College of Food Science, Northeast Agricultural University, Harbin 150030, China.
College of Food Engineering, Harbin University of Commerce, Harbin, Heilongjiang 150028, China; Heilongjiang Green Food Science Research Institute, Harbin 150028, China; National Research Center of Soybean Engineering and Technology, Harbin 150028, China.
Food Chem. 2022 Dec 1;396:133685. doi: 10.1016/j.foodchem.2022.133685. Epub 2022 Jul 13.
The purpose of this research was to comparatively investigate the interactions between bioactive flavonoids (quercetin and rutin) and two predominant soy proteins (β-conglycinin and glycinin), and the structural and functional properties of their complexes. The binding affinities of quercetin/rutin toward 7S/11S were structure-dependent, in that rutin had a higher binding affinity than that of quercetin, and 11S exhibited higher affinity toward quercetin/rutin than that of 7S. The interactions in the 7S/11S-quercetin complexes were driven by van der Waals forces and hydrogen-bonding interactions, whereas the 7S/11S-rutin complexes exhibited hydrophobic interactions. Binding to quercetin or rutin altered the secondary structures (decrease in the α-helix and random coil contents and increase in the β-sheet content), decreased the surface hydrophobicity and thermal stability, and enhanced the antioxidant capacity of 7S and 11S. These findings provide valuable information that can facilitate the design of custom-tailored protein-flavonoid macromolecules.
本研究旨在比较研究生物活性黄酮（槲皮素和芦丁）与两种主要大豆蛋白（β-伴球蛋白和大豆球蛋白）之间的相互作用，以及它们复合物的结构和功能特性。槲皮素/芦丁与 7S/11S 的结合亲和力具有结构依赖性，即芦丁的结合亲和力高于槲皮素，并且 11S 对槲皮素/芦丁的亲和力高于 7S。7S/11S-槲皮素复合物中的相互作用是由范德华力和氢键相互作用驱动的，而 7S/11S-芦丁复合物则表现出疏水性相互作用。与槲皮素或芦丁结合会改变二级结构（α-螺旋和无规卷曲含量减少，β-折叠含量增加），降低表面疏水性和热稳定性，并增强 7S 和 11S 的抗氧化能力。这些发现提供了有价值的信息，可以促进定制蛋白-黄酮大分子的设计。
