Separation and purification of angiotensin converting enzyme inhibitory peptides derived from Goat's milk casein hydrolysates

摘要: To investigate the basic information and possibility of ACE-inhibitory peptides for antihypertension materials, goat's caisin (CN) was hydrolyzed by various proteolytic enzymes were separated purified. ACE-inhibition ratios enzymatic hydrolysates CN characteristics determined. shown highest with 87.84% pepsin 48 h. By Sephadex G-25 gel chromatograms, Fraction 3 from h confirmed activity. g gh peptic RP-HPLC to first second purification in activity, respectively. The most abundant amino acid leucine (18.83%) after purification. Amino sequence analysis that Ala-Tyr-Phe-Tyr, Pro-Tyr-Tyr Tyr-Leu Leu-Lys-Asp-Tyr-Gly-Gly-Val-Ser-Leu. IC 5 0 calibrated at h, 3, 29.89, 3.07, 1.85 0.87 g/ml, Based on results this experiment, have