Effects of Maillard glycosylation with different saccharides on structural, antioxidant and functional properties of porcine myosin.

Abstract

Myosin is a crucial protein that contributes to the processing performance of meat products. This study investigated the effects of Maillard glycosylation with glucose, sucrose, and β-glucan on the structural, antioxidant, and functional properties of porcine myosin. During 0-8 h of reaction, the glycosylation degree, browning intensity, and reactive dicarbonyl compounds (GO and MGO) increased progressively, with glucose generally showing the highest reactivity. Glycosylation induced changes in conformational characteristics, characterized by decreased α-helix content and increased β-sheet and random coil proportions, which were associated with reduced surface hydrophobicity and enhanced solubility recovery. UV-Vis spectroscopy showed enhanced absorbance at 280 nm with a redshift, indicating exposure of aromatic residues. Glucose conjugates generally exhibited stronger antioxidant activity, whereas β-glucan modification resulted in superior emulsion and foam stability. Molecular docking suggested potential non-covalent interactions between saccharides and myosin through hydrogen bonds and van der Waals forces. Overall, differences in saccharide molecular structure and steric characteristics were associated with glycosylation efficiency and functional properties, providing complementary mechanistic insights into myosin modification.