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STUDY OF PROPERTIES OF GLUCOSE OXIDASE IMMOBILIZED ON MODIFIED WITH CHITOSAN AND SODIUM TRIPOLYPHOSPHATE MAGNETITE
Abstract
A new biocatalyst based on glucose oxidase immobilized on Fe3O4 magnetite nanoparticles modified with chitosan and sodium tripolyphosphate was synthesized. Magnetite nanoparticles were obtained by mixing solutions of FeCl2 and FeCl3 with ammonia while heating to a temperature of 65 ?C. To stabilize the nanoparticles and ensure the presence of amino groups on their surface, chitosan and sodium tripolyphosphate were sequentially deposited on magnetite. Immobilization of glucose oxidase on the support was carried out after preliminary activation of the carboxyl groups of the enzyme by 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride and N-hydroxysuccinimide. The activity and stability of the biocatalyst were investigated in the oxidation reaction of D-glucose to D-glucono-?-lactone. The immobilized biocatalyst was shown to retain more than 60% of the activity compared to the native form of the enzyme. The synthesized biocatalyst can be easily separated from the reaction mixture by a permanent magnet and reused without significant loss of activity. The optimal composition of the biocatalyst providing the maximum activity and operational stability was determined. It has been shown that the immobilization of glucose oxidase on modified magnetite leads to an expansion of the operating range of pH and temperatures by 15-20%, compared with the native enzyme. The successful modification of the magnetite with a fine layer of chitosan as well as the presence of target functional groups on the support surface were confirmed by the Fourier-transform infrared spectroscopy and low-temperature nitrogen adsorption.
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