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Appl Biochem Biotechnol. 2000 May;87(2):127-33.

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

Author information

1
Department of Chemical Engineering, National Technical University of Athens, Attica, Greece.

Abstract

An alpha-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 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.

PMID:
10949693
DOI:
10.1385/abab:87:2:127
[Indexed for MEDLINE]

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