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[Coimobilization of superoxide dismutase, catalase and peroxidase]
1Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, ul. Kuprevicha 5/2, Minsk, 220141 Belarus. enzyme@ns.iboch.ac.by
Abstract:
For preparationing the polyenzyme antioxidant complex, containing superoxide dismutase (SOD), catalase and horseradish peroxidase (HRP), the different successivities of those enzymes co-immobilization were compared. The optimum successivity is provided by simultaneous co-immobilization of covalently bound HRP with the SOD and catalase. The catalytic enzyme activity and the catalase operational stability was kinetically characterized in various samples. For one sample, the influence of ascorbate, glutathione and ethanol on the catalase kinetic parameters was studied. A possible scheme of different processes at the H2O2 decomposition in the presence of co-immobilized SOD, catalase, HRP and the substrates-reductans was discussed.