Molecular Mechanism of ε-Polylysine Treatment of Animal-Derived Foods: Glycine Amidinotransferase Activity Implicates Upregulation of l-Arginine and Creatine

ε-Polylysine is a novel food preservative approved by the U.S. Food and Drug Administration (FDA), yet the mechanism of its effect on animal-derived foods remains unclear. Assessment of the effect of preservatives on goat meat products is necessary. Herein, metabolite accumulation and protein expression of ε-polylysine (0.025%, w/w) spiked with goat meat were investigated by nontarget metabolomics and proteomics combined with ultrahigh performance liquid chromatography quadrupole-Orbitrap high-resolution-mass spectrometry (UHPLC-Q-Orbitrap HRMS) in a simulated in vitro digestion model. The amino side chain of ε-polylysine increased the activity of glycine aminotransferase due to its nucleophilic nature, inducing a significant upregulation of l-arginine (0.43–0.72 mg kg–1) and creatine (3.98–6.89 mg kg–1), with an improvement in muscle quality of goat meat. Downregulation of enzyme phenylalanine hydroxylase expression led to upregulation of l-phenylalanine (2.26–3.25 mg kg–1) and l-tyrosine (0.98–1.29 mg kg–1). Collectively, this study first revealed the biochemical mechanism of ε-polylysine in goat meat products, which makes available new prospects for more accurate use of ε-polylysine in animal-derived foods.