Extracellular tannase from Emericella nidulans showing hypertolerance to temperature and organic solvents

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dc.contributor.authorGoncalves, Heloisa Bressan [UNESP]
dc.contributor.authorRiul, Alana Jacomini [UNESP]
dc.contributor.authorTerenzi, Hector Francisco
dc.contributor.authorJorge, Joao Atilio
dc.contributor.authorSouza Guimaraes, Luis Henrique
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:33:38Z
dc.date.available2014-05-20T15:33:38Z
dc.date.issued2011-08-01
dc.description.abstractThe filamentous fungus Emericella nidulans (=Aspergillus nidulans) produced high levels of extracellular tannase when grown at 30 degrees C, under agitation (100 rpm), for 24 h in Khanna medium supplemented with tannic acid as carbon source. The enzyme was purified 61-fold, with 30% yield. The molecular mass of the native protein was estimated to be 302 kDa by gel filtration, with a carbohydrate content of 50%. Two protein bands (45.8 and 52 kDa) were observed after 12% SDS-PAGE, suggesting a glycoprotein constituted by three copies of each subunit. The extracellular tannase showed temperature and pH optima of 45 degrees C and 5.0, respectively, and was fully stable in the temperature range of 22-50 degrees C. with a half-life (t(50)) of about 72h at 90 degrees C. The enzyme retained around 80% of control activity when maintained for 60h at pH 4.0 or 5.0. Tannase activity was stimulated by Zn(2+), Hg(2+), Co(2+), and the detergents SDS and Triton X-100. Organic solvents (about 50%, v/v) also increased enzyme activity, particularly isopropanol, acetonitrile, and ethanol. The K(m) and V(max) values were 14.01 mM and 2.63 U mg(-1) protein in the presence of tannic acid; and 4.78 mM and 0.29 U mg(-1) protein in the presence of methyl gallate. For propyl gallate, the V(max) was 0.05 U mg(-1) protein, with K(m) of 7.69 mM; for pyrogallol, the V(max) was 7.40 U mg(-1) protein and the K(m) was 16.94 mM. Crown Copyright (C) 2011 Published by Elsevier B.V. All rights reserved.en
dc.description.affiliationUSP, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Biol, BR-14040901 Ribeirao Preto, SP, Brazil
dc.description.affiliationUNESP, Inst Quim Araraquara, BR-14800900 Araraquara, SP, Brazil
dc.description.affiliationUnespUNESP, Inst Quim Araraquara, BR-14800900 Araraquara, SP, Brazil
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.extent29-35
dc.identifierhttp://dx.doi.org/10.1016/j.molcatb.2011.03.005
dc.identifier.citationJournal of Molecular Catalysis B-enzymatic. Amsterdam: Elsevier B.V., v. 71, n. 1-2, p. 29-35, 2011.
dc.identifier.doi10.1016/j.molcatb.2011.03.005
dc.identifier.issn1381-1177
dc.identifier.urihttp://hdl.handle.net/11449/42200
dc.identifier.wosWOS:000291451000005
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofJournal of Molecular Catalysis B: Enzymatic
dc.relation.ispartofsjr0,522
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectTannaseen
dc.subjectTannin acyl hydrolaseen
dc.subjectEmericellaen
dc.subjectHyperstable enzymeen
dc.subjectFungien
dc.titleExtracellular tannase from Emericella nidulans showing hypertolerance to temperature and organic solventsen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.

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