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 degrees 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 alpha-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.

Automated summary

This study investigated the effect of glycation on the solubility of myofibrillar proteins (MPs) in water. The results showed that MPs conjugated with dextran exhibited higher solubility and stability in water compared to other glycation products. The analysis suggested that the solubilization of MPs may be attributed to the changes in their secondary and tertiary structures.