Abstract：
The development of myofibrillar proteins drinks (MPDs) can provide meat protein nutrition to specific groups of people. However, one major challenge is that myofibrillar proteins (MPs) are insoluble in solutions with a low ionic strength. Another functional constraint is the susceptibility of MPs to heat-induced aggregation. Currently, the primary approach used to improve the water solubility of MPs is to inhibit the assembly of myofilaments. Increasing the thermostability of MPs primarily inhibits the aggregation of myosin or oxidizes myosin to soluble substances. This review focuses on the description of several chemical and physical strategies, with an emphasis on the advantages, disadvantages, and recent progress. Under the myosin filament assembly process and the cross-linking aggregation mechanism, this summary helps improve our understanding of the solution and thermostability of MPs in low-ionic-strength solutions, thus providing new ideas to the development of MPDs.
摘要：
肌原纤维蛋白饮料（MPD）的开发可以为特定人群提供肉类蛋白质营养。然而,一个主要的挑战是肌原纤维蛋白（MPs）在低离子强度的溶液中是不可溶的。另一个功能约束是MP对热诱导的聚集的敏感性。目前,提高MPs水溶性的主要方法是抑制肌丝的组装。增加MPs的热稳定性主要抑制肌球蛋白的聚集或将肌球蛋白氧化为可溶性物质。这篇综述侧重于描述几种化学和物理策略，强调优势，缺点,和最近的进展。在肌球蛋白丝组装过程和交联聚集机制下,本总结有助于提高我们对低离子强度溶液中MP的溶液和热稳定性的理解，从而为MPD的发展提供新的思路。
