Purification and characterization of an extracellular alpha-L-arabinofuranosidase from Fusarium oxysporum
2000
Christakopoulos, P. | Katapodis, P. | Hatzinikolaou, D.G. | Kekos, D. | Macris, B.J.
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 of 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 to 4)-beta-D-xylanase produced by F. oxysporum in the extensive hydrolysis of arabinoxylan.
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