Alteration of the structure of rice proteins by their interaction with soy protein isolates to design novel protein composites.
Alteration of the structure of rice proteins by their interaction with soy protein isolates to design novel protein composites.
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DOI：
10.1039/c8fo00661j
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发表时间：
2018-08
期刊：
影响因子：
6.1
通讯作者：
Tao Wang;P. Xu;Zhengxing Chen;Xing Zhou;Ren Wang
中科院分区：
文献类型：
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作者：
Tao Wang;P. Xu;Zhengxing Chen;Xing Zhou;Ren Wang
大米蛋白（RPs）是具有高营养价值的植物蛋白，但由于其溶解性差（30 mV），因此很少引起工业兴趣。由于其增强的溶解性和保留的疏水性，蛋白质复合材料显示出优异的界面亲和力。蛋白质复合物的乳化和起泡能力和稳定性在pH 7下几乎是RP的两倍甚至三倍。此外，蛋白质复合物保持了RP和SPI的平衡氨基酸组成。我们的研究结果表明，通过调节pH值诱导蛋白质相互作用是食品蛋白质功能和营养修饰的一种稳健技术。
Rice proteins (RPs) are plant proteins with high nutritional value, but they attract little industrial interest because they are poorly soluble (30 mV). With their enhanced solubility and retained hydrophobicity, the protein composites displayed excellent interfacial affinities. The emulsifying and foaming capacities and stabilities of the protein composites were almost doubled or even tripled at pH 7 relative to those of RPs. Furthermore, the protein composites maintained the balanced amino acid compositions of both the RPs and SPIs. Our results demonstrate that inducing protein interactions by modulating the pH is a robust technique for the functional and nutritional modification of food proteins.