An alkaline protease produced by Pseudomonas aeruginosa MN1, isolated from an alkaline tannery waste water, was purified and characterized. The enzyme was purified 25-fold by gel filtration and ion exchange chromatography to a specific activity of 82350 U mg−1. The molecular weight of the enzyme was estimated to be 32000 daltons. The optimum pH and temperature for the proteolytic activity were pH 8.00 and 60°C, respectively. Enzyme activity was inhibited by EDTA suggesting that the preparation contains a metalloprotease. Enzyme activity was strongly inhibited by Zn2+, Cu2+ and Hg2+(5 mM), while Ca2+ and Mn2+ resulted in partial inhibition. The enzyme is different from other Pseudomonas aeruginosa alkaline proteases in its stability at high temperature; it retained more than 90% and 66% of the initial activity after 15 and 120 min incubation at 60°C. Journal of Industrial Microbiology & Biotechnology (2000) 24, 291–295.
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Received 09 June 1999/ Accepted in revised form 24 January 2000
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Bayoudh, A., Gharsallah, N., Chamkha, M. et al. Purification and characterization of an alkaline protease from Pseudomonas aeruginosa MN1. J Ind Microbiol Biotech 24, 291–295 (2000). https://doi.org/10.1038/sj.jim.2900822
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DOI: https://doi.org/10.1038/sj.jim.2900822