ABSTRACT Various antihypertensive peptides originating from food protein are introduced in this paper. Most of the reported antihypertensive peptides have inhibitory activities of angiotensin I-converting enzyme (ACE) that catalyzes release of potent vasoconstrictor, angiotensin II from angiotensin I. These ACE inhibitory peptides have been mostly isolated from proteolysis of food protein sources and fermented milk. Structural features of these ACE inhibitory peptides are briefly summarized in this review. Among these peptides, our previous studies about antihypertensive peptides, Val-Pro-Pro and Ile-Pro-Pro, generated from casein by fermentation with lactic acid bacteria will be reviewed extensively. For the current topics of our studies, newly developed peptides by an enzymatic hydrolysis of milk casein which contains much of X-Pro-Pro and X-Pro peptides will be introduced. The new peptide materials contained ACE inhibitory peptides, Val-Pro-Pro and Ile-Pro-Pro, showed dose dependent antihypertensive effect on spontaneously hypertensive rats. Moreover, recent study showed a significant blood pressure lowering effect for subjects with high-normal and mild-hypertension. Through recent our study, possibility of the bioactive peptide for human use as a functional food material will be discussed.
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