Immobilization of glucoamylase on gelatin by transition-metal chelation.
The potential applicability of glutaraldehyde-crosslinked-gelatin particles for the immobilization of enzymes by encapsulation has been extended by addition of surface-bound enzyme, leading ultimately to a method for the preparation of dual immobilized enzyme conjugates. Attachment of enzyme to the surface of the capsules was achieved by a transition-metal chelation process in which the incoming enzyme becomes a ligand. Glucoamylase was so immobilized, using titanium-urea, -acrylamide, -citric acid, and -lactose complexes or titanium (IV) chloride as means of introducing the titanium chelating centre. The retentions of enzyme activity for both the surface-bound and pre-encapsulated enzymes were functions of the chelating complex chosen. Differences were observed between the action patterns of the two forms of immobilized enzyme. These action patterns and the production of reversion products are discussed in the light of application of gelatin-immobilized glucoamylase to the production of high-DE glucose syrups.
D002614:Chelating Agents; D002850:Chromatography, Gel; D004800:Enzymes, Immobilized / Q000378:metabolism; D005780:Gelatin; D005087:Glucan 1,4-alpha-Glucosidase / Q000378:metabolism; D005959:Glucosidases / Q000378:metabolism; D008722:Methods; D009844:Oligosaccharides / Q000032:analysis; D014025:Titanium
D002614:Chelating Agents; D004800:Enzymes, Immobilized; D009844:Oligosaccharides; D005780:Gelatin; D014025:Titanium; D005959:Glucosidases; D005087:Glucan 1,4-alpha-Glucosidase