The main factor limiting the preparation of high value-added rice proteins (RPs) is their low solubility. In this experiment, whey protein isolates (WPIs), which are of high nutritional value, were compounded with RPs at pH 12, and formed RP-WPI complexes by neutralization to pH 7 (pH-cycle). The formation of the protein complexes was studied by fluorescence and ultraviolet (UV) spectra. The results showed that hydrogen bond, hydrophobic force and electrostatic interaction mediated the merging of the two proteins into particulate spheres. Meanwhile the complexes acquired considerable surface charges resisting aggregation of the protein bodies, and the solubility of RPs was increased to more than 50%. The effectiveness of protein interactions by pH-cycle used in this study indicated that the technique may be a versatile approach to improve the functional properties of food proteins.

限制高附加值大米蛋白（RPs）制备的主要因素是它们的低溶解度。在该实验中，将营养价值高的乳清蛋白分离物（WPI）与RP在pH值为12时复合，并通过中和至pH 7（pH循环）形成RP-WPI复合物。通过荧光和紫外（UV）光谱研究了蛋白质复合物的形成。结果表明，氢键，疏水力和静电相互作用介导了两种蛋白质融合成颗粒球。同时，该复合物获得了可抵抗蛋白体聚集的大量表面电荷，并且RPs的溶解度增加到超过50％。