Purification and characterization of catalase enzyme from fiery milkcap mushrooms (Lactarius pyragalus) growing in Giresun region

Catalase allows hydrogen peroxide, a stable and strong oxidizing agent, to be broken down by catalyzing the conversion of water and molecular oxygen. The catalase enzyme not only catalyses the catalytic degradation of hydrogen peroxide (detoxification), but also toxic compounds containing phenols, formic acid, formaldehyde and alcohols act as an oxidizing agent and also use hydrogen peroxide as a substrate. Catalase is an enzyme widely used in hydrogen peroxide or glucose biosensors for analytical purposes in the removal of hydrogen peroxide used for bleaching, oxidizing or sterilizing purposes. In this study, the catalase enzyme was first purified from hazelnut fungus (Lactarius pyragalus) grown in and around Giresun province and its kinetic properties were investigated. Optimum pH and temperature values, pH and temperature stability, optimum reaction time, optimum reaction time specification, appropriate enzyme and substrate concentration were determined. The optimum pH of catalase purified from bovine mushroom was found to be 8,0 and the optimum temperature to be 20 °C. The Km and Vmax values for the hydrogen peroxide (H2O2) substrate at the optimum pH and temperature of Lactarius pyragalus catalase enzyme were determined by Linewear-Burk method. The Km and Vmax values were found to be 0.310 mM and 62.112 U. The purified enzyme, which showed SDS-PAGE, had a molecular weight of 12 kDa. In this thesis, the catalase enzyme, the uses of catalase enzyme and the methods of catalase activity determination are mentioned.