[Immobilization of Penicillium vitale Pidopl. et Bilai catalase by inorganic carriers].
An efficient method is developed for P. vitale catalase immobilization through the oxidized carbohydrate enzyme component, using silochrome. The method provides the enzyme binding without losing its catalytic capacity in the immobilized preparation. When the enzyme is immobilized by high-dispersed silica containing isocyanate, aldehyde groups or active atoms of chlorine, 8, 15, and 20 mg of the enzyme is bounded per 1 g of the carrier, respectively, its catalytic capacity being completely retained. A dependence is established for the degree of catalase bonding and catalytic capacity of the immobilized enzyme of the enzyme carrier ratio in immobilization. The catalytic activity of the immobilized catalase preparations reaches 2 000 Becker units/l g. The preparations are stable in storage. Some of their properties are studied.
D002374:Catalase / Q000378:metabolism*; D004355:Drug Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D007700:Kinetics; D010407:Penicillium / Q000201:enzymology*; D012822:Silicon Dioxide
D004800:Enzymes, Immobilized; D012822:Silicon Dioxide; D002374:Catalase
Immobilizatsiia katalazy Penicillium vitale Pidopl. et Balai na neorganicheskikh nositeliakh.