Angiotensin I-converting enzyme inhibitory activity of chickpea and pea protein hydrolysates

ACE inhibitory activity was studied for different hydrolysates obtained from protein concentrates of chickpea (kabuli and desi) and yellow pea (Golden) using in vitro gastrointestinal simulation, alcalase/flavourzyme, and papain. Protein/peptide profiles studied by SDS–PAGE and SE-HPLC, showed a rich composition of the hydrolysates in small peptides having MWs under 4 kDa. Papain hydrolysed yellow pea proteins showed the highest ACE inhibitory activity. In addition, chickpea desi proteins hydrolysed by in vitro gastrointestinal simulation showed higher ACE inhibition (IC₅₀ of 140 ± 1 μg/ml) compared to its digests obtained by alcalase/flavourzyme (IC₅₀ of 228 ± 3 μg/ml) or papain (IC₅₀ of 180 ± 1 μg/ml) and to chickpea kabuli hydrolysed by gastrointestinal simulation (IC₅₀ of 229 ± 1 μg/ml). The results demonstrate that enzymatic hydrolysates of chickpea and pea proteins contain bioactive ACE inhibitory peptides; furthermore, the type of enzyme used for hydrolysis affects the ACE inhibitory activity.