein Expr. Purif.pt_BR
dc.publisher.citySan Diegopt_BR
dc.publisherAcademic Press Inc Elsevier Sciencept_BR
dc.identifier.citationProtein Expression And Purification. Academic Press Inc Elsevier Science, v. 91, n. 2, n. 175, n. 183, 2013.pt_BR
dc.sourceWeb of Sciencept_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.description.sponsorshipAgencia Nacional do Petroleo (ANP-PETRO-BRAS)pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorship1Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.description.sponsordocumentnumberFAPESP [09/51756-2, 11/10378-5]pt
dc.description.provenanceMade available in DSpace on 2014-08-01T18:16:48Z (GMT). No. of bitstreams: 0 Previous issue date: 2013en
dc.description.provenanceMade available in DSpace on 2015-11-26T17:56:26Z (GMT). No. of bitstreams: 0 Previous issue date: 2013en
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