Abstract
β-Galactosidase from Aspergillus oryzae was immobilized in crosslinked polyacrylamide gel beads. The presence of the enzyme inhibitor, such as glucono-δ-lactone or galactonoy-lactone, during polymerization procedure enhanced the residual enzymatic activity in the polymer beads, and activity yield attained up to 45%. Such enhancement effect was also observed when bovine serum albumin, dithiothreitol or glutathione was added during polymerization. Temperature and pH optima were not affected by the immobilization. The Michaelis constants for free and immobilized β-galactosidase were comparable. Lyophilized beads exhibited good stability without loss of enzymatic activity when stored at 4°C for 47 days.
