%0 Journal Article
%T Improving myofibrillar proteins solubility and thermostability in low-ionic strength solution: A review.
%A Wang K
%A Li Y
%A Zhang Y
%A Luo X
%A Sun J
%J Meat Sci
%V 189
%N 0
%D Jul 2022 6
%M 35413661
%F 7.077
%R 10.1016/j.meatsci.2022.108822
%X 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.