Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
Food Chem ; 221: 464-472, 2017 Apr 15.
Article in English | MEDLINE | ID: mdl-27979228

ABSTRACT

The objective was to identify peptides with dual antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities released from lentil proteins by Savinase®. The influence of gastrointestinal digestion on peptide bioactivity was also assayed. Fragments from vicilin, convicilin and legumin were the most abundant peptides identified. Peptides LLSGTQNQPSFLSGF, NSLTLPILRYL, TLEPNSVFLPVLLH showed the highest antioxidant (0.013-1.432µmol Trolox eq./µmol peptide) and ACE inhibitory activities (IC50=44-120µM). Gastrointestinal digestion of peptides improved their dual activity (10-14µmol Trolox eq./µmol peptide; IC50=11-21µM). In general, C-terminal heptapeptide was crucial for their dual activity. ACE inhibition relies on the formation of hydrogen bonds between C-terminal residues of lentil peptides and residues of the ACE catalytic site. The present study helps clarifying the relationship between structure and dual antioxidant/antihypertensive activity of lentil peptides opening new opportunities to food industry such as the application of lentil protein hydrolysates as ingredients for development of functional foods.


Subject(s)
Angiotensin-Converting Enzyme Inhibitors/metabolism , Antioxidants/metabolism , Lens Plant/metabolism , Antihypertensive Agents , Digestion , Molecular Docking Simulation , Peptides/chemistry , Peptidyl-Dipeptidase A/metabolism , Protein Hydrolysates/chemistry
SELECTION OF CITATIONS
SEARCH DETAIL
...