4.7 Article

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

期刊

FOOD SCIENCE AND HUMAN WELLNESS
卷 12, 期 5, 页码 1751-1761

出版社

KEAI PUBLISHING LTD
DOI: 10.1016/j.fshw.2023.02.025

关键词

Protease; Silver carp; Protein hydrolysates; Molecular docking; Bioactive peptides

向作者/读者索取更多资源

In this study, the gene encoding serine protease PmSpr288 from cold-adapted bacterium Planococcus maritimus XJ11 was cloned and overexpressed in Escherichia coli BL21 (DE3). Bioinformatics analysis revealed its membership in the serine protease S8 superfamily and the presence of a classical catalytic triad. PmSpr288 exhibited broad alkaline pH and low-moderate temperature activity, wide protein substrate specificity, and the ability to hydrolyze meat proteins. The muscle protein hydrolysates produced by PmSpr288 showed antioxidant activity, suggesting its potential biotechnological applications.
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.(c) 2023 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据