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

✍ Scribed by Douglas Shepard; Mark Donovan; E. Raghupathy; Kwok-Kam Yeung; Albert J. Owen; Joel A. Dain

• Publisher: Elsevier Science
• Year: 1983
• Tongue: English
• Weight: 458 KB
• Volume: 118
• Category: Article
• ISSN: 0008-6215
• DOI: 10.1016/0008-6215(83)88051-3

✦ Synopsis

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.

The immobilized (Y-D-galactosidase also hydrolyzed the free oligosaccharides. but had no detectable activity towards the glycolipids.