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

Katapodis, P; Nerinckx, W; Claeyssens, M; Christakopoulos, P

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