Separation and Purification of Angiotensin Converting Enzyme Inhibitory Peptides Derived from Goat's Milk Casein Hydrolysates

  • Lee, K.J. (Division of Animal Science and Technology, College of Agriculture and Life Sciences Gyeongsang National University) ;
  • Kim, S.B. (Dairy Science Division, Department of Livestock Resources Development, National Livestock Research Institute) ;
  • Ryu, J.S. (Division of Animal Science and Technology, College of Agriculture and Life Sciences Gyeongsang National University) ;
  • Shin, H.S. (Nam Yang Research and Development Center) ;
  • Lim, J.W. (Division of Animal Science and Technology, College of Agriculture and Life Sciences Gyeongsang National University)
  • Received : 2004.09.22
  • Accepted : 2004.12.22
  • Published : 2005.05.01


To investigate the basic information and the possibility of ACE-inhibitory peptides for antihypertension materials, goat's caisin (CN) was hydrolyzed by various proteolytic enzymes and ACE-inhibitory peptides were separated and purified. ACE-inhibition ratios of enzymatic hydrolysates of goat's CN and various characteristics of ACE-inhibitory peptides were determined. ACE-inhibition ratios of goat's CN hydrolysates were shown the highest with 87.84% by pepsin for 48 h. By Sephadex G-25 gel chromatograms, Fraction 3 from goat's CN hydrolysates by pepsin for 48 h was confirmed the highest ACE-inhibition activity. Fraction 3 g and Fraction 3 gh from peptic hydrolysates by RP-HPLC to first and second purification were the highest in ACE-inhibition activity, respectively. The most abundant amino acid was leucine (18.83%) in Fraction 3 gh of ACE-inhibitory peptides after second purification. Amino acid sequence analysis of Fraction 3 gh of ACE-inhibitory peptides was shown that the Ala-Tyr-Phe-Tyr, Pro-Tyr-Tyr and Tyr-Leu. IC$_{50}$ calibrated in peptic hydrolysates at 48 h, Fraction 3, Fraction 3 g and Fraction 3 gh from goat's CN hydrolysates by pepsin for 48 h were 29.89, 3.07, 1.85 and 0.87 g/ml, respectively. Based on the results of this experiment, goat's CN hydrolysates by pepsin were shown to have ACE-inhibitory activity.


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