College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.
University of California, Irvine, Irvine, CA 92697, United States.
Food Res Int. 2022 Jul;157:111326. doi: 10.1016/j.foodres.2022.111326. Epub 2022 May 23.
In this work, the interfacial rheological properties and the quantitative changes of proteins at interfacial protein layers of emulsions stabilized by soy protein isolates (SPI) and heat-treated soy protein isolates (HSPI) were investigated. The quantification results showed that the relative quantities of albumin (2S) and glycinin (11S) in SPI decreased at the oil-water interface, suggesting that they possessed lower interfacial affinities at the interface. Basic 7S globulin presented more adsorption at the oil-water interface due to the well balance of the hydrophobic and hydrophilic groups of its amino acid sequence. The HSPI (95 °C, 20 min) showed a larger apparent diffusion rate (K) and a shorter equilibrium adsorption time. The results of interfacial rheology of globulins were consistent with their interfacial quantitative changes, which demonstrated that the interfacial behavior and adsorption ability of globulin were improved by thermal treatment. In this research, the interfacial behaviors of SPI and HSPI was illustrated by their interfacial properties and quantitative results of interfacial adsorbed protein layers, would promote a profound comprehension for the interfacial behavior of the protein and the influence of thermal treatment on protein interfacial properties.
本工作研究了大豆分离蛋白（SPI）和热处理大豆分离蛋白（HSPI）稳定乳液的界面流变特性和界面蛋白层中蛋白质的定量变化。定量结果表明，SPI 中白蛋白（2S）和球蛋白（11S）的相对数量在油水界面处减少，表明它们在界面处的界面亲和力较低。由于其氨基酸序列中疏水和亲水基团的良好平衡，碱性 7S 球蛋白在油水界面上呈现出更多的吸附。HSPI（95°C，20min）表现出更大的表观扩散速率（K）和更短的平衡吸附时间。球蛋白的界面流变学结果与其界面定量变化一致，表明球蛋白的界面行为和吸附能力通过热处理得到了改善。在这项研究中，通过界面吸附蛋白层的界面性质和定量结果说明了 SPI 和 HSPI 的界面行为，这将促进对蛋白质界面行为和热处理对蛋白质界面性质影响的深入理解。
