Studies of the binding mechanism between liquid smoke from tea tree branches and proteins in dry-cured tenderloin...

This research investigates the impact of various concentrations of tea branch liquid smoke (TLS) on the protein structure of dry cured pork tenderloin using multispectral techniques, molecular docking, and 4D-DIA proteomics. The results reveal that TLS enhances the solubility of myofibrillar protein, with varying effects on tryptophan exposure based on the concentration. Notably, at 5 mL/kg, TLS inhibits myofibrillar protein unfolding. Raman spectroscopy demonstrates that higher TLS concentrations mitigate disruptions in hydrogen bonding and hydrophobicity. Guaiacol and furfural in TLS engage in π-stacking interactions with myosin, heightening myosin interaction with its carrier. 4D-DIA proteomics has revealed that TLS can down-regulate the expression of cytoplasmic and mitochondrial proteins, metabolic enzymes, and ligases, playing pivotal roles in metabolism and genetic information processing. These proteins, featuring membrane linkers and phosphatases, potentially impact peptide and amino acid biosynthesis, thereby affecting meat quality modifications.