Purification and Characterization of Tyrosinase Enzyme from the Edible Kanl？ca Mushrooms (Lactarius salmonicolor)

Tyrosinase (EC 1.14.18.1) is an enzyme containing copper that found in fungi, high plants and animals. Furthermore, it is catalyses there actions oxidation to o-quinones of o-diphenols and hydroxylation of monophenolsto o-diphenols using molecular oxygen. In this study, tyrosinase enzyme was purified for the first time from Kanl？ca Mushroom (Lactarius salmonicolor) plenty of grown in Giresun Province and around and examined the kinetic properties. Optimum pH and temperature, pH and temperature stability, optimum reaction time, determining the optimum reaction time was the appropriate enzyme and substrate concentrations. The optimum pH of the purified tyrosinase from mushroom Kanl？ca 6.0 was found to be optimal at 40oC. The purified enzyme, which showed SDS-PAGE, had a molecular weight of 30 kDa.The Km and Vmax values of L. Salmonicolor tyrosinase toward were determined by Lineweaver Burk method