[Features of covalent immobilization of catalase on cellulose membranes in reverse aerosol OT micelles in heptane].
Catalase was immobilized on periodate-activated cellulose membranes in a medium with the bicarbonate buffer and in reversed micelles of Aerosol OT in heptane. The enzyme effectively bound with the carriers in micellar media within a wide range of initial concentrations. The efficiency of immobilization depended on the volume of the polar phase in heptane, pH, and molarity of the bicarbonate buffer in reversed micelles, as well as on the process duration. The catalase covalently immobilized on cellulose membranes in reversed micelles was ten times more active compared to that immobilized on the same carrier in aqueous medium. Reversed micelles stabilized catalase at low concentrations of the enzyme in contact solution and hindered its inactivation on the carrier surface.
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D000818:Animals; D001665:Binding Sites; D002374:Catalase / Q000378:metabolism*; D002384:Catalysis; D002417:Cattle; D002482:Cellulose; D004143:Dioctyl Sulfosuccinic Acid; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006536:Heptanes; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology; D008567:Membranes, Artificial; D008823:Micelles; D013501:Surface-Active Agents
D004800:Enzymes, Immobilized; D006536:Heptanes; D008567:Membranes, Artificial; D008823:Micelles; D013501:Surface-Active Agents; D004143:Dioctyl Sulfosuccinic Acid; D002482:Cellulose; D002374:Catalase