Gu, Shuang, et al. “Identification of a Novel Post-digestion Angiotensin I-Converting Enzyme Inhibitory Peptide from Silver Prussian Carp (Carassius auratus gibelio) Roe.” ACS Food Science & Technology 3.3 (2023): 450-458. https://doi.org/10.1021/acsfoodscitech.2c00360
Abstract
Proteins of aquatic products are potential sources of bioactive peptides. This study attempted to screen 29 kinds of aquatic products with the highest angiotensin I-converting enzyme (ACE) inhibitory activity and to identify the active peptide. Results showed that the enzyme hydrolysate of silver Prussian carp roe exhibited the highest ACE inhibitory rate before (64.71%) and after (53.82%) digestion. LAKVAP identified from the enzymatic extract of silver Prussian carp roe was a competitive inhibitor, with an ACE inhibitory rate of 95.33%. The molecular docking study suggested that LAKVAP formed hydrogen bonds with S2 active sites (Gln281, His 353, and His513) and made coordinate bonds with Zn2+ (His383) of ACE, which contributed to the interaction between ACE and peptide. The results suggested that silver Prussian carp roe proteins could be suitable materials for ACE inhibitory peptide preparation, and LP-6 might be potentially beneficial as an antihypertensive agent.