Improving ACE inhibitory activity of hazelnut peptide modified by plastein: Physicochemical properties and action mechanism. (15th February 2023)

• Record Type: Journal Article
• Authors: Song, Wentian; Fu, Junxi; Zeng, Qi; Lu, Hongyan; Wang, Ji; Fang, Li; Liu, Xiaoting; Min, Weihong; Liu, Chunlei
• Is Part Of: Food chemistry. Volume 402(2023)
• Publication Date: 2023-02-15
• Subjects: ACE inhibitory peptide -- Plastein reaction -- Physicochemical properties -- Identification -- MD simulation; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.134498
• Languages: English
• ISSNs: 0308-8146

Abstract

Graphical abstract: Highlights: Hazelnut-derived ACE-inhibiting peptides were first modified by plastein reaction. N -terminal amino acid clustering contributed to the improved ACE inhibition rate. Three novel ACE inhibitory peptides were reported. YYLLVR had the highest ACE inhibitory activity with inhibition rate 89.10%. Abstract: The plastein reaction can increase the activity of angiotensin-converting enzyme (ACE) inhibitory peptides, but the underlying mechanism is unknown. Hence, hazelnut protein hydrolysate and hazelnut peptide YLVR were used as substrate to explore the effect of plastein on physicochemical properties and the mechanism of structural change. The increase in turbidity and particle size and the decrease in free amino groups indicated that the reaction occurred via condensation. The modified products of YLVR were identified by NANO-HPLC-MS/MS, indicating that the N -terminal homologous amino acid aggregates in the plastein. Novel ACE inhibitory peptide YYLVR, YLLVR, and YYLLVR were synthesized and their inhibition rates were 66.35, 72.61, and 89.10 %, respectively, which were higher than that of YLVR (52.58 %). MD simulation showed that YYLLVR exhibited the lowest binding energies of −35.98 ± 2.30 kcal/mol to ACE. Taken together, plastein reaction is a promising strategy for inducing structural modifications to improve the activity of peptide.