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Purification and characterization of an extracellular α-L- arabinofuranosidase from Fusarium oxysporum
Laboratory of Biotechnology, Department of Chemical Engineering, National Technical University of Athens.
Laboratory of Biotechnology, Department of Chemical Engineering, National Technical University of Athens.
Laboratory of Biotechnology, Department of Chemical Engineering, National Technical University of Athens.
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2000 (English)In: Applied Biochemistry and Biotechnology, ISSN 0273-2289, E-ISSN 1559-0291, Vol. 87, no 2, p. 127-133Article in journal (Refereed) Published
Abstract [en]

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 α-L-arabinofuranosidase and an endo-(1→4)-β-D-xylanase produced by F. oxysporum in the extensive hydrolysis of arabinoxylan.

Place, publisher, year, edition, pages
2000. Vol. 87, no 2, p. 127-133
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URN: urn:nbn:se:ltu:diva-3296DOI: 10.1385/ABAB:87:2:127ISI: 000088567900006PubMedID: 10949693Scopus ID: 2-s2.0-0033866230Local ID: 11ac7c18-16ea-4045-a3ac-f58a8e4f8239OAI: oai:DiVA.org:ltu-3296DiVA, id: diva2:976153
Note

Upprättat; 2000; 20130212 (cani)

Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2023-09-05Bibliographically approved

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