Formation and inhibition mechanism of novel angiotensin I converting enzyme inhibitory peptides from Chouguiyu
Angiotensin I converting enzyme (ACE) inhibitory peptides from fermented foods exhibit great potential to alleviate hypertension. In this study, the peptide extract from Chouguiyu exhibited a good inhibition effect on ACE, and the inhibition rate was significantly enhanced after fermentation for 8 d...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-07-01
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| Series: | Frontiers in Nutrition |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fnut.2022.920945/full |
| _version_ | 1811288985705644032 |
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| author | Daqiao Yang Daqiao Yang Daqiao Yang Laihao Li Laihao Li Laihao Li Chunsheng Li Chunsheng Li Chunsheng Li Shengjun Chen Shengjun Chen Shengjun Chen Jianchao Deng Jianchao Deng Jianchao Deng Shaoling Yang Shaoling Yang Shaoling Yang |
| author_facet | Daqiao Yang Daqiao Yang Daqiao Yang Laihao Li Laihao Li Laihao Li Chunsheng Li Chunsheng Li Chunsheng Li Shengjun Chen Shengjun Chen Shengjun Chen Jianchao Deng Jianchao Deng Jianchao Deng Shaoling Yang Shaoling Yang Shaoling Yang |
| author_sort | Daqiao Yang |
| collection | DOAJ |
| description | Angiotensin I converting enzyme (ACE) inhibitory peptides from fermented foods exhibit great potential to alleviate hypertension. In this study, the peptide extract from Chouguiyu exhibited a good inhibition effect on ACE, and the inhibition rate was significantly enhanced after fermentation for 8 days. The ACE inhibitory peptides were further identified, followed by their inhibition and formation mechanisms using microbiome technology and molecular docking. A total of 356 ACE inhibitory peptides were predicted using in silico, and most ACE inhibitory peptides increased after fermentation. These peptides could be hydrolyzed from 94 kinds of precursor proteins, mainly including muscle-type creatine kinase, nebulin, and troponin I. P1 (VEIINARA), P2 (FAVMVKG), P4 (EITWSDDKK), P7 (DFDDIQK), P8 (IGDDPKF), P9 (INDDPKIL), and P10 (GVDNPGHPFI) were selected as the core ACE inhibitory peptides according to their abundance and docking energy. The salt bridge and conventional hydrogen bond connecting unsaturated oxygen atoms in the peptides contributed most to the ACE inhibition. The cleavage proteases from the microbial genera in Chouguiyu for preparing these 7 core ACE inhibitory peptides were further analyzed by hydrolysis prediction and Pearson's correlation. The correlation network showed that P7, P8, and P9 were mainly produced by the proteases from LAB including Lactococcus, Enterococcus, Vagococcus, Peptostreptococcus, and Streptococcus, while P1, P2, P4, and P10 were mainly Produced by Aeromonas, Bacillus, Escherichia, and Psychrobacter. This study is helpful in isolating the proteases and microbial strains to directionally produce the responding ACE inhibitory peptides. |
| first_indexed | 2024-04-13T03:46:51Z |
| format | Article |
| id | doaj.art-5f22ea0b157f4233ab2aba9167ab8383 |
| institution | Directory Open Access Journal |
| issn | 2296-861X |
| language | English |
| last_indexed | 2024-04-13T03:46:51Z |
| publishDate | 2022-07-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Nutrition |
| spelling | doaj.art-5f22ea0b157f4233ab2aba9167ab83832022-12-22T03:03:59ZengFrontiers Media S.A.Frontiers in Nutrition2296-861X2022-07-01910.3389/fnut.2022.920945920945Formation and inhibition mechanism of novel angiotensin I converting enzyme inhibitory peptides from ChouguiyuDaqiao Yang0Daqiao Yang1Daqiao Yang2Laihao Li3Laihao Li4Laihao Li5Chunsheng Li6Chunsheng Li7Chunsheng Li8Shengjun Chen9Shengjun Chen10Shengjun Chen11Jianchao Deng12Jianchao Deng13Jianchao Deng14Shaoling Yang15Shaoling Yang16Shaoling Yang17Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, ChinaCo-Innovation Center of Jiangsu Marine Bio-industry Technology, Jiangsu Ocean University, Lianyungang, ChinaCollege of Food Science and Engineering, Ocean University of China, Qingdao, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, ChinaCo-Innovation Center of Jiangsu Marine Bio-industry Technology, Jiangsu Ocean University, Lianyungang, ChinaCollaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, ChinaCo-Innovation Center of Jiangsu Marine Bio-industry Technology, Jiangsu Ocean University, Lianyungang, ChinaCollaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, ChinaCo-Innovation Center of Jiangsu Marine Bio-industry Technology, Jiangsu Ocean University, Lianyungang, ChinaCollaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, ChinaCo-Innovation Center of Jiangsu Marine Bio-industry Technology, Jiangsu Ocean University, Lianyungang, ChinaCollaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, ChinaCo-Innovation Center of Jiangsu Marine Bio-industry Technology, Jiangsu Ocean University, Lianyungang, ChinaCollaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian, ChinaAngiotensin I converting enzyme (ACE) inhibitory peptides from fermented foods exhibit great potential to alleviate hypertension. In this study, the peptide extract from Chouguiyu exhibited a good inhibition effect on ACE, and the inhibition rate was significantly enhanced after fermentation for 8 days. The ACE inhibitory peptides were further identified, followed by their inhibition and formation mechanisms using microbiome technology and molecular docking. A total of 356 ACE inhibitory peptides were predicted using in silico, and most ACE inhibitory peptides increased after fermentation. These peptides could be hydrolyzed from 94 kinds of precursor proteins, mainly including muscle-type creatine kinase, nebulin, and troponin I. P1 (VEIINARA), P2 (FAVMVKG), P4 (EITWSDDKK), P7 (DFDDIQK), P8 (IGDDPKF), P9 (INDDPKIL), and P10 (GVDNPGHPFI) were selected as the core ACE inhibitory peptides according to their abundance and docking energy. The salt bridge and conventional hydrogen bond connecting unsaturated oxygen atoms in the peptides contributed most to the ACE inhibition. The cleavage proteases from the microbial genera in Chouguiyu for preparing these 7 core ACE inhibitory peptides were further analyzed by hydrolysis prediction and Pearson's correlation. The correlation network showed that P7, P8, and P9 were mainly produced by the proteases from LAB including Lactococcus, Enterococcus, Vagococcus, Peptostreptococcus, and Streptococcus, while P1, P2, P4, and P10 were mainly Produced by Aeromonas, Bacillus, Escherichia, and Psychrobacter. This study is helpful in isolating the proteases and microbial strains to directionally produce the responding ACE inhibitory peptides.https://www.frontiersin.org/articles/10.3389/fnut.2022.920945/fullChouguiyuACE inhibitory peptidemetagenomicspeptidomicsmolecular dockingcorrelation network |
| spellingShingle | Daqiao Yang Daqiao Yang Daqiao Yang Laihao Li Laihao Li Laihao Li Chunsheng Li Chunsheng Li Chunsheng Li Shengjun Chen Shengjun Chen Shengjun Chen Jianchao Deng Jianchao Deng Jianchao Deng Shaoling Yang Shaoling Yang Shaoling Yang Formation and inhibition mechanism of novel angiotensin I converting enzyme inhibitory peptides from Chouguiyu Frontiers in Nutrition Chouguiyu ACE inhibitory peptide metagenomics peptidomics molecular docking correlation network |
| title | Formation and inhibition mechanism of novel angiotensin I converting enzyme inhibitory peptides from Chouguiyu |
| title_full | Formation and inhibition mechanism of novel angiotensin I converting enzyme inhibitory peptides from Chouguiyu |
| title_fullStr | Formation and inhibition mechanism of novel angiotensin I converting enzyme inhibitory peptides from Chouguiyu |
| title_full_unstemmed | Formation and inhibition mechanism of novel angiotensin I converting enzyme inhibitory peptides from Chouguiyu |
| title_short | Formation and inhibition mechanism of novel angiotensin I converting enzyme inhibitory peptides from Chouguiyu |
| title_sort | formation and inhibition mechanism of novel angiotensin i converting enzyme inhibitory peptides from chouguiyu |
| topic | Chouguiyu ACE inhibitory peptide metagenomics peptidomics molecular docking correlation network |
| url | https://www.frontiersin.org/articles/10.3389/fnut.2022.920945/full |
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