Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F3

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	2014-03-01T01:12:13Z
dc.date.available	2014-03-01T01:12:13Z
dc.date.issued	1996	en
dc.identifier.issn	0168-1656	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/12011
dc.subject	Enzyme purification	en
dc.subject	Fusarium oxysporum	en
dc.subject	Partial amino acid sequence	en
dc.subject	Xylanase	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	Cellulose	en
dc.subject.other	Chemical bonds	en
dc.subject.other	Enzyme kinetics	en
dc.subject.other	Enzymes	en
dc.subject.other	High pressure liquid chromatography	en
dc.subject.other	Hydrolysis	en
dc.subject.other	Ion exchange	en
dc.subject.other	Molecular weight	en
dc.subject.other	pH	en
dc.subject.other	Purification	en
dc.subject.other	Reaction kinetics	en
dc.subject.other	Thermodynamic stability	en
dc.subject.other	Isoelectric points	en
dc.subject.other	Partial amino acid sequence	en
dc.subject.other	Xylanase	en
dc.subject.other	Biotechnology	en
dc.subject.other	alkaline xylanase	en
dc.subject.other	unclassified drug	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	controlled study	en
dc.subject.other	enzyme analysis	en
dc.subject.other	enzyme purification	en
dc.subject.other	fusarium oxysporum	en
dc.subject.other	nonhuman	en
dc.subject.other	priority journal	en
dc.subject.other	Amino Acid Sequence	en
dc.subject.other	Biotechnology	en
dc.subject.other	Chromatography, Gel	en
dc.subject.other	Chromatography, Ion Exchange	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 Homology, Amino Acid	en
dc.subject.other	Substrate Specificity	en
dc.subject.other	Xylan Endo-1,3-beta-Xylosidase	en
dc.subject.other	Xylosidases	en
dc.subject.other	Fusarium	en
dc.subject.other	Fusarium oxysporum	en
dc.title	Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F3	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/0168-1656(96)01619-7	en
heal.identifier.secondary	http://dx.doi.org/10.1016/0168-1656(96)01619-7	en
heal.language	English	en
heal.publicationDate	1996	en
heal.abstract	Two low molecular mass endo-1,4-β-D-xylanases from Fusarium oxysporum were purified to homogeneity by gel-filtration and ion-exchange chromatography. They exhibit molecular masses of 20.8 (xylanase I) and 23.5 (xylanase II) kDa, and isoelectric points of 9.5 and 8.45-8.70, respectively. Both xylanases display remarkable pH (9.0) stability. At 40 to 55°C xylanase II is more thermostable than xylanase I but less active on xylan. In contrast to xylanase I, xylanase II is able to hydrolyze 1-O-4-methylumbelliferyl-(β-D-glucopyranosyl)-β-D-xylopyranoside (muxg). Neither of these enzymes hydrolyze xylotriose. They bind on crystalline cellulose but not on insoluble xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that both enzymes cleave preferentially the internal glycosidic bonds of xylopentaose and oat spelts xylan. Thus the purified enzymes appeared to be true endo-β-1,4-xylanases. The amino terminal sequences of xylanases I and II show no homology. Xylanase I shows high similarity with alkaline low molecular mass xylanases of family G/11.Two low molecular mass endo-1,4-β-D-xylanases from Fusarium oxysporum were purified to homogeneity by gel-filtration and ion-exchange chromatography. They exhibit molecular masses of 20.8 (xylanase I) and 23.5 (xylanase II) kDa, and isoelectric points of 9.5 and 8.45-8.70, respectively. Both xylanases display remarkable pH (9.0) stability. At 40 to 55 °C xylanase II is more thermostable than xylanase I but less active on xylan. In contrast to xylanase I, xylanase II is able to hydrolyze 1-O-4-methylumbelliferyl-(β-D-glucopyranosyl)-β-D-xylopyranoside (muxg). Neither of these enzymes hydrolyze xylotriose. They bind on crystalline cellulose but not on insoluble xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that both enzymes cleave preferentially the internal glycosidic bonds of xylopentaose and oat spelts xylan. Thus the purified enzymes appeared to be true endo-β-1,4-xylanases. The amino terminal sequences of xylanases I and II show no homology. Xylanase I shows high similarity with alkaline low molecular mass xylanases of family G/11.	en
heal.publisher	Elsevier Science B.V., Amsterdam, Netherlands	en
heal.journalName	Journal of Biotechnology	en
dc.identifier.doi	10.1016/0168-1656(96)01619-7	en
dc.identifier.isi	ISI:A1996VU83500010	en
dc.identifier.volume	51	en
dc.identifier.issue	2	en
dc.identifier.spage	181	en
dc.identifier.epage	189	en