Journal of the science of food and agriculture · 2026
Bioactive peptide fractions from Vigna unguiculata: Inhibition kinetics, gastrointestinal stability, cytotoxicity assessment, and amino acid profile as compositional features associated with antihypertensive activity.
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Cú-Cañetas Trinidad, Drago Silvina R, Rodríguez-Canto Wilbert, Chel-Guerrero Luis, Betancur-Ancona David
Аннотация
BACKGROUND: Food-derived bioactive peptides are promising alternatives for hypertension management; however, their application depends on favorable safety profiles, gastrointestinal stability, and a well-defined mechanism of action. For legumes, few studies of these aspects and amino acid composition exist. This work provides an integrated characterization of peptide fractions obtained from cowpea (Vigna unguiculata) seed proteins and establishes amino acid composition-function relationships for antihypertensive applications.
RESULTS: A cowpea protein concentrate (648.3 g kg-1 protein) was hydrolyzed using Flavourzyme or a sequential pepsin-pancreatin (PP) system, followed by ultrafiltration to obtain fractions of different molecular weights. Angiotensin I-converting enzyme (ACE-I) inhibition kinetics, cytotoxicity in VERO cells, and gastrointestinal stability after simulated digestion were evaluated. Amino acid profiles were determined by high-performance liquid chromatography. All fractions exhibited a non-competitive ACE-I inhibition mechanism, with Vmax reduced by 86.6-92.1% and minimal changes in Km. Peptides retained 79.5-97.2% of inhibitory activity after digestion, with the <1 kDa-PP fraction being the most stable (97.2%). Cytotoxicity IC50 values (4.36-8.40 μg mL-1) yielded wide safety margins (92- to 146-fold) relative to ACE-I inhibitory concentrations. Amino acid analysis revealed high proportions of charged residues (41.6-47.9%), moderate aromatic content, strategic proline levels, high branched-chain amino acids, and absence of cysteine.
CONCLUSION: The <1 kDa-PP V. unguiculata peptide fractions combine non-competitive ACE-I inhibition, high digestive stability, and low cytotoxicity, presenting potential as antihypertensive ingredients in functional foods and nutraceuticals. These findings warrant further investigation, including the identification of sequences within the active fractions and in vivo validation of antihypertensive efficacy. © 2026 Society of Chemical Industry.
RESULTS: A cowpea protein concentrate (648.3 g kg-1 protein) was hydrolyzed using Flavourzyme or a sequential pepsin-pancreatin (PP) system, followed by ultrafiltration to obtain fractions of different molecular weights. Angiotensin I-converting enzyme (ACE-I) inhibition kinetics, cytotoxicity in VERO cells, and gastrointestinal stability after simulated digestion were evaluated. Amino acid profiles were determined by high-performance liquid chromatography. All fractions exhibited a non-competitive ACE-I inhibition mechanism, with Vmax reduced by 86.6-92.1% and minimal changes in Km. Peptides retained 79.5-97.2% of inhibitory activity after digestion, with the <1 kDa-PP fraction being the most stable (97.2%). Cytotoxicity IC50 values (4.36-8.40 μg mL-1) yielded wide safety margins (92- to 146-fold) relative to ACE-I inhibitory concentrations. Amino acid analysis revealed high proportions of charged residues (41.6-47.9%), moderate aromatic content, strategic proline levels, high branched-chain amino acids, and absence of cysteine.
CONCLUSION: The <1 kDa-PP V. unguiculata peptide fractions combine non-competitive ACE-I inhibition, high digestive stability, and low cytotoxicity, presenting potential as antihypertensive ingredients in functional foods and nutraceuticals. These findings warrant further investigation, including the identification of sequences within the active fractions and in vivo validation of antihypertensive efficacy. © 2026 Society of Chemical Industry.