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The primary proteins in egg whites are glycoproteins, which are hydrolyzed by digestive enzymes to produce substantial egg white glycopeptides (EWGs). However, the potential role of EWG has not been reported. In this study, EWG was obtained through simulated digestion in vitro and affinity chromatography enrichment, and we further examined the effect of EWG on protein expression in mouse macrophages (RAW264.7) through quantitative proteomic analysis. Compared to the control group, 149 differentially expressed proteins (DEPs) were upregulated, and 35 DEPs were downregulated in RAW264.7 cells by treatment with EWG (125 µg/mL). These DEPs were related to 76 KEGG pathways (such as "NF-kappa B signaling pathway", "TNF signaling pathway", "C-type lectin receptor signaling pathway") and 12 protein domains (such as "Lectin C-type domain", "Immunoglobulin domain", "Immunoglobulin V-set domain"), which suggested that EWG could exert immunomodulatory effects through immune signaling pathways and protein domains. Our findings provide promising signaling pathways for in-depth exploration of the immunomodulation of EWG and contribute to the development of EWG as a potential immunoactivity ingredient.
He et al. (Thu,) studied this question.