Purification and characterization of an extracellular α- l -arabinofuranosidase from Fusarium oxysporum

Christakopoulos, P; Katapodis, P; Hatzinikolaou, D; Kekos, D; Macris, B

dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Katapodis, P	en
dc.contributor.author	Hatzinikolaou, D	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, B	en
dc.date.accessioned	2014-03-01T01:49:32Z
dc.date.available	2014-03-01T01:49:32Z
dc.date.issued	2000	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/25832
dc.subject	Enzyme	en
dc.subject	fusarium oxysporum	en
dc.subject	Ion Exchange	en
dc.subject	Synergistic Effect	en
dc.subject	Molecular Mass	en
dc.title	Purification and characterization of an extracellular α- l -arabinofuranosidase from Fusarium oxysporum	en
heal.type	journalArticle	en
heal.identifier.primary	10.1385/ABAB:87:2:127	en
heal.identifier.secondary	http://dx.doi.org/10.1385/ABAB:87:2:127	en
heal.publicationDate	2000	en
heal.abstract	An α-l-arabinofuranosidase from Fusarium oxysporum F3 was purified to homogeneity by a two-step ion exchange intercalated by a gel filtration chromatography. The enzyme had a molecular mass of 66 kDa and was optimally active at pH 6.0 and 60°C. It hydrolyzed aryl α-l-arabinofuranosides and cleaved arabinosyl side chains from arabinoxylan and arabinan. There was a marked synergistic effect between the	en
heal.journalName	Applied Biochemistry and Biotechnology	en
dc.identifier.doi	10.1385/ABAB:87:2:127	en