Abstract：
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.
摘要：
肌原纤维蛋白(MPs)水溶性差限制了其在食品工业中的应用,并且与肌球蛋白组装成细丝相关的分子行为直接相关。本研究旨在探讨高强度超声(HIU)联合非酶糖基化对其溶解度的影响,结构特征，和MPs在低离子强度介质中的长丝形成行为。结果表明，HIU（200-400W）施用可以促进MPs与葡聚糖（DX）之间的糖基化反应，并干扰肌球蛋白棒之间的静电平衡，抑制丝状肌球蛋白聚合物的形成。经400WHIU预处理的糖化MPs具有最高的溶解度，对应于最小的颗粒大小，最高的zeta电位,最佳储存稳定性(P<0.05)。结构分析和微观形态观察表明，MP超螺旋的损失和丝状聚合物的解聚是MP增溶的主要机制。总之,HIU联合糖基化可通过破坏或抑制肌球蛋白分子的组装，有效提高MPs的水溶性。
