[Effect of temperature and composition of frozen solutions on the rate of peroxidase oxidation of 2,3-dimethyl-1,4-naphthoquinol-1-dimethylphosphate]. / Vliianie temperatury i sostava zamorozhennogo rastvora na skorost' kataliziruemogo peroksidazoi okisleniia 2,3-dimetil-1,4-naftokhinol-1-dimetilfosfata.

The horseradish peroxidase-catalyzed oxidation of 2.3-dimethyl-1.4-naphthoquinol-1-dimethylphosphate by hydrogen peroxide was investigated within the temperature range of +20 divided by -35 degrees. The increase in the concentration of the buffer solution accelerated the reaction in liquid solutions at 0 degrees and 20 degrees. The unusual shapes of the curves of temperature dependences of the reaction rate in frozen solutions of different composition can probably be due to temperature variations in some physico-chemical parameters of the system under study.

[Effect of horse radish peroxidase immobilization on the kinetics of enzymatic oxidation of guaiacol in frozen solutions]. / Vliianie immobilizatsii peroksidazy na kinetiku fermentativnogo okisleniia gvaiakola v zamorozhennykh rastvorakh.

The kinetics of horse radish peroxidase (EC 1.11.1.7) catalyzed oxidation of guaiacol by hydrogen peroxide has been studied within the temperature region of +20--35 degrees C. The covalent attachment of the enzyme to polyacrylamide gel had no significant influence on the activation energy of the reaction in liquid solutions. For frozen solutions it was demonstrated that the temperature dependencies of the reaction rate differ greatly for the soluble and bound forms of the enzyme. The observed phenomenon is probably due to the differences in the molecular mobility, distribution and arrangement of reactants in frozen state.