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dc.contributor.authorKnob, Adriana
dc.contributor.authorCarmona, Eleonora Cano [UNESP]
dc.date.accessioned2013-09-30T18:47:28Z
dc.date.accessioned2014-05-20T13:56:24Z
dc.date.available2013-09-30T18:47:28Z
dc.date.available2014-05-20T13:56:24Z
dc.date.issued2012-06-01
dc.identifierhttp://dx.doi.org/10.1007/s13213-011-0282-x
dc.identifier.citationAnnals of Microbiology. New York: Springer, v. 62, n. 2, p. 501-508, 2012.
dc.identifier.issn1590-4261
dc.identifier.urihttp://hdl.handle.net/11449/20163
dc.description.abstractThe beta-xylosidase from was purified to homogeneity by a rapid and inexpensive procedure involving ammonium sulphate fractionation and molecular exclusion chromatography. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed two bands with an estimated molecular mass of 97 and 42 kDa, respectively. Electrophoretical homogeneity was observed under non-denaturing PAGE conditions. These results indicate that this protein has a dimeric structure. The molecular mass of the native enzyme estimated by molecular exclusion chromatography was 144 kDa. The enzyme is a glycoprotein with a 56.4% carbohydrate content. The pH and temperature optima were 2.5 and 60A degrees C, respectively. The enzyme remained stable over a pH range from 2.0 to 7.0 and at temperatures up to 60A degrees C for 375 min. All divalent cations tested, except for Hg2+, inhibited beta-xylosidase activity, especially at a concentration of10 mM. The purified enzyme was also sensitive to denaturing agents SDS and EDTA and was activated by thiol-containing reducing agents. The Michaelis-Menten constant for -nitrophenyl-beta--xylopyranoside was 0.78 mM, and the maximum reaction velocity was 0.51 mu mole of -nitrophenol min(-1) mg(-1) of protein. This is the first report on the purification and characterization of a beta-xylosidase from , which has potential applications in a number of biotechnological processes, such as animal feed, juice and wine industries.en
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent501-508
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofAnnals of Microbiology
dc.sourceWeb of Science
dc.subjectPenicillium sclerotiorumen
dc.subjectbeta-Xylosidaseen
dc.subjectEnzyme purificationen
dc.subjectAcid beta-xylosidaseen
dc.titlePurification and properties of an acid beta-xylosidase from Penicillium sclerotiorumen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderSpringer
dc.contributor.institutionUniv Estadual Centro Oeste
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.description.affiliationUniv Estadual Centro Oeste, Dept Biol, BR-85010000 Guarapuava, Parana State, Brazil
dc.description.affiliationSão Paulo State Univ, Dept Biochem & Microbiol, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationUnespSão Paulo State Univ, Dept Biochem & Microbiol, BR-13506900 Rio Claro, SP, Brazil
dc.identifier.doi10.1007/s13213-011-0282-x
dc.identifier.wosWOS:000304140600006
dc.rights.accessRightsAcesso restrito
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Rio Claropt
dc.identifier.lattes4110421764783871
unesp.author.lattes4110421764783871
unesp.author.orcid0000-0002-0230-5735[2]
dc.relation.ispartofjcr1.407
dc.relation.ispartofsjr0,479
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