Enzyme-catalyzed decomposition of dibenzoyl peroxide in organic solvents.

Catalytic activity of catalase (CAT, EC 1.11.1.6), immobilized on carbon black NORIT and soot PM-100, with respect to decomposition of dibenzoyl peroxide (BPO) in non-aqueous media (acetonitrile and tetrachloromethane), was investigated with a quantitative UV-spectrophotometrical approach. Progress of the above reaction was controlled by selected kinetic parameters: the apparent Michaelis constant (Km(app)), the specific rate constant (k(sp)), the activation energy (Ea), the maximum reaction rate (Vmax), and the Arrhenius' pre-exponential factor (Z0). Conclusions on the tentative mechanism of the catalytic process observed were drawn from the calculated values of the Gibbs energy of activation (deltaG*), the enthalpy of activation (deltaH*), and entropy of activation (deltaS*).