An extracellular alpha-amylase produced by a cassava-fermenting strain of Micrococcus luteus was purified 26-fold by gel filtration and ion-exchange chromatography. The molar mass was estimated to be approximately 56 kDa. The optimum temperature of the enzyme was 30 degrees C, optimum pH 6.0 and optimum substrate concentration was 0.6% (W/V). Treatment of the enzyme at 70 degrees C for 10 min resulted in 70% loss of activity. The activation energy was determined to be 34.8 kJ/mol. The activity of the enzyme was enhanced by Mg2+, Ca2+, K+, Na+ and inhibited by EDTA, KCN and citric acid. The enzyme may find some application in local food processing.