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Biochemical Characterization of a Novel Alkaline and Detergent Stable Protease from Aeromonas veronii OB3

  • Manni, Laila (Laboratory of Microbial Biotechnology, Faculty of Sciences and Techniques, Sidi Mohammed Ben Abdellah University) ;
  • Misbah, Asmae (Laboratory of Microbial Biotechnology, Faculty of Sciences and Techniques, Sidi Mohammed Ben Abdellah University) ;
  • Zouine, Nouhaila (Laboratory of Microbial Biotechnology, Faculty of Sciences and Techniques, Sidi Mohammed Ben Abdellah University) ;
  • Ananou, Samir (Laboratory of Microbial Biotechnology, Faculty of Sciences and Techniques, Sidi Mohammed Ben Abdellah University)
  • Received : 2019.12.23
  • Accepted : 2020.06.08
  • Published : 2020.09.28

Abstract

An organic solvent- and bleach-stable protease-producing strain was isolated from a polluted river water sample and identified as Aeromonas veronii OB3 on the basis of biochemical properties (API 20E) and 16S rRNA sequence analysis. The strain was found to hyper-produce alkaline protease when cultivated on fish waste powder-based medium (HVSP, 4080 U/ml). The biochemical properties and compatibility of OB3 with several detergents and additives were studied. Maximum activity was observed at pH 9.0 and 60℃. The crude protease displayed outstanding stability to the investigated surfactants and oxidants, such as Tween 80, Triton X-100, and H2O2, and almost 36% residual activity when incubated with 1% SDS. Remarkably, the enzyme demonstrated considerable compatibility with commercial detergents, retaining more than 100% of its activity with Ariel and Tide (1 h, 40℃). Moreover, washing performance of Tide significantly improved by the supplementation of small amounts of OB3 crude protease. These properties suggest the potential use of this alkaline protease as a bio-additive in the detergent industry and other biotechnological processes such as peptide synthesis.

Keywords

References

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