@article{jfnr2017553,
author={{Zuo, Qing-xiang and Zhang, Wan-gang and Xing, Lu-juan and Zheng, Jin-xiao and Zhou, Guang-hong},
title={Stability of Angiotensin I-converting Enzyme Inhibitory Activity of Peptides Extracted from Dry-cured Jinhua Ham},
journal={Journal of Food and Nutrition Research},
volume={5},
number={5},
pages={301--308},
year={2017},
url={http://pubs.sciepub.com/jfnr/5/5/3},
issn={2333-1240},
abstract={Angiotensin I-converting enzyme (ACE) inhibitory activity of peptides extracted from traditional dry-cured Jinhua ham was investigated. The ACE-inhibitory activity was measured after the treatments of heat, NaCl, pH and simulated gastro-intestinal digestion. Peptides possessed an ACE-inhibitory activity of 53.53% at 10 mg/mL and showed a good stability against different heating temperatures (up to 100ˇăC), heating times (up to 60 min) and acid conditions. The NaCl had no significant effects on the ACE-inhibitory activity, while there was a sharp decline under alkaline condition. The ACE-inhibitory activity increased by 4.01% after pepsin treatment and then remained constant after trypsin treatment. The increased ACE-inhibitory activity after pepsin digestion could be explained by the greater exposure of hydrophobic residues. In this study, peptides extracted from Jinhua ham were proved to have ACE-inhibitory activity which showed a good stability against various processing conditions as well as the simulated gastro-intestinal digestion.},
doi={10.12691/jfnr-5-5-3}
publisher={Science and Education Publishing}
}