Purification and characterization of xylanases from Aspergillus giganteus

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-27T11:21:04Z
dc.date.accessioned2022-10-05T17:52:35Z
dc.date.available2014-05-27T11:21:04Z
dc.date.available2022-10-05T17:52:35Z
dc.date.created2014-05-27T11:21:04Z
dc.date.issued2004-04-20
dc.identifierFolia Microbiologica, v. 49, n. 1, p. 13-18, 2004.
dc.identifier0015-5632
dc.identifierhttp://hdl.handle.net/11449/67708
dc.identifier10.1007/BF02931639
dc.identifierWOS:000220630700003
dc.identifier2-s2.0-1842418765
dc.identifier4110421764783871
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3917328
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.
dc.languageeng
dc.relationFolia Microbiologica
dc.relation1.311
dc.relation0,502
dc.rightsAcesso restrito
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 giganteus
dc.typeArtigo


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