Identifying peptides from oat protein with potential hypocholesterolemic and satiety effects

Obesity and hypercholesterolemia cause significant public health challenges, demanding alternative dietary strategie. This study investigated the cholesterol-lowering and satiety-enhancing effects of peptides derived from oat protein hydrolysates. Oat protein was hydrolyzed using pepsin and trypsin, and the resulting peptides were fractionated based on hydrophobicity. The fractions were than evaluated for their inhibitory effects on dipeptidyl-peptidase 4 (DPP4) and HMG-CoA reductase (HMGCR), as well as their impact on cholesterol micelle solubility. The most potent fraction (F4) exhibited 50 % inhibition of DPP4 at 50 μg/ml, potentially enhancing satiety. Fractions F3, F4, and hydrolyzed peptides inhibited HMGCR by 85 %, 79 %, and 83 %, respectively, at 200 μg/ml, while F1 reduced cholesterol micelle solubility by 38 % at 2 mg/ml. LC-MS/MS analysis identified peptides enriched in proline, leucine, and aromatic amino acids, contributing to bioactivity. These findings suggested oat protein-derived peptides as promising candidate for functional food development formulations aimed at mitigating obesity and hypercholesterolemia. • In vitro digestion by pepsin and trypsin in simulated gut conditions was effective to generate small peptides from oat protein. • Oat peptides showed capacity to inhibit DPP4 and HMGCR, promoting satiety and lowering cholesterol. • Hydrophobic and aromatic amino acids enhanced enzyme inhibition potential. • LC-MS/MS and de novo sequencing identified key bioactive oat peptides. • Oat protein based functional foods have potential for obesity and cholesterol management.