Christakopoulos P, Katapodis P, Hatzinikolaou D G, Kekos D, Macris B J
Department of Chemical Engineering, National Technical University of Athens, Attica, Greece.
Appl Biochem Biotechnol. 2000 May;87(2):127-33. doi: 10.1385/abab:87:2:127.
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.
