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Inhibitory Effect on Angiotensin-converting Enzyme (ACE) and Optimization for Production of Ovotransferrin Hydrolysates
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 Title & Authors
Inhibitory Effect on Angiotensin-converting Enzyme (ACE) and Optimization for Production of Ovotransferrin Hydrolysates
Lee, Na-Kyoung; Ahn, Dong-Uk; Park, Keun-Kyu; Paik, Hyun-Dong;
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Angiotensin-converting enzyme (ACE) inhibitory activity and production optimization of ovotransferrin hydrolysates were studied. Ovotransferrin was hydrolyzed by several enzymes (protamex, alcalase, trypsin, pepsin, neutrase, and flavorzyme) and acid (0.03 N HCl). Ovotransferrin hydrolysate reduced ACE activity by 60.2%, 55.8%, and 42.6% when treated with trypsin, acid, and pepsin, respectively. Trypsin was selected for production of peptide having maximum AC inhibitory effect, which was greatest with 7 h hydrolysis. Central composite design determined that optimum composition of ACE inhibitory substances using substrate concentration of 20-35%, temperature of , and pH of 6.0-8.0. The optimum composition was 1% trypsin, substrate concentration of 26.32%, , and pH 6.32. Under this conditions, a maximum ACE inhibitory effect of 69.1% was evident, similar to the predicted value.
ovotranferrin;hydrolysate;angiotensin-converting enzyme;trypsin;response surface methodology;
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