You are in the accessibility menu

Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/67708
Full metadata record
DC FieldValueLanguage
dc.contributor.authorFialho, M. B.-
dc.contributor.authorCarmona, E. C.-
dc.date.accessioned2014-05-27T11:21:04Z-
dc.date.accessioned2016-10-25T18:19:30Z-
dc.date.available2014-05-27T11:21:04Z-
dc.date.available2016-10-25T18:19:30Z-
dc.date.issued2004-04-20-
dc.identifierhttp://dx.doi.org/10.1007/BF02931639-
dc.identifier.citationFolia Microbiologica, v. 49, n. 1, p. 13-18, 2004.-
dc.identifier.issn0015-5632-
dc.identifier.urihttp://hdl.handle.net/11449/67708-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/67708-
dc.description.abstractA strain of Aspergillus giganteus cultivated in a medium with xylan produced two xylanases (xylanase I and II) which were purified to homogeneity. Their molar mass, estimated by SDS-PAGE, were 21 and 24 kDa, respectively. Both enzymes are glycoproteins with 50°C temperature optimum; optimum pH was 6.0-6.5 for xylanase I and 6.0 for xylanase II. At 50°C xylanase I exhibited higher thermostability than xylanase II. Hg2+, Cu 2+ and SDS were strong inhibitors, 1,4-dithiothreitol stimulated the reaction of both enzymes. Both xylanases are xylan-specific; kinetic parameters indicated higher efficiency in the hydrolysis of oat spelts xylan. In hydrolysis of this substrate, xylotriose, xylotetraose and larger xylooligosaccharides were released and hence the enzymes were classified as endoxylanases.en
dc.format.extent13-18-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectammonium sulfate-
dc.subjectcopper-
dc.subjectdextran-
dc.subjectdithiothreitol-
dc.subjectdodecyl sulfate sodium-
dc.subjectendo 1,4 beta xylanase-
dc.subjectenzyme activator-
dc.subjectenzyme inhibitor-
dc.subjectfungal protein-
dc.subjectglycoprotein-
dc.subjectmercury derivative-
dc.subjectsephadex-
dc.subjectxylan-
dc.subjectAspergillus-
dc.subjectchemistry-
dc.subjectculture medium-
dc.subjectenzyme specificity-
dc.subjectenzyme stability-
dc.subjectenzymology-
dc.subjectgel chromatography-
dc.subjectgrowth, development and aging-
dc.subjectisolation and purification-
dc.subjectkinetics-
dc.subjectmetabolism-
dc.subjectmolecular weight-
dc.subjectpH-
dc.subjectpolyacrylamide gel electrophoresis-
dc.subjectprecipitation-
dc.subjecttemperature-
dc.subjectAmmonium Sulfate-
dc.subjectChromatography, Gel-
dc.subjectCopper-
dc.subjectCulture Media-
dc.subjectDextrans-
dc.subjectDithiothreitol-
dc.subjectElectrophoresis, Polyacrylamide Gel-
dc.subjectEndo-1,4-beta Xylanases-
dc.subjectEnzyme Activators-
dc.subjectEnzyme Inhibitors-
dc.subjectEnzyme Stability-
dc.subjectFractional Precipitation-
dc.subjectFungal Proteins-
dc.subjectGlycoproteins-
dc.subjectHydrogen-Ion Concentration-
dc.subjectKinetics-
dc.subjectMercury Compounds-
dc.subjectMolecular Weight-
dc.subjectSodium Dodecyl Sulfate-
dc.subjectSubstrate Specificity-
dc.subjectTemperature-
dc.subjectXylans-
dc.subjectAspergillus giganteus-
dc.titlePurification and characterization of xylanases from Aspergillus giganteusen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationDepto. de Bioquim. e Microbiologia Instituto de Biociências UNESP, 13506-900, Rio Claro, S. Paulo-
dc.description.affiliationUnespDepto. de Bioquim. e Microbiologia Instituto de Biociências UNESP, 13506-900, Rio Claro, S. Paulo-
dc.identifier.doi10.1007/BF02931639-
dc.identifier.wosWOS:000220630700003-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofFolia Microbiologica-
dc.identifier.scopus2-s2.0-1842418765-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

There are no files associated with this item.
Show simple item record Show full item record   View Statistics
 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.