Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8405903 | Biocatalysis and Agricultural Biotechnology | 2018 | 29 Pages |
Abstract
Halophilic proteases are extremely useful in harsh environments during industrial manufacturing processes. Production of the enzymes by halophiles has been hampered with their slow growth and complicated purification processes. Here, we developed a rapid method for extremozyme production by recombinant Bacillus subtilis. HProPRW1, a halophilic protease from an extreme haloarchaeon Halobacterium salinarum PRW1, was expressed from a salt-inducible expression system in B. subtilis. Three different signal peptides were evaluated for HProPRW1 secretion, revealing an efficient function of the HProPRW1 native signal peptide in B. subtilis. At optimal conditions, HProPRW1 could be produced within 22â¯h by recombinant B. subtilis instead of 96â¯h by wild type. The recombinant enzyme functions most optimally at 60â¯Â°C, pH 9% and 12% NaCl. The crude enzyme was stable for at least 1 month at 4â¯Â°C. This new protocol can be applied for production of other high-value halophilic enzymes.
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Authors
Ruangurai Promchai, Auttaporn Boonchalearn, Wonnop Visessanguan, Plearnpis Luxananil,