Complexation of rice proteins and whey protein isolates by structural interactions to prepare soluble protein composites
Complexation of rice proteins and whey protein isolates by structural interactions to prepare soluble protein composites
复制标题
通过结构相互作用络合大米蛋白和乳清分离蛋白以制备可溶性蛋白复合物
DOI：
10.1016/j.lwt.2018.11.006
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发表时间：
2019-03
期刊：
影响因子：
--
通讯作者：
Tao Wang
中科院分区：
文献类型：
--
作者：
Ren Wang;Pengcheng Xu;Zhengxing Chen;Xing Zhou;Tao Wang
制约高附加值大米蛋白制备的主要因素是其溶解度低。本实验将具有较高营养价值的乳清分离蛋白（whey protein isolation, wpi）与rp在pH为12的条件下复配，并中和至pH为7 （pH-cycle）形成RP-WPI复合物。用荧光光谱和紫外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在颗粒球中的融合。同时，配合物获得了相当大的表面电荷，抵抗蛋白体聚集，rp的溶解度提高到50%以上。本研究中使用的ph循环蛋白相互作用的有效性表明，该技术可能是改善食品蛋白质功能特性的一种通用方法。
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.
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影响因子：
2.9
作者：
R. Yadav;B. S. Khatkar;B. S. Yadav
通讯作者：
R. Yadav;B. S. Khatkar;B. S. Yadav
影响因子：
3.7
作者：
Hawe, Andrea;Sutter, Marc;Jiskoot, Wim
通讯作者：
Jiskoot, Wim
影响因子：
8.8
作者：
Tao Wang;M. Yue;P. Xu;Ren Wang;Zhengxing Chen
通讯作者：
Tao Wang;M. Yue;P. Xu;Ren Wang;Zhengxing Chen
影响因子：
6.1
作者：
Chen, Lin;Chen, Jianshe;Zhao, Mouming
通讯作者：
Zhao, Mouming
影响因子：
2
作者：
Lamsal, B. P.;Reitmeier, C.;Johnson, L. A.
通讯作者：
Johnson, L. A.