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Purification and characterization of an extracellular alpha-L-arabinofuranosidase from Fusarium oxysporum

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dc.contributor.author Christakopoulos, P en
dc.contributor.author Katapodis, P en
dc.contributor.author Hatzinikolaou, DG en
dc.contributor.author Kekos, D en
dc.contributor.author Macris, BJ en
dc.date.accessioned 2014-03-01T01:50:08Z
dc.date.available 2014-03-01T01:50:08Z
dc.date.issued 2000 en
dc.identifier.issn 0273-2289 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/26003
dc.subject Fusarium oxysporum en
dc.subject alpha-L-arabinofuranosidase en
dc.subject purification en
dc.subject characterization en
dc.subject synergism en
dc.subject.classification Biochemistry & Molecular Biology en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other ASPERGILLUS-AWAMORI en
dc.subject.other XYLANASE en
dc.subject.other SYSTEMS en
dc.subject.other WALL en
dc.title Purification and characterization of an extracellular alpha-L-arabinofuranosidase from Fusarium oxysporum en
heal.type journalArticle en
heal.language English en
heal.publicationDate 2000 en
heal.abstract An alpha-L-arabinofuranosidase from Fusarium oxysporum 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 degrees C. It hydrolyzed aryl alpha-L-arabinofuranosides and cleaved arabinosyl side chains from arabinoxylan and arabinan. There was a marked synergistic effect between the alpha-L-arabinofuranosidase and an endo-(1-->4)-beta-D-xylanase produced by F. oxysporum in the extensive hydrolysis of arabinoxylan. en
heal.publisher HUMANA PRESS INC en
heal.journalName APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY en
dc.identifier.isi ISI:000088567900006 en
dc.identifier.volume 87 en
dc.identifier.issue 2 en
dc.identifier.spage 127 en
dc.identifier.epage 133 en


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