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Animal Products
Asian-Australasian Journal of Animal Sciences 2005;18(5): 741-746.
DOI: https://doi.org/10.5713/ajas.2005.741    Published online November 25, 2005.
Separation and Purification of Angiotensin Converting Enzyme Inhibitory Peptides Derived from Goat`s Milk Casein Hydrolysates
K. J. Lee, S. B. Kim, J. S. Ryu, H. S. Shin, J. W. Lim
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. ACEinhibition ratios of enzymatic hydrolysates of goat`s CN and various characteristics of ACE-inhibitory peptides were determined. ACEinhibition 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. IC50 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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