Abstract
Immobilized buckwheat α-glucosidase was prepared in bead shape by radiopolymerization of synthetic monomers. The most suitable ratio of the mixture of acrylamide containing methylenebisacrylamide, potassium acrylate, magnesium acrylate and enzyme solution was found to be 1:1:2:1. The highest activity of the immobilized enzyme was about 50% of that of the native enzyme. Optimum pH was shifted to acidic values by about 0.5 unit by the immobilization. The immobilization increased the stability of the enzyme against heat. Soluble starch was not so good substrate as maltose for the immobilized enzyme, though both substrates were hydrolyzed well by the native enzyme. Nigerose, kojibiose and so on were also produced from maltose or starch sugar by the transglucosylating activity of the immobilized α-glucosidase, as in the case of the native enzyme. A column system of the immobilized enzyme was useful to the enzymatic synthesis of various oligosaccharides.
