Food Chem 2025 Jun 24;492Pt 1:145327. doi: 10.1016/j.foodchem.2025.145327.

Natural glycosylation modulates the digestive fate of a marine glycoprotein: Insights from sea cucumber major yolk protein.

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Glycosylation has been shown to influence protein degradation by modifying conformation and cleavage site accessibility. This study investigated the effects of glycosylation type on the structural and digestive degradation properties of major yolk protein (MYP), a natural glycoprotein in sea cucumbers. Enzymatic deglycosylation disrupted the α-helical structure, inducing a conformational shift towards β-sheet and unordered coil structures. Digestion analysis demonstrated that glycan removal significantly enhanced proteolysis, reducing the molecular weight of gastric-digested fragments from 4230 Da to less than 1500 Da. Additionally, intestinal digestion led to an increased abundance of small peptides, with amino acid sequence coverage reaching 64%. These findings confirmed that glycosylation conferred resistance to enzymatic degradation, thereby modulating the digestion profile of MYP. Overall, this study underscores the critical role of glycosylation in regulating the digestive fate of natural glycoproteins, providing a theoretical foundation for understanding the structure-function relationship of glycoproteins.

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