Production and characterization of alpha-galactosidase from Aspergillus flavipes

Abstract

An extracellular a-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 alpha-galactosidase and invertase activities. The optimum pH and temperature were determined as 4.5-5.0 and 45degreesC, respectively. The Km value for p-nitrophenyl-alpha-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 a-galactosidase. Copyright (C) 2003 John Wiley Sons, Ltd.