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.
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