Novel insight into the formation and inhibition mechanism of dipeptidyl peptidase-IV inhibitory peptides from fermented mandarin fish (Chouguiyu)

文献类型： 外文期刊

第一作者： Yang, Daqiao

作者： Yang, Daqiao;Li, Chunsheng;Li, Laihao;Yang, Xianqing;Chen, Shengjun;Wu, Yanyan;Feng, Yang;Yang, Daqiao;Li, Chunsheng;Li, Laihao;Yang, Xianqing;Chen, Shengjun;Wu, Yanyan;Feng, Yang;Yang, Daqiao;Li, Chunsheng;Li, Laihao;Yang, Xianqing;Chen, Shengjun;Wu, Yanyan;Feng, Yang

作者机构：

关键词： Chouguiyu; DPP-IV inhibitory peptide; Microorganism; Protease; Correlation network

期刊名称：FOOD SCIENCE AND HUMAN WELLNESS （ 影响因子：7.0； 五年影响因子：8.3 ）

ISSN：

年卷期： 2023 年 12 卷 6 期

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收录情况： SCI

摘要： Fermented foods are a potential source to produce novel dipeptidyl peptidase-IV inhibitory peptides (D4IPs). In this study, the fermented mandarin fish (Chouguiyu) was used to screen D4IPs and their formation mechanism was studied by metagenomics and peptidomics. A total of 400 D4IPs with DPP-IV inhibition structure and high hydrophobicity were identified. The correlation network map showed that Lactococcus, Bacillus, Lysobacter, Pelagivirga, Kocuria, Escherichia, Streptococcus, and Peptostreptococcus were significantly correlated with the most D4IPs. Four stable D4IPs, including KAGARALTDAETAT, GEKVDFDDIQK, VVDADEMYLKGK, and GQKDSYVGDEAQ were respectively from the precursor proteins parvalbumin, troponin, myosin, and actin, and were mainly formed by the hydrolysis of subtilisin (EC 3.4.21.62), aspartic proteinase (EC 3.4.23.1), thermolysin (EC 3.4.24.27), oligopeptidase B (EC 3.4.21.83), and proteinase P1 (EC 3.4.21.96) from Bacillus, Kocuria, Lysobacter, Lactococcus, and Peptostreptococcus. The inhibition mainly resulted from the hydrogen bond and salt bridge between D4IPs and DPP-IV enzyme. This study provides important information on the proteases and related microbial strains to directionally prepare D4IPs in Chouguiyu. (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/).

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