Purification and Characterization of an Angiotensin Converting Enzyme Inhibitor from Squid Ink

  • Kim, So-youn (Department of Food Science and Technology, College of Agriculture and Life Sciences, Chungnam National University) ;
  • Kim, Sun-hye (Department of Food Science and Technology, College of Agriculture and Life Sciences, Chungnam National University) ;
  • Song, Kyung-Bin (Department of Food Science and Technology, College of Agriculture and Life Sciences, Chungnam National University)
  • 발행 : 2003.10.01

초록

Angiotensin converting enzyme (ACE) converts angiotensin I into angiotensin II by cleaving C-terminal dipeptide of angiotensin I and inactivates bradykinin. ACE inhibitors have been screened from various food sources since the inhibitors decrease blood pressure. Therefore, in this study, an ACE inhibitor was isolated and purified from squid ink using membrane filtration, gel permeation chromatography, normal phase HPLC, and fast protein liquid chromatography. The purified inhibitor was identified to be a molecular mass of 294 by mass spectrometry, and to have IC$\sub$50/ value of 4.9 $\mu\textrm{g}$/mL.

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