Purification and characterisation of a major xylanase with cellulase and transferase activities from Fusarium oxysporum

Christakopoulos, P; Kekos, D; Macris, BJ; Claeyssens, M; Bhat, MK

dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, BJ	en
dc.contributor.author	Claeyssens, M	en
dc.contributor.author	Bhat, MK	en
dc.date.accessioned	2014-03-01T01:12:13Z
dc.date.available	2014-03-01T01:12:13Z
dc.date.issued	1996	en
dc.identifier.issn	0008-6215	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/12010
dc.subject	hemicellulose	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	cellulose	en
dc.subject.other	transferase	en
dc.subject.other	xylan endo 1,3 beta xylosidase	en
dc.subject.other	article	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme analysis	en
dc.subject.other	enzyme purification	en
dc.subject.other	fusarium oxysporum	en
dc.subject.other	priority journal	en
dc.subject.other	Cellulase	en
dc.subject.other	Chromatography, Gel	en
dc.subject.other	Chromatography, High Pressure Liquid	en
dc.subject.other	Electrophoresis, Polyacrylamide Gel	en
dc.subject.other	Enzyme Stability	en
dc.subject.other	Extracellular Space	en
dc.subject.other	Fusarium	en
dc.subject.other	Glycosides	en
dc.subject.other	Glycosyltransferases	en
dc.subject.other	Hydrogen-Ion Concentration	en
dc.subject.other	Kinetics	en
dc.subject.other	Polysaccharides	en
dc.subject.other	Substrate Specificity	en
dc.subject.other	Temperature	en
dc.subject.other	Umbelliferones	en
dc.subject.other	Xylan Endo-1,3-beta-Xylosidase	en
dc.subject.other	Xylans	en
dc.subject.other	Xylosidases	en
dc.subject.other	Felis catus	en
dc.subject.other	Fusarium	en
dc.subject.other	Fusarium oxysporum	en
dc.title	Purification and characterisation of a major xylanase with cellulase and transferase activities from Fusarium oxysporum	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/0008-6215(96)00146-2	en
heal.identifier.secondary	http://dx.doi.org/10.1016/0008-6215(96)00146-2	en
heal.language	English	en
heal.publicationDate	1996	en
heal.abstract	A major xylanase from Fusarium oxysporum was purified to homogeneity by gel filtration, affinity, and ion-exchange chromatographies. It has a molecular mass of 60.2 kDa and pi of 6.6 and was optimally active at pH 7.4 and at 50 degrees C. The enzyme was stable over the pH range 5.8-8.2 at 40 degrees C for 24 h and lost 45% of its original activity at pH 9.0 under the identical conditions, The enzyme rapidly hydrolysed xylans from oat spelts (husks) and birchwood, but the activities on carboxymethylcellulose (CMC), filter paper, and Avicel were very low, Determination of k(cat)/K-m revealed that the enzyme hydrolysed oat spelts and birchwood xylans, 15-30 times more efficiently than CMC. In a 24 h incubation, at pH 7.0 and 9.0, the enzyme hydrolysed oat spelts and birchwood xylans by 75 and 65%, respectively, However, at pH 7.0, the enzyme released almost equal amounts of xylose and xylobiose from both xylans, whereas at pH 9.0, the concentration of xylobiose was twice as muchi as that of xylose and xylotriose. Xylanase attacked preferentially the internal glycosidic bonds of xylo- and 4-methylumbelliferyl cello-oligosaccharides [MeUmb(Glc)(n)]. The enzyme catalysed transglycosylation reaction with xylotriose, xylotetraose, and xylopentaose as donors and 4-methylumbelliferyl beta-D-glucoside (MeUmbGlc) as an acceptor. (C) 1996 Elsevier Science Ltd.	en
heal.publisher	ELSEVIER SCIENCE BV	en
heal.journalName	Carbohydrate Research	en
dc.identifier.doi	10.1016/0008-6215(96)00146-2	en
dc.identifier.isi	ISI:A1996VC55600008	en
dc.identifier.volume	289	en
dc.identifier.spage	91	en
dc.identifier.epage	104	en