Protein structures combining designable nutritional and functional properties are attracting great attention in the food industry. In this study, novel protein composites with shared internal structures were fabricated by co-dissolving rice proteins (RPs) and pea proteins (PPs) at pH 12 prior to a one-step neutralization. Structural and morphological characterization revealed that both unfolded protein molecules reacted at pH 12 via their secondary structures, driven by hydrophobic forces. The co-assembled structures therefore obtained considerable resistance against acid-induced refolding, affording the formation of nanoscale (∼100 nm), water-dispersible composites at pH 7. Eventually, the drawbacks of either proteins, such as the insolubility of RPs or slow digestion of PPs, were overcome due to structural alterations. Moreover, the strategy raised the level of Lys which was limiting in RPs in the same way as the level of those that were limiting in PPs such as Met and Cys-s. Based on the above results, the study would enrich the techniques of processing protein ingredients toward tailored structures and on-demand nutritional properties.

中文翻译：

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通过桥接大米蛋白和豌豆蛋白之间的二级结构以增强营养特性来制造亲水性复合材料。

结合了可设计的营养和功能特性的蛋白质结构在食品工业中引起了极大的关注。在这项研究中，在一步中和之前，通过在pH 12下共溶解大米蛋白（RPs）和豌豆蛋白（PPs）来制造具有共享内部结构的新型蛋白复合物。结构和形态特征表明，两个未折叠的蛋白质分子在pH 12下均通过它们的二级结构是由疏水力驱动的。因此，这种共组装结构对酸诱导的复性具有相当大的抵抗力，可在pH 7下形成纳米级（〜100 nm），水分散性复合物。最终，这两种蛋白的缺点，例如RP的不溶性或缓慢PPs的消化，由于结构改变而被克服。而且，该策略提高了RPs中限制Lys的水平，与限制Met和Cys-s中PPs限制的Lys水平相同。基于以上结果，该研究将丰富针对特定结构和按需营养特性加工蛋白质成分的技术。