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Microbiol Res. 2020 Mar 18;236:126468. doi: 10.1016/j.micres.2020.126468. [Epub ahead of print]

Identification and characterization of the gene encoding an extracellular protease from haloarchaeon Halococcus salifodinae.

Author information

1
School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Jingkou District, Zhenjiang 212013, Jiangsu, People's Republic of China.
2
School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Jingkou District, Zhenjiang 212013, Jiangsu, People's Republic of China. Electronic address: cuihenglin@ujs.edu.cn.

Abstract

Extracellular proteases from haloarchaea (halolysins) can resist high salt conditions. In this study, the gene encoding a halolysin from Halococcus salifodinae was identified. The hlyA gene encoded an active halolysin with the classical Asp-His-Ser catalytic triad of serine proteases. Site-directed mutagenesis showed that the three cysteine residues in the catalytic domain were important for the extracellular proteolytic activity and displayed an additive effect on the activity. Truncation mutants of the C-terminal extension (CTE) domain displayed very low or almost no extracellular protease activity towards milk and small peptide substrates, indicating its importance for the function of HlyA. CTE can be functionally interchangeable among halolysins. Additionally, the HlyA expressing strain as a starter culture for fish sauce fermentation significantly increased the peptide release and total free amino acid content in fish sauce. This study enriches our knowledge of the key amino acid residues and domains of halolysins, and provides an opportunity for applications of halolysins in fish sauce fermentation.

KEYWORDS:

Extracellular protease; Fish sauce; Gene; Haloarchaeon; Halococcus salifodinae; Protease activity

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