Identification of oyster-derived hypotensive peptide acting as angiotensin-I-converting enzyme inhibitor

Kazuhiro Shiozaki, Momo Shiozaki, Junko Masuda, Akiko Yamauchi, Shuichi Ohwada, Toshiki Nakano, Toshiyasu Yamaguchi, Tadao Saito, Koji Muramoto, Minoru Sato

Research output: Contribution to journalArticlepeer-review

38 Citations (Scopus)


Angiotensin-I-converting enzyme (ACE) plays a crucial role in the crisis of hypertension. Some peptides that originate from protease hydrolysates are known to suppress ACE activity in vitro and in vivo. Here, we investigated whether trypsin hydrolysate of oyster Crassostrea gigas showed hypotensive activity and ACE inhibition. The hydrolysate significantly suppressed systolic blood pressure and ACE activity in spontaneously hypertensive rats following a one-shot oral administration and a long-term feeding experiment lasting 9 weeks. Each hydrolysate from oyster tissue showed ACE inhibitory activity, indicating the hypotensive effect was due to synergism. One potent ACE inhibitory peptide, Asp-Leu-Thr-Asp-Tyr, was identified from the hydrolysate of the striate muscle, and the peptide exhibited hypotensive activity in vivo. Protease digestion analysis suggested that Asp-Tyr could be the real effector of this penta-peptide in vivo.

Original languageEnglish
Pages (from-to)865-872
Number of pages8
JournalFisheries Science
Issue number5
Publication statusPublished - 2010


  • Angiotensin-I-converting enzyme
  • Hypotensive
  • Oyster
  • Peptide
  • Spontaneously hypertensive rat


Dive into the research topics of 'Identification of oyster-derived hypotensive peptide acting as angiotensin-I-converting enzyme inhibitor'. Together they form a unique fingerprint.

Cite this