Effect of immobilization on the stability and substrate specificity of α-d-galactosidase isolated from the invertebrate Turbo cornutus (original) (raw)

A mixture of glycosidases from the liver of the 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 Lu-D-galactosidase were compared. Immobilization increased the stability of the a-D-galactosidase towards inactivation by heat. urea, or trypsin. and permitted repeated use of the membrane preparation without significant loss of activity. The untreated enzyme hydrolyzed the terminal cu-D-galactopyranosyl group from melibiose, raffinose. stachyose. O-cu-D-galactopyranosyl-( l&+4)-O-P-D-galactopyranosyl-( l-+4)-O-/3-D-glucopyranosylceramide. and 2.3-di-cl-acyl-l-O-[O-P-Dgalactopyranosyl-( l--+6)-O-cr-D-galactopyranosyl]-D-glycerol.