Purification and mode of action of a low molecular mass endo-1,4-β- d-glucanase from Fusarium oxysporum

Christakopoulos, P; Kekos, D; Macris, B; Claeyssens, M; Bhat, M

dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, B	en
dc.contributor.author	Claeyssens, M	en
dc.contributor.author	Bhat, M	en
dc.date.accessioned	2014-03-01T01:43:25Z
dc.date.available	2014-03-01T01:43:25Z
dc.date.issued	1995	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/24115
dc.subject	Enzyme	en
dc.subject	fusarium oxysporum	en
dc.subject	High Pressure Liquid Chromatography	en
dc.subject	Ion Exchange Chromatography	en
dc.subject	Low Molecular Mass	en
dc.subject	Mode of Action	en
dc.title	Purification and mode of action of a low molecular mass endo-1,4-β- d-glucanase from Fusarium oxysporum	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/0168-1656(94)00147-5	en
heal.identifier.secondary	http://dx.doi.org/10.1016/0168-1656(94)00147-5	en
heal.publicationDate	1995	en
heal.abstract	A low molecular mass (23.2 kDa) endo-1,4-β-d-glucanase from Fusarium oxysporum was purified to homogeneity by gel-filtration and ion-exchange chromatographies. The enzyme was optimally active at pH 6.0 and at 50 ° C. It had a pI value of 8.6 and was stable at 55 ° C for 1 h. It hydrolyzed carboxymethylcellulose, cello-oligosaccharides (Glcn) and 4-methylumbelliferylcello-oligosaccharides but did not hydrolyze	en
heal.journalName	Journal of Biotechnology	en
dc.identifier.doi	10.1016/0168-1656(94)00147-5	en