Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis
Food-originated angiotensin-I-converting enzyme (ACE)-inhibitory peptides to preserve hypertension are widely investigated over the past decade. Our research aims to discovery novel ACE-inhibitory peptides from bovine milk by couple of complex proteases (alcalase and protease). By means of response...
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2020-01-01
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| Series: | Artificial Cells, Nanomedicine, and Biotechnology |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/21691401.2019.1699824 |
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| author | Li Chen Wenfei Shangguan Chunju Bao Guowei Shu He Chen |
| author_facet | Li Chen Wenfei Shangguan Chunju Bao Guowei Shu He Chen |
| author_sort | Li Chen |
| collection | DOAJ |
| description | Food-originated angiotensin-I-converting enzyme (ACE)-inhibitory peptides to preserve hypertension are widely investigated over the past decade. Our research aims to discovery novel ACE-inhibitory peptides from bovine milk by couple of complex proteases (alcalase and protease). By means of response surface methodology with the conditions of pH 9.01, 61.81 °C and 6.5% ratio of enzyme to substrate, the hydrolysis model contributes to best-performing ACE-inhibitory activity of 85.02%. Through the further purification by consequent ultrafiltration, macroporous resin and gel chromatography, fraction G2-2 is eventually obtained with ACE-inhibitory activity as high as 92.7%. Two novel peptides of VLPVPQ and VAPFPE are identified by Q-Exactive LC–MS/MS. The molecular docking study further suggests that two novel peptides have good combinations of the S1 and S2 active site pockets and Zn(II) of ACE. Our study provides a fitted mathematical model to produce two novel milk-derived ACE-inhibitory peptides, potentially developing the functional foods, especially for hypertension therapy as initial treatment. |
| format | Article |
| id | doaj-art-1cdf8bf09f794460bd2f92c70e4a848d |
| institution | Kabale University |
| issn | 2169-1401 2169-141X |
| language | English |
| publishDate | 2020-01-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Artificial Cells, Nanomedicine, and Biotechnology |
| spelling | doaj-art-1cdf8bf09f794460bd2f92c70e4a848d2025-08-20T03:41:21ZengTaylor & Francis GroupArtificial Cells, Nanomedicine, and Biotechnology2169-14012169-141X2020-01-0148118018710.1080/21691401.2019.1699824Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysisLi Chen0Wenfei Shangguan1Chunju Bao2Guowei Shu3He Chen4College of Food Engineering and Nutritional Science, Shaanxi Normal University, Xi’an, PR ChinaSchool of Food and Biological Engineering, Shaanxi University of Science and Technology, Xi’an, PR ChinaSchool of Food and Biological Engineering, Shaanxi University of Science and Technology, Xi’an, PR ChinaSchool of Food and Biological Engineering, Shaanxi University of Science and Technology, Xi’an, PR ChinaSchool of Food and Biological Engineering, Shaanxi University of Science and Technology, Xi’an, PR ChinaFood-originated angiotensin-I-converting enzyme (ACE)-inhibitory peptides to preserve hypertension are widely investigated over the past decade. Our research aims to discovery novel ACE-inhibitory peptides from bovine milk by couple of complex proteases (alcalase and protease). By means of response surface methodology with the conditions of pH 9.01, 61.81 °C and 6.5% ratio of enzyme to substrate, the hydrolysis model contributes to best-performing ACE-inhibitory activity of 85.02%. Through the further purification by consequent ultrafiltration, macroporous resin and gel chromatography, fraction G2-2 is eventually obtained with ACE-inhibitory activity as high as 92.7%. Two novel peptides of VLPVPQ and VAPFPE are identified by Q-Exactive LC–MS/MS. The molecular docking study further suggests that two novel peptides have good combinations of the S1 and S2 active site pockets and Zn(II) of ACE. Our study provides a fitted mathematical model to produce two novel milk-derived ACE-inhibitory peptides, potentially developing the functional foods, especially for hypertension therapy as initial treatment.https://www.tandfonline.com/doi/10.1080/21691401.2019.1699824ACE-inhibitory peptidebovine milkcomplex proteasesmolecular docking |
| spellingShingle | Li Chen Wenfei Shangguan Chunju Bao Guowei Shu He Chen Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis Artificial Cells, Nanomedicine, and Biotechnology ACE-inhibitory peptide bovine milk complex proteases molecular docking |
| title | Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis |
| title_full | Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis |
| title_fullStr | Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis |
| title_full_unstemmed | Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis |
| title_short | Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis |
| title_sort | collaborative optimization and molecular docking exploration of novel ace inhibitory peptides from bovine milk by complex proteases hydrolysis |
| topic | ACE-inhibitory peptide bovine milk complex proteases molecular docking |
| url | https://www.tandfonline.com/doi/10.1080/21691401.2019.1699824 |
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