This study aimed to prepare collagen glycopeptides by
transglutaminase-induced
glycosylation and to explore their salt taste-enhancing effects and
mechanism. Collagen glycopeptides were obtained by Flavourzyme-catalyzed
hydrolysis, followed by transglutaminase-induced glycosylation. The
salt taste-enhancing effects of collagen glycopeptides were evaluated
by sensory evaluation and an electronic tongue. LC–MS/MS and
molecular docking technologies were employed to investigate the underlying
mechanism responsible for the salt taste-enhancing effect. The optimal
conditions were 5 h for enzymatic hydrolysis, 3 h for enzymatic glycosylation,
and 1.0% (E/S, w/w) for transglutaminase. The grafting degree of collagen
glycopeptides was 26.9 mg/g, and the salt taste-enhancing rate was
59.0%. LC–MS/MS analysis revealed that Gln was the glycosylation
modification site. Molecular docking confirmed that collagen glycopeptides
can bind to salt taste receptors epithelial sodium channel protein
and transient receptor potential vanilloid 1 through hydrogen bonds
and hydrophobic interaction. Overall, collagen glycopeptides have
a significant salt taste-enhancing effect, which contributes to the
application of collagen glycopeptides for salt reduction without compromising
taste in the food industry.
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