Kinetics of laccase-catalyzed oxidative polymerization of catechol

Oxidative polymerization of catechol catalyzed by laccase enzyme from Trametes versicolor (ATCC 200801) in aqueous solution containing acetone was investigated in a batch system. The effects of initial catechol and dissolved oxygen concentrations on the initial reaction rate of oxidative polymerization were experimented. An interactive kinetic model as a function of catechol and dissolved oxygen concentrations was developed for enzymatic polymerization and corresponding biokinetic parameters have been evaluated for the first time. The parameters of the model, Vmax, Kmm, KmO2 and Ki were found 0.247 g O2 m−3 min−1, 70.75 g m−3, 10.4 g m−3 and 48.15 g m−3, respectively. The activation energy and reaction rate constant of oxidative catechol polymerization were calculated as 66.8 kJ mol−1 and 216.3 s−1, respectively. The estimated activation energy and rate constant of the reaction are of the order of magnitude with previously reported values for laccase-catalyzed reactions of different monomers.