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• W3217582246 endingPage "184" @default.
• W3217582246 startingPage "174" @default.
• W3217582246 abstract "A moderately halotolerant serine protease was previously isolated from Bacillus subtilis from salted, fermented food. Eight mutation sites on the protein surface were selected for protein engineering based on sequence and structural comparisons with moderately halotolerant proteases and homologous non-halotolerant proteases. The newly constructed multiple mutants with substituted Asp and Arg residues were compared with the recombinant wild type (rApr) and the previously constructed mAla-8 substituted with Ala to analyze the contribution of protein surface charge to the salt adaptation of the protease. The three mutants showed >1.2-fold greater halotolerance than rApr. In addition, the mutants showed a broader range of pH stability than rApr, retaining >80% of their maximum activity in the pH range 5.0-11. The mutants also retained >75% of their activity after incubation for 1 h at pH 8.0 and 55°C or at pH 11.5 and 25°C. The Asp and Arg residues exchanged by multiple substitution probably played a role in increasing protein surface hydration and solubility in high salt conditions. This study illustrated that increasing a high proportion of the negative or positive charge on the surface of the Bacillus serine protease stably improved the protein's salt adaptation." @default.
• W3217582246 created "2021-12-06" @default.
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• W3217582246 date "2021-11-22" @default.
• W3217582246 modified "2023-09-30" @default.
• W3217582246 title "Improvement of the halotolerance of a <i>Bacillus</i> serine protease by protein surface engineering" @default.
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• W3217582246 doi "https://doi.org/10.1002/jobm.202100335" @default.
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