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http://dx.doi.org/10.5851/kosfa.2010.30.2.286

Inhibitory Effect on Angiotensin-converting Enzyme (ACE) and Optimization for Production of Ovotransferrin Hydrolysates  

Lee, Na-Kyoung (Division of Animal Life Science and Bio/Molecular Informatics Center, Konkuk University)
Ahn, Dong-Uk (Department of Animal Science, Iowa State University and Major in Biomodulation, Seoul National University)
Park, Keun-Kyu (Animal Resources Research Center, Konkuk University)
Paik, Hyun-Dong (Division of Animal Life Science and Bio/Molecular Informatics Center, Konkuk University)
Publication Information
Food Science of Animal Resources / v.30, no.2, 2010 , pp. 286-290 More about this Journal
Abstract
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 $35-55^{\circ}C$, and pH of 6.0-8.0. The optimum composition was 1% trypsin, substrate concentration of 26.32%, $51.29^{\circ}C$, and pH 6.32. Under this conditions, a maximum ACE inhibitory effect of 69.1% was evident, similar to the predicted value.
Keywords
ovotranferrin; hydrolysate; angiotensin-converting enzyme; trypsin; response surface methodology;
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Times Cited By Web Of Science : 0  (Related Records In Web of Science)
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