Identification and Antihypertension Study of Novel Angiotensin I-Converting Enzyme Inhibitory Peptides from the Skirt of <i>Chlamys farreri</i> Fermented with <i>Bacillus natto</i>
Jie Gao, Qi Liu, Ling Zhao, Jia Yu, Shanglong Wang, Tingfeng Cao, Xiang Gao, Yuxi Wei
Abstract
The aim of this study was to isolate the angiotensin I-converting enzyme (ACE) inhibitory peptides from the skirt of Chlamys farreri fermented with Bacillus natto and to explore the antihypertension effect through in vivo studies. ACE inhibitory peptides were purified from the fermentation mixture by ultrafiltration, gel filtration chromatography, and reversed-phase high-performance liquid chromatography sequentially. The amino acids’ sequence of the five novel ACE inhibitory peptides were identified by liquid chromatography–tandem mass spectrometry. Animal experiments demonstrated that the novel ACE inhibitory peptides significantly reduced the blood pressure in spontaneously hypertensive rats after a single or long-time treatment. Potential mechanisms were explored, and the results indicated that the novel peptides could regulate the renal renin-angiotensin system, improve vascular remodeling, inhibit myocardial fibrosis, and rebalance the gut microbial dysbiosis. Our results suggest that the fermentation products of the Chlamys farreri skirt by B. natto are potential sources of active peptides processing antihypertension activities.