biostudies-literatureMartineau-Cote DPulse Science Research Cluster 3-Activity ASC-06 Activity 14A6432-6443https://www.ebi.ac.uk/biostudies/studies/S-EPMC10979453biostudies-literatureUnknown72(12)Faba bean flour, after <i>in vitro</i> gastrointestinal digestion, showed important antioxidant and angiotensin-converting enzyme (ACE) inhibitory activities. In the present study, 11 faba bean- derived peptides were synthesized to confirm their bioactivities and provide a deeper understanding of their mechanisms of action. The results revealed that 7 peptides were potent antioxidants, namely, NYDEGSEPR, TETWNPNHPEL, TETWNPNHPE, VIPTEPPH, VIPTEPPHA, VVIPTEPPHA, and VVIPTEPPH. Among them, TETWNPNHPEL had the highest activity in the ABTS (EC₅₀ = 0.5 ± 0.2 mM) and DPPH (EC₅₀ = 2.1 ± 0.1 mM) assays (<i>p</i> < 0.05), whereas TETWNPNHPE had the highest activity (<i>p</i> < 0.05) in the ORAC assay (2.84 ± 0.08 mM Trolox equivalent/mM). Synergistic and/or additive effects were found when selected peptides (TETWNPNHPEL, NYDEGSEPR, and VVIPTEPPHA) were combined. Four peptides were potent ACE inhibitors, where VVIPTEPPH (IC₅₀ = 43 ± 1 μM) and VVIPTEPPHA (IC₅₀ = 50 ± 5 μM) had the highest activity (<i>p</i> < 0.05), followed by VIPTEPPH (IC₅₀ = 90 ± 10 μM) and then VIPTEPPHA (IC₅₀ = 123 ± 5 μM) (<i>p</i> < 0.05). These peptides were noncompetitive inhibitors, as supported by kinetic studies and a molecular docking investigation. This study demonstrated that peptides derived from faba beans have multifunctional bioactivities, making them a promising food-functional and nutraceutical ingredient.Journal of agricultural and food chemistryAntioxidant and Angiotensin-Converting Enzyme Inhibitory Activity of Faba Bean-Derived Peptides After <i>In Vitro</i> Gastrointestinal Digestion: Insight into Their Mechanism of Action.PMC10979453J-001964L'Hocine LMartineau-Cote DAchouri AKarboune SfalseAntioxidant and Angiotensin-Converting Enzyme Inhibitory Activity of Faba Bean-Derived Peptides After <i>In Vitro</i> Gastrointestinal Digestion: Insight into Their Mechanism of Action.Faba bean flour, after <i>in vitro</i> gastrointestinal digestion, showed important antioxidant and angiotensin-converting enzyme (ACE) inhibitory activities. In the present study, 11 faba bean- derived peptides were synthesized to confirm their bioactivities and provide a deeper understanding of their mechanisms of action. The results revealed that 7 peptides were potent antioxidants, namely, NYDEGSEPR, TETWNPNHPEL, TETWNPNHPE, VIPTEPPH, VIPTEPPHA, VVIPTEPPHA, and VVIPTEPPH. Among them, TETWNPNHPEL had the highest activity in the ABTS (EC₅₀ = 0.5 ± 0.2 mM) and DPPH (EC₅₀ = 2.1 ± 0.1 mM) assays (<i>p</i> < 0.05), whereas TETWNPNHPE had the highest activity (<i>p</i> < 0.05) in the ORAC assay (2.84 ± 0.08 mM Trolox equivalent/mM). Synergistic and/or additive effects were found when selected peptides (TETWNPNHPEL, NYDEGSEPR, and VVIPTEPPHA) were combined. Four peptides were potent ACE inhibitors, where VVIPTEPPH (IC₅₀ = 43 ± 1 μM) and VVIPTEPPHA (IC₅₀ = 50 ± 5 μM) had the highest activity (<i>p</i> < 0.05), followed by VIPTEPPH (IC₅₀ = 90 ± 10 μM) and then VIPTEPPHA (IC₅₀ = 123 ± 5 μM) (<i>p</i> < 0.05). These peptides were noncompetitive inhibitors, as supported by kinetic studies and a molecular docking investigation. This study demonstrated that peptides derived from faba beans have multifunctional bioactivities, making them a promising food-functional and nutraceutical ingredient.2024-01-01T00:00:00Z2024 Mar2025-04-21T21:27:40.356Z2025-04-05T18:25:33.929ZS-EPMC109794533847011010.1021/acs.jafc.4c00829