Isolation, purification and the anti-hypertensive effect of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from Ruditapes philippinarum fermented with Bacillus natto. Issue 10 (12th September 2018)
- Record Type:
- Journal Article
- Title:
- Isolation, purification and the anti-hypertensive effect of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from Ruditapes philippinarum fermented with Bacillus natto. Issue 10 (12th September 2018)
- Main Title:
- Isolation, purification and the anti-hypertensive effect of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from Ruditapes philippinarum fermented with Bacillus natto
- Authors:
- Chen, Yingyun
Gao, Xiang
Wei, Yuxi
Liu, Qi
Jiang, Yuhong
Zhao, Ling
Ulaah, Sadeeq - Abstract:
- Abstract : A novel ACE inhibitory peptide (Val-Ile-Ser-Asp-Glu-Asp-Gly-Val-Thr-His) with a high anti-hypertensive effect isolated from Ruditapes philippinarum fermented with Bacillus natto . Abstract : Hypertension is known as an important factor in cardiovascular disease. An angiotensin-I-converting enzyme (ACE) inhibitor is one of the synthetic drugs that is widely used to control hypertension. Here, we have prepared and investigated the ACE inhibitory peptide from Ruditapes philippinarum fermented with Bacillus natto . The fermented product obtained under optimized fermentation conditions exhibited ACE inhibitory activity. The ACE inhibitory peptides were purified by ultrafiltration, gel filtration chromatography and RP-HPLC, sequentially. A novel peptide with high ACE inhibitory activity (IC50 of 8.16 μM) was isolated and the amino acid sequence was identified to be Val-Ile-Ser-Asp-Glu-Asp-Gly-Val-Thr-His (VISDEDGVTH) by LC-MS/MS. The Lineweaver–Burk plots suggested that VISDEDGVTH acts as a competitive inhibitor against ACE. Our in vitro study indicated the stability of VISDEDGVTH against gastrointestinal proteases. An in vivo study in rats proved the significant anti-hypertension effect of the peptide. Furthermore, the cellular mechanism of VISDEDGVTH moderating hypertension was investigated. We found that VISDEDGVTH enhanced the release of NO, inhibited the secretion of EF-1, and scavenged ROS in human vascular endothelial cells. Our study suggests that VISDEDGVTHAbstract : A novel ACE inhibitory peptide (Val-Ile-Ser-Asp-Glu-Asp-Gly-Val-Thr-His) with a high anti-hypertensive effect isolated from Ruditapes philippinarum fermented with Bacillus natto . Abstract : Hypertension is known as an important factor in cardiovascular disease. An angiotensin-I-converting enzyme (ACE) inhibitor is one of the synthetic drugs that is widely used to control hypertension. Here, we have prepared and investigated the ACE inhibitory peptide from Ruditapes philippinarum fermented with Bacillus natto . The fermented product obtained under optimized fermentation conditions exhibited ACE inhibitory activity. The ACE inhibitory peptides were purified by ultrafiltration, gel filtration chromatography and RP-HPLC, sequentially. A novel peptide with high ACE inhibitory activity (IC50 of 8.16 μM) was isolated and the amino acid sequence was identified to be Val-Ile-Ser-Asp-Glu-Asp-Gly-Val-Thr-His (VISDEDGVTH) by LC-MS/MS. The Lineweaver–Burk plots suggested that VISDEDGVTH acts as a competitive inhibitor against ACE. Our in vitro study indicated the stability of VISDEDGVTH against gastrointestinal proteases. An in vivo study in rats proved the significant anti-hypertension effect of the peptide. Furthermore, the cellular mechanism of VISDEDGVTH moderating hypertension was investigated. We found that VISDEDGVTH enhanced the release of NO, inhibited the secretion of EF-1, and scavenged ROS in human vascular endothelial cells. Our study suggests that VISDEDGVTH serves as an anti-hypertension and anti-inflammatory drug and as a beneficial ingredient in functional foods and pharmaceuticals. … (more)
- Is Part Of:
- Food & function. Volume 9:Issue 10(2018)
- Journal:
- Food & function
- Issue:
- Volume 9:Issue 10(2018)
- Issue Display:
- Volume 9, Issue 10 (2018)
- Year:
- 2018
- Volume:
- 9
- Issue:
- 10
- Issue Sort Value:
- 2018-0009-0010-0000
- Page Start:
- 5230
- Page End:
- 5237
- Publication Date:
- 2018-09-12
- Subjects:
- Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
Nutrition -- Periodicals
664.07 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/FO ↗
http://pubs.rsc.org/en/journals/journal/fo ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c8fo01146j ↗
- Languages:
- English
- ISSNs:
- 2042-6496
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.038457
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 8001.xml