Improving the solubility of myofibrillar proteins in water by destroying and suppressing myosin molecular assembly via glycation.

Filamentous myosin is a self-assembling polymer that prevents myofibrillar proteins (MPs) from functioning in low ionic strength media. This study was aimed at investigating if glycation has the potential to improve the solubility of MPs in water. MPs were conjugated with monosaccharides, oligosaccharides, and polysaccharides under wet reaction conditions at 37 °C. The conjugation was verified by SDS-PAGE, FT-IR and amino acid analyses. MPs conjugated with dextran (DX) exhibited a higher solubility and dispersion stability in water, which corresponded to smaller particle size and more uniform distribution (P < 0.05). According to secondary and tertiary structure analyses, the loss of α-helix structures and unfolding of the MPs appear to be the main reasons for MP solubilization. Additionally, according to the zeta-potential, confocal laser scanning microscopy, and atomic force microscopy observation results, glycation can provide electrostatic repulsion or steric hindrance to disintegrate existing filamentous myosin aggregates and inhibit further self-assembly behavior.