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Identification, functional gastrointestinal stability and molecular docking studies of lentil peptides with dual antioxidant and angiotensin I converting enzyme inhibitory activities
- García-Mora, Patricia, Martín-Martínez, Mercedes, Angeles Bonache, María, González-Múniz, Rosario, Peñas, Elena, Frias, Juana, Martinez-Villaluenga, Cristina
- Food chemistry 2017 v.221 pp. 464-472
- active sites, antihypertensive effect, antioxidants, convicilin, digestion, enzyme inhibition, food industry, functional foods, gastrointestinal system, hydrogen bonding, ingredients, legumin, lentils, molecular models, peptides, peptidyl-dipeptidase A, protein hydrolysates, vicilin
- 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.