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

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.