Toward water-solvation of rice proteins via backbone hybridization by casein.
Toward water-solvation of rice proteins via backbone hybridization by casein.
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DOI：
10.1016/j.foodchem.2018.03.084
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发表时间：
2018-08
期刊：
影响因子：
8.8
通讯作者：
Tao Wang;M. Yue;P. Xu;Ren Wang;Zhengxing Chen
中科院分区：
文献类型：
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作者：
Tao Wang;M. Yue;P. Xu;Ren Wang;Zhengxing Chen
水不溶性是制约大米蛋白、玉米醇溶蛋白等食品蛋白商品化的主要瓶颈之一。本文报道了大米蛋白与酪蛋白按1：0.01的质量比进行结构杂交，可将大米蛋白的溶解度提高到90%以上。结构分析表明，RPS和酪蛋白的骨架在碱性溶液(pH 12.0)中整合在一起，折叠在一起形成更高的结构，随后被中和。得到的杂交骨架提高了分子在中和过程中对结构变化的抵抗力，并形成了具有明显暴露的极性基团的蛋白质小体，这些蛋白质小体可能在没有酪蛋白的情况下被掩埋。形态观察证实，形成了定义明确的纳米颗粒，没有明显的聚集。这两种蛋白质还保留了它们完整的初级多肽链，从而显著保护了动植物衍生品的原始性质。
Water insolubility is one of the major bottlenecks restricting the commercial availability of such food proteins as rice proteins (RPs), zein,etc. Here, we report that the structural hybridization of RPs and casein in a mass ratio of 1:0.01 can boost the solubility of RPs to over 90%. A structural analysis demonstrated that the backbones of the RPs and casein were integrated in basic solution (pH 12.0) and folded together into higher structures with subsequent neutralization. The hybrid backbones obtained improved the molecules’ resistance to structural changes during neutralization, and formed protein bodies with appreciable exposed polar groups, which may have been buried in the absence of casein. Morphological observations confirmed the formation of well-defined nanoscale particles with no visible aggregation. Both proteins also retained their intact primary peptide chains, thus significantly protecting the original nature of the plant and animal derivatives.