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.
Highlights
A number of peptides generated from food proteins have been shown to possess various bioactivities such as antihypertensive, antioxidant, immunomodulation, antimicrobial and antiobesity [1,2,3]
In order to study the Angiotensin I-converting enzyme (ACE)-inhibitory effect of Jinhua ham peptides (JHP), the ACE-inhibitory activity of the peptides was analyzed under a gradient range of concentrations (Figure 1)
According to the current study, ACE-inhibitory peptides were stable against heat treatment as well as the NaCl
Summary
A number of peptides generated from food proteins have been shown to possess various bioactivities such as antihypertensive, antioxidant, immunomodulation, antimicrobial and antiobesity [1,2,3]. Bioactive peptides can be released by hydrolysis, digestion or during food processing including fermentation and ripening [4,5]. Dry-cured meat product can release a great quantity of free amino acids and small peptides during fermentation and ripening periods [7]. During the long-ripening period, muscle proteins are hydrolyzed by endogenous enzymes, slowly releasing small peptides and free amino acids which contribute to the unique flavor of Jinhua ham [8,9]. In terms of bioactive peptides in Jinhua ham, current studies have focused on their antioxidant activity. Crude peptides extracted from Jinhua ham were proved to possess DPPH scavenging ability of 77.39% and great antioxidant activity in PC12 cell model [10,11]. No studies have investigated the antihypertensive abilities of Jinhua ham peptides (JHP) to date
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