Catalytic properties and stability of catalase in reversed micelles of aerosol OT in octane
Artemchik, V.D.; Eremin, A.N.; Metelitsa, D.I.
Biokhimiia 55(2): 293-298
1990
ISSN/ISBN: 0320-9725 PMID: 1692742 Document Number: 350069
The catalactic 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 catalatic activity of the enzyme and its ability to induce proxidatic oxidation of TMB, were found. The catalatic function of the enzyme was shown to be dependent on its concentration in AOT micelles. The catalase stability monitored by the catalatic 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.