Kinetic evaluation of catalase and peroxygenase activities of tyrosinase

Amperometric O2 and H2O2 sensors are used to kinetically examine catalase activity (conversion of H2O2 to (1/2)O2 and H2O) and peroxygenase activity (H2O(sub 2-) dependent oxygenation of substrates) of mushroom tyrosinase. It is found that the catalase activity of mushroom tyrosinase is three-order of magnitude greater than that of mollusk hemocyanin.