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A proteolytic enzyme produced by a cassava-fermenting strain of Micrococcus luteus was extracted and purified 50-fold by gel filtration and ion exchange chromatography. The optimum pH for the enzyme was 7.0, the optimum temperature 25 °C, the apparent molecular weight 42 kDa and the Km value, 0.45 mg ml-1 with casein as substrate. The enzyme was stimulated by Ca2+ and Mg2+ but inhibited by Zn2+ and Co2+ ions. Other inhibitors were EDTA, KCN, citric acid and L-cysteine indicating the enzyme todoi:10.1515/znc-1996-5-623 fatcat:stn4hgvv5nfuvnyxi55sqlzope