Design of novel edible hydrocolloids by structural interplays between wheat gluten proteins and soy protein isolates
Design of novel edible hydrocolloids by structural interplays between wheat gluten proteins and soy protein isolates
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通过小麦麸质蛋白和大豆分离蛋白之间的结构相互作用设计新型可食用亲水胶体
DOI：
10.1016/j.foodhyd.2019.105395
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发表时间：
2020-03-01
影响因子：
10.7
通讯作者：
Wang, Tao
中科院分区：
文献类型：
--
作者：
He, Jian;Wang, Ren;Wang, Tao
小麦面筋蛋白（WPs）是一种高产的营养蛋白，但由于其水溶性较差，在工业上很少有吸引力。在pH为12的条件下，以WP/SPI （W/S）为1:0.1 ~ 1:2共溶WPs和大豆分离蛋白（SPI）为pH循环，将WPs的水溶性从4.5%提高到72.4%，同时保持蛋白一级结构的完整。形态学分析、荧光和远紫外光谱分析表明，WPs在中和过程中通过蛋白共折叠与SPIs相互作用形成组合颗粒结构。由于未折叠的蛋白质骨架具有较高的结构强度，因此组合结构具有明显的抗复性。更带电的表面提供了复杂的蛋白质与水分子更大的亲和力，并保护蛋白质分子不聚集。此外，氨基酸组成基本满足成人对氨基酸的需求。结果表明，通过调节pH诱导蛋白质络合可能是一种简便易行的将不溶性蛋白质修饰成可食用的水胶体的方法，在提高蛋白质营养价值方面具有很大的潜力。
Wheat gluten proteins (WPs) are nutritious protein with a large yield, but they are rarely industrially attractive due to their poor water solubility. In this experiment, a pH-cycle was used by co-dissolving WPs and soy protein isolates (SPIs) with WP/SPI ratios (W/S) from 1:0.1 to 1:2 at pH 12, and further readjusting the pH to neutral, which improved the water solubility of WPs from 4.5% to 72.4% while maintaining the intact primary structure of proteins. The morphological analysis, fluorescence and far-UV spectra illustrated that the WPs interacted with SPIs to form combined particulate architectures by the co-folding of proteins during neutralization. The combined structures are significantly resistant to renaturation due to the unfolded protein backbones with high structural tenacity. The more charged surface provided complexed proteins with greater affinity to water molecules and protected the protein molecules from aggregation. Moreover, the amino acid compositions closely met the amino acid requirements for adults. The results indicate that the protein complexation induced by adjusting the pH may be a facile and applicative approach to modify insoluble proteins into edible hydrocolloids, and has great potential for enhancing nutritional values of proteins.