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PARTIAL PURIFICATION AND CHARACTERIZATION OF AN ACID INVERTASE FROM SACCHARUM OFFICINARUM L.
Abstract
An acid invertase was isolated and partially purified from mature sugarcane (var HSF 240) stem juice by a combination of Ammonium sulphate, DEAE-cellulose and gel filtration. The purified acid invertase had a specific activity of 17.05 Umg-1. Invertase was characterized for various parameters. The pH and temperature optima of the enzyme were 3.0 and 45°C respectively. The Km value and energy of activation (Ea) of the enzyme was 5mM and 21.37 kJmol-1, respectively. Irreversible thermal inactivation of the enzyme was studied at different temperatures that followed the first order kinetics. Different kinetic and thermodynamic parameters were also investigated. A slight increase in the activity of acid invertase was observed with Ca+2, Mn+2 and Mg+2 ions while Cd2+, Pb2+ and Hg2+ ions inhibited the activity.
