Model development for horseradish peroxidase catalyzed removal of aqueous phenol

Abstract

Once activated by hydrogen peroxide, horseradish peroxidase (HRP) catalyzes the oxidation of aqueous aromatic compounds to produce high molecular weight polymers of low solubility. A pseudo steady-state kinetic model of the HRP-hydrogen peroxide-aromatic compound system was modified to incorporate enzyme inactivation mechanisms in order to improve its predictive ability. The kinetic constants of the model were calibrated using a series of experimental data sets. The model's ability to predict the time-dependent removal of phenol within the range of 0.5-6 mM from a batch reactor was validated. The model accounts for permanent losses of enzyme activity through inactivation by free radicals as well as interaction with end-product polymers as they form.