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The crucial roles of proteases in food and other industries stimulate research to find additional sources of the enzyme especially from non-conventional sources. In this study, protease was partially characterized from Jatropha curcas leaves.The enzyme had pH and temperature optima of 4.0 and 45oC respectively. A decline in residual activity of the enzyme was observed at above 45oC and the activation energy (Ea) from Arrhenius plot was 0.57kJ/mol. The enzyme showed specificity in the order; casein>hemoglobin> albumin> ovalbumin. Initial velocity studies for the determination of kinetic parameters revealed a KM and Vmax of 0.48 mg/ml and 0.014µmol/min respectively with a computed index of physiological efficiency (Kcat) of 0.029 min-1. Furthermore, Dixon-Webb’s plot identified ionizable groups at the active site with pKa1 and pKa2 of 5.0 and 5.3 respectively as well as an enthalpy of ionization of 0.047 kcal/mol implicating aspartate as an important amino acid at the active site of the enzyme. The protease was highly sensitive to cysteine protease specific inhibitor iodoacetate while 1,10phenanthroline and ethylenediaminetetraacetate slightly inhibited the enzyme. Data from this study suggest that J. curcas protease possesses closely similar properties to other known industrial proteases

Partial Characterization of Protease from the Leaves of Jatropha curcas