College of Life Science, Yangtze University, Jingzhou 434025, Hubei, P. R. China.
Institute of Food Sciences and Technology, National Taiwan University, Taipei 10617, Republic of China.
J Agric Food Chem. 2023 Jul 19;71(28):10718-10728. doi: 10.1021/acs.jafc.3c01991. Epub 2023 Jul 6.
The interaction mechanism between nanoliposomes (NL) and a soybean protein isolate (SPI) was investigated via the complexation between NL and two major components of SPI, i.e., β-conglycinin (7S) and glycinin (11S). The endogenous fluorescence emissions of 7S and 11S were statically quenched after complexation with NL, and the polarity of the SPI fluorophore increased. The interaction between NL and SPI was exothermic and spontaneous, 7S/11S secondary structures were altered, and more hydrophobic groups were exposed on protein surfaces. Moreover, the NL-SPI complex had a large zeta potential to attain system stability. Hydrophobic forces and hydrogen bonds played vital roles in the interaction between NL and 7S/11S, and a salt bridge was also involved in the NL-11S interaction. The binding characteristics between NL and 7S/11S were chiefly governed by the protein characteristics, such as amino acid composition, surface hydrophobicity, and advanced structure. These findings could deepen the understanding of the interaction mechanism between NL and SPI.
通过考察纳米脂质体（NL）与大豆分离蛋白（SPI）两种主要成分——β-伴球蛋白（7S）和大豆球蛋白（11S）之间的相互作用，研究了 NL 与 SPI 的相互作用机制。7S 和 11S 的内源荧光发射在与 NL 结合后被静态猝灭，并且 SPI 荧光团的极性增加。NL 与 SPI 之间的相互作用是放热和自发的，7S/11S 二级结构发生改变，蛋白质表面更多的疏水性基团暴露出来。此外，NL-SPI 复合物具有较大的 ζ 电位以达到系统稳定性。疏水力和氢键在 NL 与 7S/11S 之间的相互作用中起着重要作用，盐桥也参与了 NL-11S 相互作用。NL 与 7S/11S 之间的结合特性主要由蛋白质特性决定，如氨基酸组成、表面疏水性和高级结构。这些发现可以加深对 NL 与 SPI 相互作用机制的理解。
