Purification and Some Properties of α-Galactosidase from Penicillium purpurogenum

α-Galactosidase was purified by ion-exchange chromatographies on DEAE-cellulose and SE-cellulose columns from the culture filtrate of Penicillium purpurogenum No. 618. The final preparation was judged homogeneous by SDS-PAGE and its molecular mass and isoelectric point were estimated to be 67 kDa and 4.1, respectively. The N-terminal amino acid sequence of the enzyme was analyzed and aligned with those of other α-galactosidases. In addition, the enzyme acted on the stubbed α-galactosyl residue connected to the β-1,4-manno-oligosaccharide chain, indicating that this specificity was quite different from that of Mortierella vinacea α-galactosidase.