EFFECT OF IMMOBILIZATION ON THE STABILITY AND SUBSTRATE SPECIFICITY OF α-D-GALACTOSIDASE ISOLATED FROM THE INVERTEBRATE TURBO CORNUTUS

Article abstract of DOI:10.1016/0008-6215(83)88051-3

A mixture of glycosidases from the liver of invertebrate Turbo cornutus was co-immobilized with bovine serum albumin in the form of membranes by use of glutaraldehyde as a crosslinking reagent.The properties of the native and immobilized α-D-galactosidase were compared.Immobilization incerased the stability of the α-D-galactosidase towards inactivation by heat, urea, or trypsin, and permitted repeated use of the membrane preparation wihout significant loss of activity.The untreated enzyme hydrolyzed the terminal α-D-galactopyranosyl group from melibiose, raffinose, stachyose, O-α-D-galactopyranosyl-(1<*>4)-O-β-D-galactopyranosyl-(1<*>4)-O-β-D-glucopyranosylceramide, and 2,3-di-O-acyl-1-O-6)-O-α-D-galactopyranosyl>-D-glycerol.The immobilized α-D-galactosidase also hydrolyzed the free oligosaccharides, but had no detectable activity towards the glycolipids.