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dc.contributor.authorRibeiro Leite, Rodrigo Simoes-
dc.contributor.authorAlves-Prado, Heloiza Ferreira-
dc.contributor.authorCabral, Hamilton-
dc.contributor.authorPagnocca, Fernando Carlos-
dc.contributor.authorGomes, Eleni-
dc.contributor.authorDa-Silva, Roberto-
dc.date.accessioned2013-09-30T18:41:58Z-
dc.date.accessioned2014-05-20T13:56:18Z-
dc.date.accessioned2016-10-25T17:05:40Z-
dc.date.available2013-09-30T18:41:58Z-
dc.date.available2014-05-20T13:56:18Z-
dc.date.available2016-10-25T17:05:40Z-
dc.date.issued2008-11-06-
dc.identifierhttp://dx.doi.org/10.1016/j.enzmictec.2008.07.006-
dc.identifier.citationEnzyme and Microbial Technology. New York: Elsevier B.V., v. 43, n. 6, p. 391-395, 2008.-
dc.identifier.issn0141-0229-
dc.identifier.urihttp://hdl.handle.net/11449/20122-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/20122-
dc.description.abstractThe purified beta-glucosidase of Aureobasidium pullulans ER-16 is one of more thermostable enzyme reported to date. Considering the unfeasibility of using purified enzyme for industrial application, it was interesting to analyze this property for the crude enzyme. Thermophilic fungus Thermoascus aurantiacus CBMAI-756 and mesophilic A. pullulans ER-16 were cultivated in different hemicellulosic materials on solid-state cultivation for beta-glucosidase production. Wheat bran was most appropriate for beta-glucosidase production by both microorganisms. T. aurantiacus exhibited maximum enzyme production (7.0 U/ml or 70 U/g) at 48-72 h and A. pullulans a maximum (1.3 U/ml or 13 U/g) at 120 h. Maximum activities were at 75 degrees C with optimum pH at 4.5 and 4.0, for T aurantiacus and A. pullulans, respectively. A. pullulans's beta-glucosidase was more pH stable (4.5-10.0 against 4.5-8.0) and more thermostable (90% after 1 h at 75 degrees C against 85% after 1 h at 70 degrees C) than the enzyme from the thermophilic T. aurantiacus. The t((1/2)) at 80 degrees C were 50 and 12.5 min for A. pullulans and T. aurantiascus, respectively. These data confirm the high thermostability of crude beta-glucosidase from A. pullulans. Both beta-glucosidases were strongly inhibited by glucose, but ethanol significantly increased the activity of the enzyme from T. aurantiacus. (C) 2008 Elsevier B.V. All rights reserved.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.format.extent391-395-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectBeta-glucosidaseen
dc.subjectThermostabilityen
dc.subjectAureobasidium pullulansen
dc.subjectThermoascus aurantiacusen
dc.subjectSolid-state cultivationen
dc.titleProduction and characteristics comparison of crude beta-glucosidases produced by microorganisms Thermoascus aurantiacus e Aureobasidium pullulans in agricultural wastesen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.description.affiliationSão Paulo State Univ, UNESP, IBILCE, Lab Biochem & Appl Microbiol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationSão Paulo State Univ, UNESP, Fac Engn Ilha Solteira, FEIS, BR-15385000 Ilha Solteira, SP, Brazil-
dc.description.affiliationUniv São Paulo, Fac Pharmaceut Sci Ribeirao Preto, Dept Pharmaceut Sci, BR-14040903 Ribeirao Preto, SP, Brazil-
dc.description.affiliationUnespSão Paulo State Univ, UNESP, IBILCE, Lab Biochem & Appl Microbiol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespSão Paulo State Univ, UNESP, Fac Engn Ilha Solteira, FEIS, BR-15385000 Ilha Solteira, SP, Brazil-
dc.identifier.doi10.1016/j.enzmictec.2008.07.006-
dc.identifier.wosWOS:000260561800001-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofEnzyme and Microbial Technology-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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