Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Dipeptide (Tyr-Ile) Acting as an Inhibitor of Angiotensin-I-Converting Enzyme (ACE) from the Hydrolysate of Jellyfish Nemopilema nomurai

  • Kim, Yeon-Kye (Food and Safety Research Division, National Fisheries R&D Institute) ;
  • Lim, Chi-Won (Food and Safety Research Division, National Fisheries R&D Institute) ;
  • Yeun, So-Mi (Food and Safety Research Division, National Fisheries R&D Institute) ;
  • Lee, Moon-Hee (Food and Safety Research Division, National Fisheries R&D Institute) ;
  • Moon, Ho-Sung (Food and Safety Research Division, National Fisheries R&D Institute) ;
  • Cho, Hyeon-Ah (Food and Safety Research Division, National Fisheries R&D Institute) ;
  • Yoon, Na-Young (Food and Safety Research Division, National Fisheries R&D Institute) ;
  • Yoon, Ho-Dong (Food and Safety Research Division, National Fisheries R&D Institute) ;
  • Park, Hee-Yeon (Food and Safety Research Division, National Fisheries R&D Institute) ;
  • Lee, Doo-Seog (Food and Safety Research Division, National Fisheries R&D Institute)
  • Received : 2011.10.06
  • Accepted : 2011.11.08
  • Published : 2011.12.31
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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 $C_{18}$ 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 $6.56{\pm}1.12$ and $3.10{\pm}0.28\;{\mu}M$, 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.

Keywords

References

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