Dipeptide (Tyr-Ile) acting as an inhibitor of angiotensin-I-converting enzyme (ACE) from the hydrolysate of jellyfish nemopilema nomurai

Abstract

The jellyfish Nemopilema nomurai was hydrolyzed with papain and a novel dipeptide purified via ultrafiltration, gel filtration chromatography with Sephadex LH-20, and reverse phase chromatography using C18 and C12 columns. The IR, 1H NMR, 13C NMR, and MS spectrometer analyses showed that the dipeptide comprised tyrosine-isoleucine (Tyr-Ile). The IC50 and Ki values were 6.56 ± 1.12 and 3.10 ± 0.28 μM, respectively, indicating competitive inhibition of angiotensin-I-converting enzyme (ACE). As a novel ACE-inhibitory active peptide, Tyr-Ile may have potential for use in antihypertensive therapy. © The Korean Society of Fisheries and Aquatic Science.