PURIFICATION AND SOME PROPERTIES OF ALPHA-GALACTOSIDASE FROM CANDIDA-GUILLIERMONDII H-404

Candida guilliermondii H-404, isolated from soil, produced thermostable alpha-galactosidase, but small amounts of other glycosidases (such as beta-galactosidase, alpha-glucosidase, and beta-glucosidase). The enzyme was separated into two fractions by DEAE-Toyopearl 650M chromatography, and the two enzymes were designated galactosidase I and II. These two enzymes had the same molecular weight (270,000 by gel filtration, 64,000 by SDS-PAGE). The isoelectric points of alpha-galactosidase I and II were 6.16 and 6.21, respectively. These two enzymes were different from each other in pH stability, temperature stability, and effects of Fe2+ and Cu2+ ion on alpha-galactosidase activity. The enzyme had stronger transfer activity and wider acceptor specificity than alpha-galactosidases which have been reported.