1984 Volume 31 Issue 3 Pages 156-160
An α-amylase from Bacillus subtilis (liquefying type) was immobilized on partially imido esterized granular polyacrylonitrile (PAN) by an amidination reaction . The action patterns in the hydrolysis of soluble starch were compared between the native and the immobilized α-amylase . The hydrolysis character of immobilized α-amylase was not basically changed except for retardation in the production of oligosaccharides due to diff usional limitation and the deficiency of maltohexaose production potency. The amount of glucose production by a combination of the enzymatic reactions by the immobilized α-amylase with the native glucoamylase was also studied at 40°C. Approximately the same glucose amount was attained between the native and the immobilized α-amylase in the successive hydrolysis by glucoamylase.
