Amund, Olukayode O.Omidiji, O.2019-06-242019-06-241990-03-01Amund, O. O., Omidiji, O., & Ilori, O. (1990). Purification and properties of a neutral protease produced by Lactobacillus brevis. Journal of biotechnology, 13(4), 361-365.https://doi.org/10.1016/0168-1656(90)90083-Nhttp://repository.elizadeuniversity.edu.ng/handle/20.500.12398/123A proteolytic enzyme was produced by a strain of Lactobacillus brevis isolated from an oriental beverage. The enzyme 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 35°C and the molecular weight 34,674 Da. Furthermore, the enzyme was stimulated by cations including Ca2+, Mg2+, Na+ and K+ and inhibited by Zn2+ and Co2+ ions. Other inhibitors were EDTA, ascorbic acid and citric acid. The enzyme is probably a neutral metalloprotease.enLactobacillusProteasepHTemperatureCationArticle