Partial Purification and Characterization of an Acid Invertase from Saccharum Officinarum L
نویسندگان
چکیده
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 Umg1. 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, 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, Mn and Mg ions while Cd, Pb and Hg ions inhibited the activity.
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