Peroxidase-Like Activity of Catalase Immobilized on Carbon Materials

Abstract

The immobilization of catalase was carried out from enzyme solutions in acid (pH < 3.5) and alkaline (pH > 11) medium on two kinds of soot differing by the average size of the particles. Under these conditions the peroxidase-like activity of immobilized catalase in the oxidation of phenol has been studied. The effect of the initial concentration of the substrate on the rate of the process catalysed by catalase immobilized on the soot of finer-grained structure has been studied. The relationships obtained are described by the equation of Michaelis- Menten. The kinetic parameters (the constant of Michaelis - K m , the maximum reaction rate - V max , the rate constant - k and the activation energy - E a ) of the process were calculated. It was found that catalase absorbed on the soot of larger globular particles does not take part in the peroxidase oxidation of phenol.