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

作者：Barbana Chockry; Boye Joyce Irene^*

来源：Food Research International, 2010, 43(6): 1642-1649.

DOI：10.1016/j.foodres.2010.05.003

• ACE inhibitory activity
• Bioactivity
• Chickpea
• Enzymatic digestion
• Pea

CE 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 SOS-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 (IC(50) of 140 +/- 1 mu g/ml) compared to its digests obtained by alcalase/flavourzyme (IC(50) of 228 +/- 3 mu g/m1) or papain (IC(50) of 180 +/- 1 mu/ml) ;and to chickpea kabuli hydrolysed by gastrointestinal simulation (IC(50) of 229 +/- 1 mu/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.

• 出版日期2010-7