Partial Purification and Physicochemical Properties of Arginase from the Liver of Tillapia zilli

Abstract

The study of the catalytic and physicochemical characteristics of the Tilapia Zilli liver arginase was carried out to provide information describing the survival of this fish species in the gold-mine reservoir. Tilapia zilli liver arginase was isolated and partially purified with 80% ammonium sulphate precipitation and CM-Sephadex C-25 ion exchange chromatography. The enzyme was purified with a specific activity and yield of 51.721 U/mL and 12.35% respectively. The enzyme had Km and Vmax values of 25 mM and 6.77 U/mL, respectively. Enzyme activity was optimum at pH 6.0 and temperature of 80 °C. Fe2+ and Hg2+ were strong inhibitors of enzymes in the inhibitory experiments. The findings demonstrated that amino acids do not inhibit the enzyme. In summary, Tilapia zilli's survival in the gold mine reserve is significantly influenced by the physiological functions of its liver arginase.