Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins

Inhibitors of angiotensin I-converting enzyme (ACE) have been shown to have antihypertensive effects and have been utilized for pharmaceuticals and physiologically functional foods. In the present study, efforts were directed to find ACE inhibitory activities derived from muscle proteins. Porcine skeletal muscle proteins were hydrolyzed by eight proteases, and the inhibitory activities of the hydrolysates toward ACE were measured. Among the digests of the water-insoluble protein fraction prepared from muscle, thermolysin digest demonstrated the highest activity. Also, among hydrolysates of porcine myosin produced by the same enzymes, thermolysin digest showed the most potent inhibitory activity. Two ACE inhibitory peptides were purified from thermolysin digest of myosin. The sequences of these inhibitory peptides, named myopentapeptides A and B, were Met-Asn-Pro-Pro-Lys and Ile-Thr-Thr-Asn-Pro. These sequences were found in the primary structure of the myosin heavy chain. The concentrations of the peptides showing 50% inhibition values (IC50) of ACE were 945.5 and 549.0 μM, respectively. Also, six tripeptides, Met-Asn-Pro, Asn-Pro-Pro, Pro-Pro-Lys, Ile-Thr-Thr, Thr-Thr-Asn, and Thr-Asn-Pro, which have parts of the sequences of the myopentapeptides, demonstrated activity. Their IC50 values were 66.6, 290.5, >1000, 678.2, 672.7, and 207.4 μM, respectively.