Characterization of Metalloprotease from Serratia marcescens

Authors

  • Syeda Sadaf Wajahat Department of Biosciences, Mohammad Ali Jinnah University, Karachi, Pakistan.
  • M. Kamran Azim Department of Biosciences, Mohammad Ali Jinnah University, Karachi, Pakistan.
  • Faizan Saleem Department of Biology, McMaster University, Hamilton, ON L8S 4K1, Canada

Abstract

Serratia marcescens is a gram-negative bacterium belonging to the family of Enterobacteriaceae. Here we report the characteristics of the bacterial peptidase produced by a novel S. marcescens isolate. Protease activity assays were conducted using different methods using casein as substrate. Protease activity was carried out at different temperatures and pH and using EDTA as inhibitor. The S. marcescens protease was partially purified by ammonium sulfate precipitation and gel filtration chromatography. Protease assay showed the activity of crude enzyme as 1.572 U/ml and 0.46 U/ml of partially purified protease. The S. marcescens protease was classified as metalloprotease as protease activity was inhibited by EDTA up to 83%. The optimum temperature and pH of this protease were 45 °C and 8.0 respectively.

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Published

2023-04-13

How to Cite

Wajahat, S. S., Azim, M. K., & Saleem, F. (2023). Characterization of Metalloprotease from Serratia marcescens. PAKISTAN JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, 55(2), 128–137. Retrieved from https://www.pjbmb.com/index.php/pjbmb/article/view/66