Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Angiotensin-Converting Enzyme Inhibitory Activity of Enzymatic Hydrolysates of Crassostrea gigas (Oyster)

굴 효소 가수분해물의 angiotensin converting enzyme 저해작용

  • Do, Hyung-Joo (Department of Bioscience and Biotechnology, Graduate school, Silla University) ;
  • Park, Hye-Jin (Department of Bioscience and Biotechnology, Graduate school, Silla University) ;
  • Kim, Ok-Ju (Department of Bioscience and Biotechnology, Graduate school, Silla University) ;
  • Kim, Andre (Department of Pharmaceutical Engineering, College of Medical & Life Science, Silla University) ;
  • Choi, Yeung-Joon (Department of Seafood Science and Technology/ Institute of Marine Industry, Gyeongsang National University) ;
  • Choung, Se-Young (Department of Hygienic Chemistry, College of Pharmacy, Kyung Hee University) ;
  • Ha, Jong-Myung (Department of Bioscience and Biotechnology, Graduate school, Silla University)
  • 도형주 (신라대학교 대학원 생명공학과) ;
  • 박혜진 (신라대학교 대학원 생명공학과) ;
  • 김옥주 (신라대학교 대학원 생명공학과) ;
  • 김안드레 (신라대학교 제약공학과) ;
  • 최영준 (경상대학교 해양식품공학과/해양산업연구소) ;
  • 정세영 (경희대학교 약학대학 위생약학 및 독성학실) ;
  • 하종명 (신라대학교 대학원 생명공학과)
  • Received : 2011.12.06
  • Accepted : 2011.12.09
  • Published : 2012.02.28
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Abstract

The peptides of enzymatic hydrolysates from oyster were determined by inhibitory activity against angiotensin-converting enzyme. The ACE inhibitory activity of enzymatic oyster hydrolysates increases with hydrolysis time. Among enzymatic oyster hydrolysates, oyster hydrolysates incubated with Protamex showed the best ACE inhibitory activity after 10 h. Hydrolysates were filtered through a HiSep ultrafiltration membrane (M.W. cut-off 30 kDa, 10 kDa) to obtain the peptide fractions with ACE inhibition activity. These fractions were applied to an HPLC column (watchers 120 ODS-AP $250{\times}4.6$ ($5{\mu}m$)). Six active fractions were collected and the range of ACE inhibition was from 29.56 to 85.85%. Peptide was purified from fraction B, showing the highest ACE inhibitory activity, and its sequence was Leu-Gln-Pro. These results suggest that PEH may be beneficial for developing antihypertensive food and drug.

굴 효소 가수분해물은 굴을 alcalase, protamex, neutrase, flavourzyme, pepsin으로 각각 처리하였고, 이들의 ACE 저해활성을 측정하였다. ACE 저해활성은 가수분해 시간에 따라 증가 또는 감소하였으며, 그 중 10시간 이상 가수분해 처리한 PEH에서 가장 높은 ACE 저해활성을 나타내었다. PEH 가수분해물을 한외여과(30, 10 kDa) 하여 낮은 분자량의 분획물을 얻었다. 30 kDa와 10 kDa 이하 분자량 별 ACE 저해활성은 각각 $69.18{\pm}0.75$, $83.71{\pm}1.12$의 활성을 나타내었다. 이 결과 10 kDa 이하의 시료로부터 HPLC column (watchers 120 ODS-AP $250{\times}4.6$ ($5{\mu}m$))을 이용하여 각각의 활성 분획을 분취하여 얻은 6분획의 ACE 저해 활성은 29.56~85.85% 로 나타났다. 그 중 저해활성이 가장 높게 나타나는 B fraction의 아미노산 서열을 확인한 결과 Leu-Gln-Pro 임을 확인하였고, peptide합성하여 얻은 저해활성 농도($IC_{50}$)가 1.18 uM임을 확인하였다. 이러한 결과는 PEH를 이용하여 건강 기능성 식품의 개발에 도움이 될 수 있을 것으로 생각된다.

Keywords

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