Hydrolysis of Galactose from Glycolipids and Glycoprotein by Young Rat Brain β-Galactosidases Immobilized to Sepharose 4B

An extract of glycosidic enzymes from young rat brain was immobilized to cyanogen bromide-activated Sepharose 4B. Most glycosidases retained approximately 10-25% of their activities after immobilization. Immobilized β-galactosidases were used repeatedly without detectable loss of enzyme activity in the hydrolysis of p-nitrophenyl-β-d -galactopyranoside. In addition to the synthetic substrate, the immobilized rat brain β-galactosidases could also hydrolyze galactose from lactose, galactosylcerebroside, asialofetuin, and GM₁-ganglioside. The hydrolysis of GM₁- to GM₂-ganglioside was confirmed on TLC.