Purification and characterization of an extracellular alpha-L-arabinofuranosidase from Fusarium oxysporum.
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.
Christakopoulos
P
P
Department of Chemical Engineering, National Technical University of Athens, Attica, Greece.
Katapodis
P
P
Hatzinikolaou
D G
DG
Kekos
D
D
Macris
B J
BJ
D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D005670:Fusarium / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D013696:Temperature; D014990:Xylans / Q000378:metabolism
D014990:Xylans; C085118:arabinoxylan; D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase