Huang_2026_Food.Chem.X_36_104027

Oyster peptides exhibit diverse bioactivities but suffer from poor stability and digestive degradation, limiting functional food applications. To overcome these, this study employed transglutaminase (TGase)-catalyzed glycosylation to conjugate glucosamine (GlcN) with an oyster peptide ultrafiltration fraction (UF3), and evaluated the structural, physicochemical, and hypolipidemic properties. Results showed that glycosylation induced a beta-sheet to alpha-helix shift and transformed the microstructure into a smooth, thin-film network. These changes reduced average particle size, lowered surface hydrophobicity, and enhanced solubility and thermal stability. The glycosylated product (GUF3) exhibited improved inhibitory activities against pancreatic lipase and cholesterol esterase. Moreover, GUF3 showed superior gastrointestinal resistance, retaining higher enzyme inhibition after intestinal digestion than UF3. In free fatty acids-induced HepG2 cells, GUF3 more effectively reduced lipid accumulation, total cholesterol, and triglycerides. Collectively, TGase-catalyzed glycosylation improves the structure, digestive stability, and hypolipidemic activity of oyster peptides, supporting GUF3 as a promising ingredient for hyperlipidemia management.