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Research Article | Open Access

Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacterium

Weijun Lenga, Xiaoyun Wua, Xianghui Qia, Hongying Liub, Li Yuana( ), Ruichang Gaoa( )
School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China
Ocean College of Hebei Agriculture University, Qinhuangdao 066000, China
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Abstract

In this study, a gene encoding serine protease (PmSpr288) from cold-adapted bacterium, namely Planococcus maritimus XJ11, was cloned and overexpressed in Escherichia coli BL21 (DE3). Bioinformatics analysis revealed that PmSpr288 belongs to serine protease S8 superfamily with a classical catalytic triad comprised by the Asp49, His86 and Ser251. Moreover, PmSpr288 was found to be active over broad alkaline pH and low-moderate temperature, and exhibited wide range of protein substrate specificity. In addition, PmSpr288 was able to hydrolyze the meat proteins actin and myosin, and molecular docking results suggested that the crucial interaction between PmSpr288 and actin/myosin complexes was mainly occupied by hydrogen bonds. The muscle protein hydrolysates of silver carp prepared by PmSpr288 was shown to have antioxidant activity via DPPH radical scavenging assay, which presented an IC50 valve of 1.309 mg/mL. In conclusion, these characteristics imply that PmSpr288 has potential biotechnological application prospect for the production of bioactive peptides.

Keywords

Molecular dockingProteaseBioactive peptidesSilver carpProtein hydrolysates

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Food Science and Human Wellness
Volume 12 Issue 5,
September 2023
Pages 1751-1761
DOI: 10.1016/j.fshw.2023.02.025
Cite this article:
Leng W, Wu X, Qi X, et al. Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacterium. Food Science and Human Wellness, 2023, 12(5): 1751-1761. https://doi.org/10.1016/j.fshw.2023.02.025

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Received: 29 September 2021
Revised: 01 May 2022
Accepted: 21 May 2022
Published: 21 March 2023
© 2023 Beijing Academy of Food Sciences.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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