Entrapment of β-galactosidase in polyvinylalcohol hydrogel

beta-Galactosidase isolated from Aspergillus oryzae was immobilized in lens-shaped polyvinylalcohol capsules (with activity 25 U g(-1)) giving 32% of its original activity. Immobilization did not change the pH optimum (4.5) of lactose hydrolysis. The relative enzyme activity during product inhibition testing was, in average, 10% higher for immobilized enzyme. No decrease of activity was observed after 35 repeated batch runs and during 530 h of continuous hydrolysis of lactose (10%, w/v) at 45 degrees C. The immobilized enzyme was stable for 14 months without any change of activity during the storage at 4 degrees C and pH 4.5.