热稳定性
肌球蛋白
肌原纤维
溶解度
离子强度
化学
离子键合
蛋白质聚集
肌丝
生物化学
离子
酶
有机化学
水溶液
作者
Ke Wang,Yan Li,Yimin Zhang,Xin Luo,Jingxin Sun
出处
期刊:Meat Science
[Elsevier]
日期:2022-07-01
卷期号:189: 108822-108822
被引量:25
标识
DOI:10.1016/j.meatsci.2022.108822
摘要
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.
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