[Covalent immobilization of catalase on molded cellulose carriers]

We optimized the conditions of the covalent binding of bovine liver catalase to phosphate-cellulose matrices (gauze, granules, and paper with various surface density) and to acetate-cellulose porous membranes of different productivity. The capacity of the catalase binding to the molded cellulose carriers depends on the physico-chemical characteristics of the latter. The maximum concentration of the bound catalase after periodate oxidation of the carriers at room temperature was determined. The catalytic activity of the immobilized enzyme was quantified; under optimal conditions it is 24% for acetate-cellulose membranes and 24.3% for phosphate-cellulose paper and reduces with the increase of the total protein binding capacity of both the carriers.