Two novel peptides with angiotensin I converting enzyme inhibitory and antioxidative activities from Scorpaena notata muscle protein hydrolysate. (16th June 2016)
- Record Type:
- Journal Article
- Title:
- Two novel peptides with angiotensin I converting enzyme inhibitory and antioxidative activities from Scorpaena notata muscle protein hydrolysate. (16th June 2016)
- Main Title:
- Two novel peptides with angiotensin I converting enzyme inhibitory and antioxidative activities from Scorpaena notata muscle protein hydrolysate
- Authors:
- Aissaoui, Neyssene
Abidi, Ferid
Hardouin, Julie
Abdelkafi, Zaineb
Marrakchi, Naziha
Jouenne, Thierry
Marzouki, M. Nejib - Abstract:
- Abstract: Fish protein hydrolysate was prepared from muscle of small red scorpionfish ( Scorpaena notata ) by treatment with a protease from the fungus Penicillium digitatum . Protein hydrolysate was found to strongly inhibit the angiotensin I converting enzyme and exhibited high antioxidative activity through 1, 1‐diphenyl‐2‐picrylhydrazyl free radical scavenging assay. After ultrafiltration, peptides were isolated by a two‐step procedure: size exclusion chromatography on a Toyopearl HW‐40 followed by reversed‐phase high‐performance liquid chromatography with a high purification yield of 2.5 mg of peptide per gram of initial protein. Two major peptides were then identified by nanoscale liquid chromatography coupled to tandem mass spectrometry (nano‐LC‐MS/MS), corresponding to the following sequences: Leu‐Val‐Thr‐Gly‐Asp‐Asp‐Lys‐Thr‐Asn‐Leu‐Lys (1, 204.665 Da) and Asp‐Thr‐Gly‐Ser‐Asp‐Lys‐Lys‐Gln‐Leu (992.511 Da). These peptides, mainly composed of hydrophilic amino acids, showed high antioxidative and angiotensin I converting enzyme inhibitory activities. These data suggest that the two novel peptides isolated from the muscle hydrolysate of small red scorpionfish can be a beneficial ingredient for functional foods or pharmaceuticals against hypertension and oxidative stress.
- Is Part Of:
- Biotechnology and applied biochemistry. Volume 64:Number 2(2017)
- Journal:
- Biotechnology and applied biochemistry
- Issue:
- Volume 64:Number 2(2017)
- Issue Display:
- Volume 64, Issue 2 (2017)
- Year:
- 2017
- Volume:
- 64
- Issue:
- 2
- Issue Sort Value:
- 2017-0064-0002-0000
- Page Start:
- 201
- Page End:
- 210
- Publication Date:
- 2016-06-16
- Subjects:
- angiotensin I converting enzyme inhibitory activity -- antioxidant peptides -- hydrophilic amino acids -- protein hydrolysate -- purification and identification -- therapeutic compounds
Biotechnology -- Periodicals
Biochemical engineering -- Periodicals
Biochemistry -- Periodicals
Biochemistry -- Periodicals
Genetic Techniques -- Periodicals
Microbiological Techniques -- Periodicals
660.6 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1470-8744 ↗
http://www.babonline.org/ ↗
http://onlinelibrary.wiley.com/ ↗
http://bab.portlandpress.com/ ↗
http://bab.portlandpress.co.uk/ ↗ - DOI:
- 10.1002/bab.1478 ↗
- Languages:
- English
- ISSNs:
- 0885-4513
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2089.848000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 2523.xml