- Volume 18 Issue 5
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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
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