• ACE-inhibitory activity;
  • biologically active peptides;
  • lentil globulin hydrolysate


The aim of this study was the identification of potentially bioaccessible ACE-inhibitory peptides obtained by in vitro gastrointestinal digestion of lentil globulins. ACE-inhibitory peptides were purified by ion exchange chromatography and gel filtration. After the first step of purification, three peptide fractions with potential antihypertensive properties were obtained and the highest inhibitory activity was determined for the fraction 5 (IC50 = 0.02 mg mL−1). This fraction was separated on Sephadex G10, and six peptide fractions were obtained. The peptides of fraction (5-F) with the highest potential antihypertensive activity (IC50 = 0.13 mg mL−1) were identified using ESI-MS/MS. The sequences of peptides were KLRT, TLHGMV and VNRLM. Based on Lineweaver–Burk plots for the fraction 5-F, the kinetic parameters as Km (1.24 mm), Vmax (0.012 U min−1), Ki (0.12 mg mL−1) and mode of inhibition were determined.