Angiotensin I-converting Enzyme Inhibitory Activity of Peanut Protein Hydrolysates Prepared with Alcalase

Peanut protein hydrolysates were prepared by enzymatic hydrolysis with Alcalase and Neutrase, and the angiotensin I-converting enzyme (ACE) inhibitory activities of the enzymatic hydrolysates were investigated at different hydrolysis times. The unhydrolyzed protein showed no inhibitory activity. Hydrolysates generated with Neutrase displayed very low ACE inhibitory activity, while those obtained with Alcalase exhibited high inhibitory activity. The highest ACE inhibitory activity with the IC_ 50 value of 0.56 mg protein/mL was found in the hydrolysate obtained with Alcalase at 30 min of hydrolysis time. These results indicate that peanut protein is a good protein source of ACE inhibitory peptides when hydrolyzed with the protease Alcalase. The peanut protein hydrolysates prepared with Alcalase might be utilized for physiologically functional foods with antihypertensive activity.