溶解度
化学
糖基化
肌球蛋白
肌原纤维
解聚
生物物理学
色谱法
有机化学
化学工程
生物化学
受体
工程类
生物
作者
Ge Han,Yuexin Li,Qian Liu,Qian Chen,Haotian Liu,Baohua Kong
标识
DOI:10.1016/j.ultsonch.2022.106140
摘要
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 < 0.05). Structure analysis and microscopic morphology observations suggested that the loss of the MP superhelix and the depolymerization of filamentous polymers were the main mechanisms for MP solubilization. In conclusion, HIU combined with glycation can effectively improve the water solubility of MPs by destroying or suppressing the assembly of myosin molecules.
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