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http://dx.doi.org/10.5713/ajas.2005.741

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)
Publication Information
Asian-Australasian Journal of Animal Sciences / v.18, no.5, 2005 , pp. 741-746 More about this Journal
Abstract
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.
Keywords
ACE-inhibitory Peptide; Goat's Milk CN; Proteolytic Enzyme;
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