Physiochemical properties of purified Catalase enzyme from Azolla

Enzymes are the reaction catalysts of biological systems which accelerate and direct specific biochemical reactions. Antioxidant enzymes are capable of stabilizing, or deactivating free radicals before they attack cellular components. Catalase catalyzes the reduction of hydroperoxides, thereby protecting mammalian cells against oxidative damage. The aim of the project is to analyze the presence of antioxidant enzyme and to purify the enzyme from the aquatic fern Azolla. The catalase enzyme presence was confirmed by standard assay procedure and purified through DEAE cellulose and Sephadox G-75 Column chromatography. The purified catalase enzyme was subjected for Molecular weight determination by SDS-PAGE analysis. Since the separated enzyme appeared as a single band, it was concluded that catalase enzyme as tetrameric. The purified catalase was found about 55,000 Da molecular weight. Maximum enzyme activity observed at pH 7 which was the optimum pH level of the catalase enzyme purified from Azolla and the optimum temperature level was 10°C.