Improved water solubility of myofibrillar proteins by ultrasound combined with glycation: A study of myosin molecular behavior

[Display omitted] •Ultrasound pretreatment promoted the subsequent glycation reaction.•Conjugates pretreated by 400 W ultrasound exhibited optimal water solubility.•The increased net charge induced dissociation of myofibrillar proteins (MPs).•The ultrasound–glycation combination inhibited filament formation in low-salt media. The poor water solubility of myofibrillar proteins (MPs) limits their application in food industry, and is directly related to the molecular behavior associated with myosin assembly into filaments. This study aims to explore the effect of high-intensity ultrasound (HIU) combined with nonenzymatic glycation on the solubility, structural characteristics, and filament-forming behavior of MPs in low ionic strength media. The results showed that the HIU (200–400 W) application could promote the subsequent glycation reaction between MPs and dextran (DX) and interfere with the electrostatic balance between myosin rods, suppressing the formation of filamentous myosin polymers. Glycated MPs pretreated by 400 W HIU had the highest solubility, which corresponded to the smallest particle size, highest zeta potential, and optimum storage stability (P