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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/74130
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dc.contributor.authorGonçalves, Heloísa Bressan-
dc.contributor.authorJorge, João Atílio-
dc.contributor.authorPessela, Benevides Costa-
dc.contributor.authorLorente, Glória Fernandez-
dc.contributor.authorGuisán, José Manuel-
dc.contributor.authorGuimarães, Luis Henrique Souza-
dc.date.accessioned2014-05-27T11:27:27Z-
dc.date.accessioned2016-10-25T18:40:48Z-
dc.date.available2014-05-27T11:27:27Z-
dc.date.available2016-10-25T18:40:48Z-
dc.date.issued2013-01-01-
dc.identifierhttp://dx.doi.org/10.1007/s10529-012-1111-4-
dc.identifier.citationBiotechnology Letters, v. 35, n. 4, p. 591-598, 2013.-
dc.identifier.issn0141-5492-
dc.identifier.issn1573-6776-
dc.identifier.urihttp://hdl.handle.net/11449/74130-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/74130-
dc.description.abstractThe extracellular tannase from Emericela nidulans was immobilized on different ionic and covalent supports. The derivatives obtained using DEAE-Sepharose and Q-Sepharose were thermally stable from 60 to 75 °C, with a half life (t50) >24 h at 80 °C at pH 5. 0. The glyoxyl-agarose and amino-glyoxyl derivatives showed a thermal stability which was lower than that observed for ionic supports. However, when the stability to pH was considered, the derivatives obtained from covalent supports were more stable than those obtained from ionic supports. DEAE-Sepharose and Q-Sepharose derivatives as well as the free enzyme were stable in 30 and 50 % (v/v) 1-propanol. The CNBr-agarose derivative catalyzed complete tannic acid hydrolysis, whereas the Q-Sepharose derivative catalyzed the transesterification reaction to produce propyl gallate (88 % recovery), which is an important antioxidant. © 2012 Springer Science+Business Media Dordrecht.en
dc.format.extent591-598-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectEmericela-
dc.subjectEnzyme immobilization-
dc.subjectPropyl gallate-
dc.subjectTannase-
dc.subjectTannin acyl hydrolase-
dc.subject1-propanol-
dc.subjectExtracellular-
dc.subjectFree enzyme-
dc.subjectHalf lives-
dc.subjectQ-Sepharose-
dc.subjectTannic acid-
dc.subjectThermally stable-
dc.subjectTransesterification reaction-
dc.subjectCatalysis-
dc.subjectFlavonoids-
dc.subjectThermodynamic stability-
dc.subjectSynthesis (chemical)-
dc.subjectcarboxylesterase-
dc.subjectgallic acid propyl ester-
dc.subjectimmobilized enzyme-
dc.subjecttannase-
dc.subjecttannin derivative-
dc.subjectchemistry-
dc.subjectEmericella-
dc.subjectenzyme stability-
dc.subjectenzymology-
dc.subjectmetabolism-
dc.subjectpH-
dc.subjecttemperature-
dc.subjectCarboxylic Ester Hydrolases-
dc.subjectEnzyme Stability-
dc.subjectEnzymes, Immobilized-
dc.subjectHydrogen-Ion Concentration-
dc.subjectPropyl Gallate-
dc.subjectTannins-
dc.subjectTemperature-
dc.titleCharacterization of a tannase from Emericela nidulans immobilized on ionic and covalent supports for propyl gallate synthesisen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionInstituto de Fermentaciones Industriales, CSIC-
dc.contributor.institutionUniversidad Autonoma de Madrid-
dc.description.affiliationInstituto de Química de Araraquara - UNESP, Rua Prof. Francisco Degni s/n, Araraquara, 14800-000-
dc.description.affiliationDepartamento de Biologia Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto - USP, Avenida Bandeirantes 3900, Ribeirão Preto, 14040-901-
dc.description.affiliationDepartamento de Microbiologia Instituto de Fermentaciones Industriales, CSIC, C/Juan de La Cierva 3, 28006 Madrid-
dc.description.affiliationDepartamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica, CSIC Universidad Autonoma de Madrid, C/Marie Curie 2, 28049 Madrid-
dc.description.affiliationUnespInstituto de Química de Araraquara - UNESP, Rua Prof. Francisco Degni s/n, Araraquara, 14800-000-
dc.identifier.doi10.1007/s10529-012-1111-4-
dc.identifier.wosWOS:000316081800016-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofBiotechnology Letters-
dc.identifier.scopus2-s2.0-84874814840-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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