Investigation on antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activity of Bambara bean protein hydrolysates
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
Protein isolate was hydrolysed by Alcalase, thermolysin and trypsin. BBPH produced by Alcalase showed highest angiotensin-converting enzyme (ACE) inhibitory properties (IC50:52 mu g/mL). Hydrolysates produced by Alcalase and thermolysin exhibited similar dipeptidyl peptidase-IV (DPP-IV) inhibitory activity (IC50:1.73 mg/mL), while low inhibitory activity was observed for hydrolysate produced by trypsin. BBPH also showed protective effect against oxidative stress with significant 2,2-diphenyl-1-picrylhydrazyl radical scavenging and ferrous chelating activity. Bioactive peptides of BBPH produced by thermolysin showed better resistance to simulated gastrointestinal digestion (SGID), while the DPP-IV and ACE inhibitory properties were significantly reduced. Molecular weight distribution showed significant reduction in peptides of the molecular weight range 200-400 Da in BBPH produced by Alcalase, after SGID. LC-ESI-TOF-MS and in silico analysis showed the presence of potential peptides with both ACE and DPP-IV inhibitory properties in BBPH produced by thermolysin.
Details
| Original language | English |
|---|---|
| Pages (from-to) | 162-169 |
| Number of pages | 8 |
| Journal | Food Chemistry |
| Volume | 250 |
| Publication status | Published - 1 Jun 2018 |
| Peer-reviewed | Yes |
External IDs
| Scopus | 85044356667 |
|---|---|
| WOS | 000424510200022 |
Keywords
Keywords
- Bambara bean protein hydrolysates, Angiotensin converting enzyme inhibitory properties, Dipeptidyl peptidase-IV inhibitory properties, Antioxidant properties, Simulated gastrointestinal digestion, FUNCTIONAL-PROPERTIES, IN-VITRO, BIOACTIVE PEPTIDES, GRAIN LEGUMES, FOOD, DIGESTION, IDENTIFICATION, CHICKPEA, RELEASE, ACID