Phaseolus lunatus protein concentrates and the proteases Alcalase (R) and Pepsin-Pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Protein concentrate obtained from germinated and ungerminated seeds flour was hydrolyzed with Alcalase (R) at enzyme/substrate ratio (E/S) 1/10 and during 0.5 and 2.0 h, respectively. Dn the other hand, protein concentrate obtained from ungerminated (E/S: 1/10) and germinated (E/S: 1/50) seeds flour was sequentially hydrolyzed with Pepsin-Pancreatin during 1.0 and 3.0 h, respectively. Peptide fractions with ACE inhibitory activity in a range of 0.9 to 3.8 µg/mL were obtained by G-50 gel filtration chromatography and high-performance liquid chromatography C18 reverse phase chromatography. The observed amino acid composition suggests a substantial contribution of hydrophobic residues to the peptides' inhibitory potency, which potentially acts via blocking of angiotensin II production. These results show that P. lunatus seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with Alcalase (R) and Pepsin-Pancreatin.Keywords: P. lunatus; hydrolysates; peptides; ACE inhibitory activity.Practical Application: Legume proteins can enzymatically produce bioactive specific peptides for use in functional foods.