You are in the accessibility menu

Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/74187
Full metadata record
DC FieldValueLanguage
dc.contributor.authorRiul, Alana Jacomini-
dc.contributor.authorGonçalves, Heloísa Bressan-
dc.contributor.authorJorge, João Atílio-
dc.contributor.authorGuimarães, Luis Henrique Souza-
dc.date.accessioned2014-05-27T11:27:29Z-
dc.date.accessioned2016-10-25T18:40:58Z-
dc.date.available2014-05-27T11:27:29Z-
dc.date.available2016-10-25T18:40:58Z-
dc.date.issued2013-01-01-
dc.identifierhttp://dx.doi.org/10.1016/j.molcatb.2012.09.001-
dc.identifier.citationJournal of Molecular Catalysis B: Enzymatic, v. 85-86, p. 126-133.-
dc.identifier.issn1381-1177-
dc.identifier.issn1873-3158-
dc.identifier.urihttp://hdl.handle.net/11449/74187-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/74187-
dc.description.abstractTannases have attracted wider attention because of their biotechnological potential, especially enzymes from filamentous fungi and other microorganisms. However, the biodiversity of these microorganisms has been poorly explored, and few strains were identified for tannase production and characterization. This article describes the production, purification and characterization of a glucose- and solvent-tolerant extracellular tannase from Aspergillus phoenicis. High enzymatic levels were obtained in Khanna medium containing tannic acid up to 72 h at 30 °C under 100 rpm. The purified enzyme with 65% of carbohydrate content had an apparent native molecular mass of 218 kDa with subunits of 120 kDa and 93 kDa and was stable at 50 °C for 1 h. Optima of temperature and pH were 60 °C and 5.0-6.5, respectively. The enzyme was not affected significantly by most ions, detergents and organic solvents. While glucose did not affect the tannase activity, the addition of a high concentration of gallic acid did. The Km values were 1.7 mM (tannic acid), 14.3 mM (methyl-gallate) and 0.6 mM (propyl-gallate). The enzyme was able to catalyze the transesterification reaction to produce propyl-gallate. All biochemical properties suggest the biotechnological potential of the glucose- and solvent-tolerant tannase from A. phoenicis. © 2012 Elsevier B.V. All rights reserved.en
dc.format.extent126-133-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectAspergillus-
dc.subjectEnzyme characterization-
dc.subjectGlucose-tolerant enzyme-
dc.subjectOrganic solvent-
dc.subjectTannase-
dc.subjectAspergillus phoenicis-
dc.subjectBiochemical properties-
dc.subjectCarbohydrate content-
dc.subjectExtracellular-
dc.subjectFilamentous fungi-
dc.subjectGallic acids-
dc.subjectHigh concentration-
dc.subjectPurified enzyme-
dc.subjectTannic acid-
dc.subjectTransesterification reaction-
dc.subjectBiodiversity-
dc.subjectBiotechnology-
dc.subjectCarbohydrates-
dc.subjectCharacterization-
dc.subjectEnzymes-
dc.subjectFlavonoids-
dc.subjectMicroorganisms-
dc.subjectOrganic solvents-
dc.subjectPurification-
dc.subjectSoaps (detergents)-
dc.subjectSolvents-
dc.subjectGlucose-
dc.subjectdetergent-
dc.subjectgallic acid methyl ester-
dc.subjectgallic acid propyl ester-
dc.subjectglucose-
dc.subjectorganic solvent-
dc.subjecttannase-
dc.subjecttannin-
dc.subjectcarbohydrate analysis-
dc.subjectcarbon source-
dc.subjectcatalysis-
dc.subjectconcentration (parameters)-
dc.subjectculture medium-
dc.subjectenzyme activity-
dc.subjectenzyme purification-
dc.subjectenzyme synthesis-
dc.subjecthydrolysis-
dc.subjectmolecular weight-
dc.subjectnonhuman-
dc.subjectpH-
dc.subjectthermostability-
dc.subjecttransesterification-
dc.subjectFungi-
dc.titleCharacterization of a glucose- and solvent-tolerant extracellular tannase from Aspergillus phoenicisen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.description.affiliationInstituto de Química de Araraquara - UNESP, Rua Mário Degni s/n, 14800-900 Araraquara, São Paulo-
dc.description.affiliationDepartamento de Biologia Faculdade de Filosofia Ciências e Letras de Ribeirão Preto USP, Avenida Bandeirantes 3900, 14040-901 Ribeirão Preto, São Paulo-
dc.description.affiliationUnespInstituto de Química de Araraquara - UNESP, Rua Mário Degni s/n, 14800-900 Araraquara, São Paulo-
dc.identifier.doi10.1016/j.molcatb.2012.09.001-
dc.identifier.wosWOS:000312231000018-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal of Molecular Catalysis B: Enzymatic-
dc.identifier.scopus2-s2.0-84866863408-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

There are no files associated with this item.
 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.