Whole-genome sequencing of a protease-producing strain isolated from fermented golden pompano and molecular docking of the protease to fish proteins
文献类型： 外文期刊
作者： Wang, Huifang 1 ; Qiu, Yingjie 1 ; Chen, Shengjun 1 ; Zhao, Yongqiang 1 ; Wu, Yanyan 1 ; Wang, Yueqi 1 ;
作者机构： 1.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Natl R&D Ctr Aquat Prod Proc, Key Lab Aquat Prod Proc,Minist Agr & Rural Affairs, Guangzhou 510300, Peoples R China
2.Beibu Gulf Univ, Coll Food Engn, Guangxi Coll & Univ Key Lab Dev & High value Utili, Qinzhou 535000, Guangxi, Peoples R China
3.Jiangsu Ocean Univ, Coinnovat Ctr Jiangsu Marine Bioind Technol, Lianyungang 222005, Peoples R China
4.Sanya Trop Fisheries Res Inst, Key Lab Efficient Utilizat & Proc Marine Fishery R, Sanya 572018, Peoples R China
关键词： Bacillus tropicus; Fermented golden pompano; Genome sequencing; Molecular docking; Protease
期刊名称：FOOD BIOSCIENCE （ 影响因子：5.2； 五年影响因子：5.4 ）
ISSN： 2212-4292
年卷期： 2024 年 57 卷
页码：
收录情况： SCI
摘要： In fermented fish products, microorganisms catalyze protein degradation by secreting proteases, thereby altering the nutritional values of foods. In this study, we isolated a high proteinase-producing strain from fermented golden pompano (Trachinotus ovatus), and from the 16S rRNA, we identified the strain as Bacillus tropicus, which we named Bacillus tropicus MX-8. This strain could form a distinct proteolytic circle around the colony when plated on agar containing 3% skimmed milk powder and could grow under 0-5% salinity. Its protease significantly degraded fish proteins. Genome sequencing analysis revealed that the genome of B. tropicus MX-8 comprised one circular chromosome and three circular plasmids. A total of 27 genes encoding proteases, including a neutral protease and three serine proteases, were identified in the non-redundant protein database. Homology modeling showed that serine protease 2 had the best model quality and the highest sequence match. Molecular docking experiments revealed the presence of several amino acid active sites on serine protease 2. These active sites mainly rely on hydrogen bonding to interact with actin heavy chains and myosin to form complexes, which can promote further protein degradation. This study demonstrated that B. tropicus MX-8 has the potential to ferment fish, providing a theoretical basis for the production of rapidly fermented fish products.
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