[Catalytic properties and stability of catalase in reversed micelles of aerosol OT in octane].
The catalytic function of catalase and its peroxidatic activity during tetramethylbenzidine (TMB) oxidation by cumene hydroperoxide were studied in reversed micelles of Aerosol OT (AOT) in octane relative to the [H2O]/[AOT] ratio and the initial catalase concentration. The optimum conditions permitting to retain the catalytic activity of the enzyme and its ability to induce peroxidation of TMB, were found. The catalytic function of the enzyme was shown to be dependent on its concentration in AOT micelles. The catalase stability monitored by the catalytic reaction and the decrease of the Soret band were analyzed. Both processes have two phases differing by the rate constants of the pseudo-first order. The catalase inserted into AOT micelles is characterized by the high stability as compared to other hemoproteins (cytochrome P-450, myoglobin, hemoglobin, peroxidase) under identical conditions.
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D000818:Animals; D001555:Benzene Derivatives / Q000378:metabolism; D001560:Benzidines / Q000378:metabolism; D002374:Catalase / Q000378:metabolism*; D002384:Catalysis; D002417:Cattle; D004143:Dioctyl Sulfosuccinic Acid; D004795:Enzyme Stability; D008099:Liver / Q000201:enzymology; D008823:Micelles; D009795:Octanes
D001555:Benzene Derivatives; D001560:Benzidines; D008823:Micelles; D009795:Octanes; D004143:Dioctyl Sulfosuccinic Acid; C021758:3,3',5,5'-tetramethylbenzidine; D002374:Catalase; C007164:cumene hydroperoxide; C026728:octane
Kataliticheskie svoĭstva i stabil'nost' katalazy v obrashchennykh mitsellakh aérozolia OT v oktane.