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The extracellular metalloprotease ofSerratia marcescens: I. Purification and characterization

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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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Author notes

  1. P. S. Aiyappa

    Present address: Waksman Institute of Microbiology, Rutgers University, The State University of New Jersey, 08903, New Brunswick, New Jersey, USA

Authors and Affiliations

  1. Division of Biology, Kansas State University, 66506, Manhattan, Kansas, USA

    P. S. Aiyappa & J. O. Harris

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  1. P. S. Aiyappa
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  2. J. O. Harris
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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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