Enhanced Production and Characterization of a Highly Stable Extracellular Protease from an Extreme Halophilic Isolate Salicola marasensis

Authors

  • Amene Samaei-Nouroozi Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, Tehran, Iran.
  • Mahsa Moshfegh Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, Tehran, Iran.
  • Mohammad Ali Faramarzi Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, Tehran, Iran.
  • Mohammad Reza Khoshayand Department of Drug and Food Control, Faculty of Pharmacy and Pharmaceuticals Quality Assurance Research Center, Tehran University of Medical Sciences, Tehran, Iran.
  • Mohsen Amin Department of Drug and Food Control, Faculty of Pharmacy and Pharmaceuticals Quality Assurance Research Center, Tehran University of Medical Sciences, Tehran, Iran.
  • Nika Khoshnevis Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, Tehran, Iran.
  • Shahla Rezaei Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, Tehran, Iran.
Abstract:

Owing to their superior catalytic activity in the extreme conditions, extremozymes have found the potential biotechnological applications for industrial purposes. A robust extracellular protease activity was detected in the culture broth of Salicola marasensis, an extreme halophilic bacterium, after a 48 h-incubation. The effect of different media ingredients in a liquid state fermentation was followed with the aim of improving the enzyme production yield. Fractional factorial and Box-Behnken designs were applied to get a 3.4 fold (from 6.0 to 20.3 U mL−1) improvement of protease production. The distinguishing features of this enzyme were stability at a wide range of pH (5.0–11.0) and temperature (25–60 °C), significant compatibility towards organic solvents, metal ions, chemicals, and surfactants, and hydrolysis of a variety of substrates. The properties of this enzyme can be of tremendous help in terms of the halophilic proteolytic extract’s industrial applications.

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Journal title

volume 17  issue 4

pages  1392- 1412

publication date 2018-10-01

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