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Himali, S., Zhang, W. G., Lee, E. J. and Ahn, D. U. Egg Yolk Phosvitin and Functional Phosphopeptides—Review. Journal of Food Science, 76 (7), R143-R150. 2011.

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Article

Stability of Angiotensin I-converting Enzyme Inhibitory Activity of Peptides Extracted from Dry-cured Jinhua Ham

1Key Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Nanjing Agricultural University, Nanjing 210095, China


Journal of Food and Nutrition Research. 2017, Vol. 5 No. 5, 301-308
DOI: 10.12691/jfnr-5-5-3
Copyright © 2017 Science and Education Publishing

Cite this paper:
Qing-xiang Zuo, Wan-gang Zhang, Lu-juan Xing, Jin-xiao Zheng, Guang-hong Zhou. Stability of Angiotensin I-converting Enzyme Inhibitory Activity of Peptides Extracted from Dry-cured Jinhua Ham. Journal of Food and Nutrition Research. 2017; 5(5):301-308. doi: 10.12691/jfnr-5-5-3.

Correspondence to: Guang-hong  Zhou, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Nanjing Agricultural University, Nanjing 210095, China. Email: guanghong.zhou@hotmail.com

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 100°C), 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.

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