Purification and characterization of a thermostable intracellular β-xylosidase from the thermophilic fungus Sporotrichum thermophile

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dc.contributor.author Katapodis, P en
dc.contributor.author Nerinckx, W en
dc.contributor.author Claeyssens, M en
dc.contributor.author Christakopoulos, P en
dc.date.accessioned 2014-03-01T01:24:54Z
dc.date.available 2014-03-01T01:24:54Z
dc.date.issued 2006 en
dc.identifier.issn 1359-5113 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/17502
dc.subject β-d-Xylosidase en
dc.subject Epoxyalkyl glycosides en
dc.subject Inhibition en
dc.subject Purification en
dc.subject Sporotrichum thermophile en
dc.subject Thermostability en
dc.subject.classification Biochemistry & Molecular Biology en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.classification Engineering, Chemical en
dc.subject.other Column chromatography en
dc.subject.other Enzyme inhibition en
dc.subject.other Fungi en
dc.subject.other Optimization en
dc.subject.other pH effects en
dc.subject.other Purification en
dc.subject.other Sugars en
dc.subject.other Thermodynamic stability en
dc.subject.other β-d-Xylosidase en
dc.subject.other Epoxyalkyl glycosides en
dc.subject.other Protein properties en
dc.subject.other Sporotrichum thermophile en
dc.subject.other Enzymes en
dc.subject.other Corynascus heterothallicus en
dc.subject.other Fungi en
dc.subject.other Sporothrix en
dc.title Purification and characterization of a thermostable intracellular β-xylosidase from the thermophilic fungus Sporotrichum thermophile en
heal.type journalArticle en
heal.identifier.primary 10.1016/j.procbio.2006.06.021 en
heal.identifier.secondary http://dx.doi.org/10.1016/j.procbio.2006.06.021 en
heal.language English en
heal.publicationDate 2006 en
heal.abstract An intracellular beta-xylosidase from the thermophilic fungus Sporotricum thermophile strain ATCC 34628 was purified to homogeneity by Q-Sepharose and Mono-Q column chromatographies. The protein properties correspond to molecular mass and pI values of 45 kDa and 4.2, respectively. The enzyme is optimally active at pH 7.0 and 50 degrees C. The purified beta-xylosidase is fully stable at pH 6.0-8.0 and temperatures up to 50 degrees C and retained over 58% of its activity after 1 h at 60 degrees C. The enzyme hydrolyzes beta-1,4-linked xylo-oligosaccharides with chain lengths from 2 to 6, releasing xylose from the non-reducing end, but is inactive against xylan substrates. The apparent K-m and V-max values from p-nitrophenyl beta-D-xylopyranoside are 1.1 mM and 114 mu mol p-nitrophenol min(-1) mg(-1), respectively. Alcohols inactivate the enzyme, ethanol at 10% (v/v) yields a 30% decrease of its activity. The enzyme is irreversibly inhibited by 2,3-epoxypropyl beta-D-xylobioside while alkyl epoxides derived from D-Xylose were not inhibitors of the enzyme. The enzyme catalyses the condensation reaction using high donor concentration, up to 60% (w/v) xylose. (c) 2006 Elsevier Ltd. All rights reserved. en
heal.publisher ELSEVIER SCI LTD en
heal.journalName Process Biochemistry en
dc.identifier.doi 10.1016/j.procbio.2006.06.021 en
dc.identifier.isi ISI:000242259100007 en
dc.identifier.volume 41 en
dc.identifier.issue 12 en
dc.identifier.spage 2402 en
dc.identifier.epage 2409 en

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