Myofibrillar proteins (MPs) are underutilized because of their weak solubility in low-salt conditions. In this research, mixing MPs with sodium alginate (SA) was studied to improve the solubility of MPs, and the effects of pH, mixing ratios (r), and protein preheating were examined. Mixing with SA improved the solubility of MPs at pH 6.5 and 5.5, and the precipitation of MPs was completely inhibited by an MPs/SA ratio of 20 and 5.0, respectively. The solubility of MPs was not improved by mixing with SA at other pHs. The mixing behavior of MPs and SA was greatly influenced by the electrostatic interaction, depletion interaction, and bridging flocculation. Preheating MPs (70 °C, 30 min) reduced the amounts of SA required to inhibit their precipitation and improved the heat stability of MPs/SA mixtures. These improvements may have resulted from the exposure of embedded negatively charged groups, decrease of particle size in MPs, and disulfide crosslinking after preheating. These findings demonstrate an approachable route to obtain soluble forms of MPs, which may find application in liquid products.

中文翻译：

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通过与海藻酸钠混合改善肌原纤维蛋白（MPs）的溶解度：pH，混合比和MPs预热的影响

肌原纤维蛋白（MPs）由于在低盐条件下的弱溶解性而未被充分利用。在这项研究中，研究了将MP与藻酸钠（SA）混合以提高MP的溶解度，并考察了pH，混合比（r）和蛋白质预热的影响。与SA混合可改善MPs在pH 6.5和5.5时的溶解度，并且MPs / SA比分别为20和5.0完全抑制了MPs的沉淀。通过在其他pH值下与SA混合不能改善MP的溶解度。MPs和SA的混合行为受静电相互作用，耗竭相互作用和桥接絮凝的影响很大。预热MPs（70°C，30分钟）减少了抑制其沉淀所需的SA量，并改善了MPs / SA混合物的热稳定性。这些改善可能是由于嵌入的带负电基团的暴露，MP中粒径的减小以及预热后的二硫键交联所致。这些发现证明了获得可溶形式的MP的可行途径，其可能在液体产品中得到应用。