Salt dependent resistance against chemical denaturation of alkaline protease from a newly isolated haloalkaliphilic Bacillus sp

Bioresource Technology
M S DodiaS P Singh

Abstract

Only few enzymes from haloalkaliphiles are biochemically characterized for their kinetic behaviour and stability. In view of this realization, an alkaline protease from Bacillus sp. AH-6, displaying salt-dependent resistance against chemical denaturation by Urea and Guanidium hydrochloride was investigated for denaturation and in vitro protein folding. The crude enzyme was highly resistant against urea (8 M) denaturation up to 72 h; however, on purification, it turned sensitive and got denatured within 2 h. Interestingly, the purified enzyme regained the resistance in the presence of NaCl. Effective refolding of the purified enzyme was achieved with glycerol; however, other approaches such as lower protein concentrations, rapid dilution and slow removal of the denaturant did not further add to refolding. The results are important from the viewpoint that only few enzymes from haloalkaliphilic bacteria are characterized. Since the resistance against chemical denaturation is a rare phenomenon, the findings would enrich the knowledge on protein stability and denaturation. Besides, such biocatalysts would definitely have novel applications under harsh chemical environments.

References

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Citations

Jul 24, 2013·Extremophiles : Life Under Extreme Conditions·Vikash Kumar, T Satyanarayana
Nov 6, 2014·Canadian Journal of Microbiology·Baisuo ZhaoShulin Chen
Nov 28, 2012·International Journal of Biological Macromolecules·Megha K Purohit, Satya P Singh
Jun 10, 2011·Journal of Basic Microbiology·Anil Kumar Singh, Hari S Chhatpar
Feb 9, 2013·International Journal of Biological Macromolecules·S D Gohel, S P Singh
May 2, 2014·Frontiers in Microbiology·Rajeshwari Sinha, Sunil K Khare
Jan 31, 2017·The Journal of Physical Chemistry. B·Nicola SteinkeSylvia E McLain
Apr 24, 2020·World Journal of Microbiology & Biotechnology·Ganapathi UmaThavasimuthu Citarasu

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