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*).
Horozova
E
E
Department of Physical Chemistry, University of Plovdiv, Bulgaria. horozova@argon.acad.bg
Dimcheva
N
N
Jordanova
Z
Z
D000097:Acetonitriles; D001585:Benzoyl Peroxide / Q000493:pharmacokinetics*; D001711:Biotransformation; D002151:Calorimetry; D002251:Carbon Tetrachloride; D002374:Catalase / Q000378:metabolism*; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000378:metabolism*; D007700:Kinetics; D012997:Solvents; D013696:Temperature
D000097:Acetonitriles; D004800:Enzymes, Immobilized; D012997:Solvents; D002251:Carbon Tetrachloride; D002374:Catalase; D001585:Benzoyl Peroxide; C032159:acetonitrile