Summary
An extracellular protease ofSerratia marcescens produced during growth on skim milk medium was isolated by ethanol precipitation. The protease was purified by salt fractionation, DEAE-cellulose ion exchange chromatography and gel filtration chromatography on Agarose P-100. It has a broad optimum from pH 6.0 to 9.0 and a temperature optimum of 45°C for proteolytic activity on casein. It was classified as a metallo-protease by virtue of its inactivation by metal-ion chelators and reactivation by ferrous ions. Proteolytic activity was not affected by diiso-propylfluorophosphate, p-chloromercuribenzoate and dithiothreitol.
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Aiyappa, P.S., Harris, J.O. The extracellular metalloprotease ofSerratia marcescens: I. Purification and characterization. Mol Cell Biochem 13, 95–100 (1976). https://doi.org/10.1007/BF01837059
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DOI: https://doi.org/10.1007/BF01837059