Angiotensin I-Converting Enzyme Inhibitory Activity of the ${\kappa}-Casein$ Fragments Hydrolysated by Chymosin, Pepsin, and Trypsin

${\kappa}-Casein$의 Chymosin, Pepsin 및 Trypsin 가수분해물에 대한 안지오텐신 변환효소 저해효과의 탐색

  • Published : 1997.12.01


The isolated ${\kappa}-Casein$ on gel permeation chromatography was hydrolyzed by chymosin, trypsin, and pepsin. The 3% TCA soluble portion of the hydrolysates were dialyzed on the angiotensin-I converting enzyme (ACE) inhibition rate (%,) and inhibitory activity $(IC_{50})$ were determined. The trypsin hydrolysate exhibited the highest ACE inhibition rate while the chymosin hydrolysation showed the lowest activity. The hydrolysate was dialyzed using dialysis membrane with various molecular cut-offs, and $IC_{50}$ was determined. As the pore size of the dialysis tubing increased, the ACE inhibitory activity decreased.