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 α-l-arabinofuranosidase and an endo-(1 →4)-β-d-xylanase produced by F. oxysporum in the extensive hydrolysis of arabinoxylan.
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Christakopoulos, P., Katapodis, P., Hatzinikolaou, D.G. et al. Purification and characterization of an extracellular α-l-arabinofuranosidase from Fusarium oxysporum . Appl Biochem Biotechnol 87, 127–133 (2000). https://doi.org/10.1385/ABAB:87:2:127
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DOI: https://doi.org/10.1385/ABAB:87:2:127