The alkaline xylanase III from Fusarium oxysporum F3 belongs to family F/10

Christakopoulos, P; Nerinckx, W; Kekos, D; Macris, B; Claeyssens, M

dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Nerinckx, W	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, B	en
dc.contributor.author	Claeyssens, M	en
dc.date.accessioned	2014-03-01T01:13:26Z
dc.date.available	2014-03-01T01:13:26Z
dc.date.issued	1997	en
dc.identifier.issn	0008-6215	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/12473
dc.subject	Enzyme purification	en
dc.subject	Fusarium oxysporum	en
dc.subject	Partial amino acid sequence	en
dc.subject	Xylanase	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Chemistry, Applied	en
dc.subject.classification	Chemistry, Organic	en
dc.subject.other	glucoside	en
dc.subject.other	umbelliferone derivative	en
dc.subject.other	xylan endo 1,3 beta xylosidase	en
dc.subject.other	amino acid sequence	en
dc.subject.other	article	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme isolation	en
dc.subject.other	enzyme purification	en
dc.subject.other	fusarium oxysporum	en
dc.subject.other	gel filtration	en
dc.subject.other	ion exclusion chromatography	en
dc.subject.other	nonhuman	en
dc.subject.other	priority journal	en
dc.subject.other	Amino Acid Sequence	en
dc.subject.other	Amino Acids	en
dc.subject.other	Endo-1,4-beta Xylanases	en
dc.subject.other	Enzyme Stability	en
dc.subject.other	Fusarium	en
dc.subject.other	Hydrogen-Ion Concentration	en
dc.subject.other	Isoelectric Point	en
dc.subject.other	Molecular Sequence Data	en
dc.subject.other	Molecular Weight	en
dc.subject.other	Sequence Analysis	en
dc.subject.other	Sequence Homology, Amino Acid	en
dc.subject.other	Substrate Specificity	en
dc.subject.other	Xylosidases	en
dc.subject.other	Fusarium	en
dc.subject.other	Fusarium oxysporum	en
dc.subject.other	Triticum aestivum subsp. spelta	en
dc.title	The alkaline xylanase III from Fusarium oxysporum F3 belongs to family F/10	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/S0008-6215(97)00075-X	en
heal.identifier.secondary	http://dx.doi.org/10.1016/S0008-6215(97)00075-X	en
heal.language	English	en
heal.publicationDate	1997	en
heal.abstract	Xylanase III from Fusarium oxysporum F3 was purified to homogeneity by ion-exchange chromatography and gel filtration. The enzyme has a molecular mass of 38 kDa, an isoelectric point of 9.5, and is maximally active on oat spelt xylan at pH 7 and 45 degrees C with a K-m of 0.8 mg/mL. The xylanase displays remarkable stability at pH 9.0. It is not active on xylotriose but hydrolyzes the 4-methylumbelliferyl glycosides of beta-xylobiose and beta-D-glucopyranosyl-(1 --> 4)-beta-D-xylopyranose and to a lower extent 4-methylumbelliferyl beta-cellobioside. When acted on xylooligosaccharides and xylan, analysis of reaction mixtures by high-pressure liquid chromatography shows preferred internal glycoside cleavage. Thus the purified enzyme appears to be a true endo-beta-1,4-xylanase. Partial amino acid analysis of xylanase III shows high sequence homology with xylanases of family F/10. (C) 1997 Elsevier Science Ltd.	en
heal.publisher	ELSEVIER SCI LTD	en
heal.journalName	Carbohydrate Research	en
dc.identifier.doi	10.1016/S0008-6215(97)00075-X	en
dc.identifier.isi	ISI:A1997XR58000008	en
dc.identifier.volume	302	en
dc.identifier.issue	3-4	en
dc.identifier.spage	191	en
dc.identifier.epage	195	en