Identification, functional gastrointestinal stability and molecular docking studies of lentil peptides with dual antioxidant and angiotensin I converting enzyme inhibitory activities

•Lentil peptides showing potential antihypertensive activity were identified.•Bioactive fragments derived from lentil vicilin, convicilin and legumin.•Gastrointestinal digestion of peptides improved markedly their bioactivity.•C-terminal heptapeptide was crucial for antioxidant and ACE inhibitory ac...

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Bibliographic Details
Published in:Food chemistry 2017-04, Vol.221, p.464-472
Main Authors: García-Mora, Patricia, Martín-Martínez, Mercedes, Angeles Bonache, María, González-Múniz, Rosario, Peñas, Elena, Frias, Juana, Martinez-Villaluenga, Cristina
Format: Article
Language:English
Subjects:
ACE inhibitory activity
Angiotensin-Converting Enzyme Inhibitors - metabolism
Antihypertensive Agents
Antioxidant activity
Antioxidants - metabolism
Digestion
Gastrointestinal digestion
Lens Plant - metabolism
Lentil peptides
Molecular docking
Molecular Docking Simulation
Peptides - chemistry
Peptidyl-Dipeptidase A - metabolism
Protein Hydrolysates - chemistry
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Summary:•Lentil peptides showing potential antihypertensive activity were identified.•Bioactive fragments derived from lentil vicilin, convicilin and legumin.•Gastrointestinal digestion of peptides improved markedly their bioactivity.•C-terminal heptapeptide was crucial for antioxidant and ACE inhibitory activities.•ACE inhibition relies on hydrogen bonds involving residues of the catalytic site. 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.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2016.10.087