Journal
FOODS
Volume 12, Issue 1, Pages -Publisher
MDPI
DOI: 10.3390/foods12010050
Keywords
Muscovy duck plasma; ACE inhibitory peptide; purification; identification; molecule docking
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This study investigated angiotensin-converting enzyme inhibitory peptides (ACE-IPs) derived from Muscovy duck plasma hydrolysate (MDPH). The crude ACE-IPs were separated and purified using ultrafiltration, gel chromatography, and reversed-phase high-performance liquid chromatography (RP-HPLC). The components with the highest ACE inhibition potential were selected for identification. The peptide VALSSLRP showed high ACE inhibitory activity (91.67 +/- 0.73%) due to its tight binding to the S1 ' pocket and formation of 3 hydrogen bonds. This study provides new information about the generation of ACE-IPs from duck blood plasma.
In this study, angiotensin-converting enzyme inhibitory peptides (ACE-IPs) derived from Muscovy duck (Cairina moschata) plasma hydrolysate (MDPH) were investigated. According to the general research protocol for bioactive peptides, the crude ACE-IPs of Muscovy duck plasma were separated and purified by ultrafiltration, gel chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC). Then the components with the highest ACE inhibition potential were selected for identification. Finally, the inhibition mechanism was explored by molecular docking and in silico simulated digestion. A total of 121 peptides was detected, and five were screened for synthesis verification and molecular docking. The peptide VALSSLRP revealed high ACE inhibitory activity (91.67 +/- 0.73%) because this peptide bound tightly to the S1 ' pocket and formed 3 hydrogen bonds. Meaningfully, this work provides some new information about the generation of ACE-IPs derived from duck blood plasma.
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