Korean Journal of Fisheries and Aquatic Sciences (한국수산과학회지)

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Purification of Angiotensin I-Converting Enzyme Inhibitory Peptide from Squid Todarodes pacificus Skin

오징어(Todarodes pacificus) 껍질로부터 Angiotensin I 전환효소 저해 펩티드의 분리 정제

  • Lee, Jung-Kwon (Department of Marine Biotechnology, Gangneung-Wonju National University) ;
  • Jeon, Joong-Kyun (Department of Marine Biotechnology, Gangneung-Wonju National University) ;
  • Byun, Hee-Guk (Department of Marine Biotechnology, Gangneung-Wonju National University)
  • 이정권 (강릉원주대학교 해양생물공학과) ;
  • 전중균 (강릉원주대학교 해양생물공학과) ;
  • 변희국 (강릉원주대학교 해양생물공학과)
  • Received : 2011.02.25
  • Accepted : 2011.04.12
  • Published : 2011.04.30
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Abstract

In this study, an angiotensin I-converting enzyme (ACE) inhibitor from squid skin was purified and characterized. Squid (Todarodes pacificus) skin protein isolates were hydrolyzed using six commercial proteases: alcalase, ${\alpha}$-chymotrypsin, neutrase, papain, pepsin, and trypsin. The peptic hydrolysate had the highest ACE inhibitory activity. The ACE inhibitory peptide was purified using Sephadex G-25 column chromatography and reverse phase high-performance liquid chromatography (HPLC) with a $C_{18}$ column. The purified ACE inhibitory peptide was identified and sequenced, and found to consist of seven amino acid residues: Ser-Ala-Gly-Ser-Leu-Val-Pro (657Da). The $IC_{50}$ value of the purified ACE inhibitory peptide was 766.2 ${\mu}M$, and Lineweaver-Burk plots suggested that the purified peptide acts as a noncompetitive ACE inhibitor. These results suggest that the ACE inhibitory peptide purified from the peptic hydrolysate of squid skin may be of benefit in developing antihypertensive drugs and functional foods.

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References

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