Kinetic Properties of the Rhizopus Glucoamylase and Bacillus α-Amylase,which are Immobilized on Cellulofine

Glucoamylase from Rhizopus niveus was immobilized on Cellulofine, a kind of cellulose gel, to construct an enzyme-Cellulofine structure, of which the molar activities k₀ for maltose and for soluble starch were found almost equal to 4 and 1/9 times, respectively, of those found with the intact enzyme. Liquefying Bacillus α-amylase was fixed to make another enzyme-Cellulofine structure, of which ratio of the molar activities, k₀ (modified)/k₀ (intact) for an oligomer substrate maltohexaose is much larger than those for high-polymer substrates, amylose and soluble starch. These findings suggest that the substrate specificity of the amylase-Cellulofine structure is improved to be useful for the enzyme-catalyzed hydrolysis of saccharides having small degree of polymerization.