The present study was concerned with the characterization of partially purified extracellular α-amylase from Candida glabrata isolated from soil and using whey as substrate. The production is carried out under optimum conditions, after 4 days of incubation; the enzyme was partially purified by ammonium sulfate precipitation. A trial for the purification of α-amylase resulted in an enzyme with specific activity of (78.88 units/mg protein) with (2.73 folds) purification. The partially purified α-amylase showed highest activity at pH 6.0. The α-amylase activity increased as the increase of enzyme concentration. The optimum substrate concentration (starch) was 0.4 % while the optimum incubation temperature was 55 ºC. The Michealis constant (Km) and the maximum velocity (Vmax) determined from Lineweaver-Burk plots of initial velocity data at different concentrations of the substrate were, respectively 0.27 mg/ml and 1016.26 μg/ml. This study indicated that this yeast can be exploited for production of α-amylase for biotechnological and industrial applications.

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