Purification, characterization and mass spectrometric identification of two thermophilic xylanases from Sporotrichum thermophile

Vafiadi, C; Christakopoulos, P; Topakas, E

dc.contributor.author	Vafiadi, C	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Topakas, E	en
dc.date.accessioned	2014-03-01T01:34:23Z
dc.date.available	2014-03-01T01:34:23Z
dc.date.issued	2010	en
dc.identifier.issn	1359-5113	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/20717
dc.subject	Sporotrichum thermophile	en
dc.subject	Endo-1,4-beta-xylanase	en
dc.subject	Purification	en
dc.subject	Hemicellulose	en
dc.subject	Mass spectrometric sequencing	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.classification	Engineering, Chemical	en
dc.subject.other	CATALYTIC-PROPERTIES	en
dc.subject.other	PREDICTION	en
dc.subject.other	PROTEINS	en
dc.subject.other	ENDO-BETA-1,4-XYLANASE	en
dc.subject.other	GLYCOSYLATION	en
dc.subject.other	FAMILIES	en
dc.subject.other	SEQUENCE	en
dc.subject.other	ABILITY	en
dc.subject.other	FUNGI	en
dc.title	Purification, characterization and mass spectrometric identification of two thermophilic xylanases from Sporotrichum thermophile	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.procbio.2009.10.009	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.procbio.2009.10.009	en
heal.language	English	en
heal.publicationDate	2010	en
heal.abstract	Two xylanases were purified to electrophoretic homogeneity from the thermophilic fungus Sporotrichum thermophile grown in a submerged liquid culture using wheat straw as carbon source. The enzymes, StXyn1 and StXyn2, have molecular masses of 24 kDa and 48 kDa, respectively, and are optimally active at pH 5 and at 60 degrees C. Both enzymes displayed remarkable stability up to 50 degrees C for I h, exhibiting a half-life of 60 min (StXyn1) and 115 min (StXyn2) at 60 degrees C. Biochemical characterization of the two xylanases against poly- and oligosaccharides indicated that StXyn1 and StXyn2 hydrolytic profiles match those of xylanase family I I and family 10, respectively. LC-MS/MS analysis provided peptide mass and sequence information that assisted the identification of the corresponding xylanase genes from the S. thermophile genome and the classification of the two purified StXyn1 and StXyn2 as a family GH11 and GH10 endo-1,4-beta-xylanases, respectively. (C) 2009 Elsevier Ltd. All rights reserved.	en
heal.publisher	ELSEVIER SCI LTD	en
heal.journalName	PROCESS BIOCHEMISTRY	en
dc.identifier.doi	10.1016/j.procbio.2009.10.009	en
dc.identifier.isi	ISI:000275100900017	en
dc.identifier.volume	45	en
dc.identifier.issue	3	en
dc.identifier.spage	419	en
dc.identifier.epage	424	en