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김연계,임치원,연소미,이문희,문호성,조현아,윤나영,윤호동,박희연,이두석 한국수산과학회 2011 Fisheries and Aquatic Sciences Vol.14 No.4
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 C_(18) and C_(12) columns. The IR, 1H NMR, 13C NMR, and MS spectrometer analyses showed that the dipeptide comprised tyrosine-isoleucine (Tyr-Ile). The IC_(50) and K_i values were 6.56 ± 1.12 and 3.10 ± 0.28 μM, respectively, indicating competitive inhibition of angiotensin-Ι-converting enzyme (ACE). As a novel ACE-inhibitory active peptide, Tyr-Ile may have potential for use in antihypertensive therapy.