Effect of heat sterilization on peptide release and anti-arteriosclerosis value of braised chicken after in vitro digestion

This study aimed to clarify effects of heat sterilization temperatures on the release of peptides and nutritional value of braised chicken after digestion. Braised chicken was sterilized at 121 ℃ (HS), 100 ℃ (MS), and 80 ℃ (LS) for 30 min before in vitro digestion. The release of peptides was assessed by UPLC-LTQ-Orbitrap-MS, while functional differences were analyzed by network pharmacology combined with molecular dynamics simulations. A total of 918 peptides were identified and 53 peptides were significantly reduced in LS, MS, and HS groups compared with the control group. The 373 potential targets of these peptides were uncovered, 106 of which were highly associated with arteriosclerosis. In protein-protein-interaction network, SRC, IL1B, MMP9, CD4 and CASP3 were key targets. GO and KEGG enrichment analysis documented that function involved in modulation were G protein-coupled peptide receptor activity, external side of plasma membrane, extracellular matrix disassembly, and neuroactive ligand-receptor interaction. Molecular docking and molecular dynamics simulations suggested that the interaction between peptides and associated targets depended upon hydrogen bonds and hydrophobic interactions. ALESPERPFLAILGGAK, RTKYETDAIQ, VNDAFGTAH, DAEDIVNTPKPDER and EDFGGHHPDPN exhibited the strongest binding ability with SRC, IL1B, MMP9, CD4 and CASP3, respectively. These results suggest that elevated sterilization temperatures result in decreased peptide release, which may diminish the nutritional value of braised chicken, particularly in relation to arteriosclerosis. These findings suggested insights for optimizing sterilization processes to preserve bioactive peptides in meat products.