ArticleFood chemistry: X2026
Site-specific N-glycoproteomics reveals alteration of N-glycan structures and heterogeneity to enhance thermally induced gelation characteristics of egg white proteins.
Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
N-glycans are complex carbohydrates crucial for the structural integrity and functionality of proteins. Here, we present a high-resolution egg white protein N-glycoproteomic atlas that systematically unveils the microheterogeneity across N-glycosites, glycoproteins, and co-occurring N-glycans. Notably, hawthorn leaf flavonoids (HF) markedly reduced undecorated and high-mannose N-glycans while increasing paucimannose and sialylated-only N-glycans, and these changes strongly correlated with elevated protein stability. Site-specific N-glycan comparative analysis further revealed that HF increased 15 N-glycans at four glycoproteins (such as Hex
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