Scholarly record

ENZYMATIC KINETICS OF THE OXIDATION OF 2,3,6-TRIMETHYLPHENOL IN THE PRESENCE OF IMMOBILIZED PEROXIDASE

Ольга Валентиновна Гребенникова, Александрина Михайловна Сульман, E. I. Shimanskaya, Esther Sulman, Valentin Yu. Doluda

Abstract

At the present stage of development of the biotechnological industry, the most promising objects are enzymes of the oxidoreductase class, which are capable of catalyzing redox processes. One of the most studied enzymes of this class is horseradish root peroxidase. Its immobilization on various carriers allows the biocatalyst to be reused in various technological processes. In recent years, magnetic nanoparticles have been increasingly used as effective carriers of enzymes.In this work, we study the oxidation of 2,3,6-trimethylphenol using horseradish root peroxidase as a catalyst immobilized on magnetic nanoparticles - Fe3O4, SiO2, Al2O3. As a result of such oxidation, an intermediate of vitamin E, 2,3,5-trimethylhydroquinone, was obtained. During the experiments, the kinetics of the oxidation of 2,3,6-trimethylphenol was studied using hydrogen peroxide as an affordable and inexpensive oxidant. The highest activity was 0.237 units/g(cat.), As compared with the native enzyme (0.346 units/g(cat)) Showed peroxidase immobilized on Fe3O4. When the enzyme was immobilized on inorganic carriers of SiO2 and Al2O3, the activity of biocatalysts was slightly lower (0.218 and 0.180 units/g(cat.), Respectively). The thermodynamic parameters ?S? and ?H? were also determined in the work. For the native HRP, ?S? = 36.4 J/mol*K and ?H? = 110.5 kJ/mol. For HRP immobilized on Fe3O4, ?S? = 2.38 J/mol*K and ?H? = 102.45 kJ/mol. The data obtained show that the immobilized enzyme is a good and effective catalyst for the oxidation of substituted phenols. The resulting catalytic systems are highly stable and can be reused, which leads to the efficiency of this method of biochemical environmentally friendly production of vitamins.

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