Production and characterization of α-galactosidase from Aspergillus flavipes

An extracellular α‐galactosidase from the culture filtrate of Aspergillus flavipes grown on melibiose as a carbon source was partially purified by hydroxylapatite and diethylaminoethylcellulose chromatographies. Electrophoretic analysis showed protein bands corresponding to α‐galactosidase and invertase activities. The optimum pH and temperature were determined as 4.5–5.0 and 45°C, respectively. The Km value for p‐nitrophenyl‐α‐d‐galactopyranoside was found to be 1.89 mm. The results reported in this study indicate that Aspergillus flavipes is indeed an active source of extracellular α‐galactosidase. Copyright © 2003 John Wiley & Sons, Ltd.