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Evaluation of Angiotensin -I- Converting Enzyme Inhibitory Activity and Protein Changes of Enzymatic Hydrolysate Extracted from Hanwoo Loin and Round Myosin B

한우 등심과 우둔에서 추출한 Myosin B의 효소적 가수분해물의 단백질 변화와 Angiotensin -I- Converting Enzyme(ACE) 저해효과

  • Kim, Y.J. (Dept. of Animal Science and Institute of Agricultural Science and Technology, Chonnam National University) ;
  • Chin, Koo-Bok (Dept. of Animal Science and Institute of Agricultural Science and Technology, Chonnam National University)
  • 김영주 (전남대학교 동물자원학부 식육과학 연구실 및 농업과학기술연구소) ;
  • 진구복 (전남대학교 동물자원학부 식육과학 연구실 및 농업과학기술연구소)
  • Published : 2007.02.28

Abstract

This study was performed to determine the protein profiles using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Angiotensin-I-converting enzyme(ACE) inhibitory activity (IC50) as affected by the various meat cuts, digestion times with pepsin. Hydrolysates having the protein concentration of 10 ug/mL had approximately 36∼39% ACE inhibitory activities, regardless of meat cut and digestion time. Protein concentration and ACE inhibitory activity of the diluted hydrolysate increased after 1-hr digestion. In original hydrolysates, ACE inhibitory activities of loin had higher than those of round (P<0.05). In addition, non-heated hydrolysates had higher ACE inhibitory activities than heated counterparts. When myosin B was digested by pepsin more than 1 hr, improved ACE inhibitory activities were observed as compared to the non-digested control.

Keywords

Angiotensin converting enzyme(ACE) inhibitory activity;Myosin B;Hanwoo loin and round

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