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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/20079
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dc.contributor.authorCarmona, E. C.-
dc.contributor.authorFialho, M. B.-
dc.contributor.authorBuchgnani, E. B.-
dc.contributor.authorCoelho, G. D.-
dc.contributor.authorBrocheto-Braga, M. R.-
dc.contributor.authorJorge, J. A.-
dc.date.accessioned2014-05-20T13:56:07Z-
dc.date.accessioned2016-10-25T17:05:34Z-
dc.date.available2014-05-20T13:56:07Z-
dc.date.available2016-10-25T17:05:34Z-
dc.date.issued2005-01-01-
dc.identifierhttp://dx.doi.org/10.1016/j.procbio.2004.01.010-
dc.identifier.citationProcess Biochemistry. Oxford: Elsevier B.V., v. 40, n. 1, p. 359-364, 2005.-
dc.identifier.issn1359-5113-
dc.identifier.urihttp://hdl.handle.net/11449/20079-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/20079-
dc.description.abstractA strain of Aspergillus versicolor produces a xylanolytic complex containing two components, the minor component being designated xylanase II. The highest production of xylanase II was observed in cultures grown for 5 days in 1% wheat bran as carbon source, at pH 6.5. Xylanase II was purified 28-fold by DEAE-Sephadex and HPLC GF-5 10 gel filtration. Xylanase II was a monomeric glycoprotein, exhibiting a molecular mass of 32 kDa with 14.1% of carbohydrate content. Optimal pH and temperature values for the enzyme activity were about 6.0-7.0 and 55 degreesC, respectively. Xylanase II thermoinactivation at 50degreesC showed a biphasic curve. The ions Hg2+, Cu2+ and the detergent SDS were strong inhibitors, while Mn2+ ions and dithiothreitol were stimulators of the enzyme activity. The enzyme was specific for xylans, showing higher specific activity on birchwood xylan. The Michaelis-Menten constant (K-m) for birchwood xylan was estimated to be 2.3 mg ml(-1) while maximal velocity (V-max) was 233.1 mumol mg(-1) min(-1) of protein. The hydrolysis of oat spell xylan released only xylooligosaccharides. Published by Elsevier Ltd.en
dc.format.extent359-364-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectAspergillus versicolorpt
dc.subjectxylanasept
dc.subjectendoxylanasept
dc.subjectenzyme purificationpt
dc.titleProduction, purification and characterization of a minor form of xylanase from Aspergillus versicoloren
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationUNESP, Inst Biociencias, Dept Bioquim & Microbiol, BR-13506900 Rio Claro, SP, Brazil-
dc.description.affiliationUnespUNESP, Inst Biociencias, Dept Bioquim & Microbiol, BR-13506900 Rio Claro, SP, Brazil-
dc.identifier.doi10.1016/j.procbio.2004.01.010-
dc.identifier.wosWOS:000224162000047-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofProcess Biochemistry-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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