dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorKnob, Adriana
dc.creatorCarmona, Eleonora Cano
dc.date2013-09-30T18:47:22Z
dc.date2014-05-20T13:56:21Z
dc.date2016-10-25T17:05:42Z
dc.date2013-09-30T18:47:22Z
dc.date2014-05-20T13:56:21Z
dc.date2016-10-25T17:05:42Z
dc.date2009-10-01
dc.date.accessioned2017-04-05T21:14:53Z
dc.date.available2017-04-05T21:14:53Z
dc.identifierNew Biotechnology. Amsterdam: Elsevier B.V., v. 26, n. 1-2, p. 60-67, 2009.
dc.identifier1871-6784
dc.identifierhttp://hdl.handle.net/11449/20143
dc.identifierhttp://acervodigital.unesp.br/handle/11449/20143
dc.identifier10.1016/j.nbt.2009.03.002
dc.identifierWOS:000271547200010
dc.identifierhttp://dx.doi.org/10.1016/j.nbt.2009.03.002
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/865875
dc.descriptionIn recent decades, beta-xylosidases have been used in many processing industries. In this work, the study of xylosidase production by Penicillium sclerotiorum and its characterization are reported. Optimal production was obtained in medium supplemented with oat spelts xylan, pH 5.0, at 30 degrees C, under stationary condition for six days. The optimum activity temperature was 60 degrees C and unusual optimum pH 2.5. The enzyme was stable at 50 and 55 degrees C, with half-life of 240 and 232 min, respectively. High pH stability was verified from pH 2.0 to 4.0 and 7.5. The beta-xylosidase was strongly inhibited by divalent cations, sensitive to denaturing agents SDS, EDTA and activated by thiol-containing reducing agents. The apparent V(max) and K(m) values was 0.48 mu mol PNXP min(-1) mg(-1) protein and 0.75 mM, respectively. The enzyme was xylose tolerant with a K(i) of 28.7. This enzyme presented interesting characteristics for biotechnological process such as animal feed, juice and wine industries.
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageeng
dc.publisherElsevier B.V.
dc.relationNew Biotechnology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectBiochemical properties
dc.subjectEnzyme characterization
dc.subjectEnzyme production
dc.subjectPenicillium sclerotiorum
dc.subjectbeta-Xylosidase
dc.titleCell-associated acid beta-xylosidase production by Penicillium sclerotiorum
dc.typeOtro


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