Huang Xin, Xia Boxue, Liu Yaxuan, Wang Cuina
Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China.
Food Chem X. 2024 May 14;22:101459. doi: 10.1016/j.fochx.2024.101459. eCollection 2024 Jun 30.
Rice protein (RP) and polyphenols are often used in functional foods. This study investigated the non-covalent interactions between RP and three polyphenols (curcumin, CUR; quercetin, QUE; resveratrol, RES) and used the complexes as emulsifiers to create emulsions. Three polyphenols interacted with RP to varying extents, with QUE showing the greatest binding affinity and inducing the greatest alterations in its secondary structure. Molecular docking analysis elucidated the driving forces between them including hydrophobic interactions, hydrogen bonding, and van der Waals forces. Combination with QUE or RES induced structural changes of RP, increasing particle size of complexes. The synergistic effect of polyphenols and protein also enhanced radical scavenging capacity of complexes. Compared to pure protein, all complexes successfully created emulsions with smaller particle size (378-395 nm vs. 470 nm), higher absolute potential (37.43-38.26 mV vs. 35.62 mV), and greater lipid oxidation stability by altering protein conformation.
大米蛋白（RP）和多酚常用于功能性食品中。本研究调查了RP与三种多酚（姜黄素，CUR；槲皮素，QUE；白藜芦醇，RES）之间的非共价相互作用，并将形成的复合物用作乳化剂来制备乳液。三种多酚与RP的相互作用程度各不相同，其中QUE表现出最大的结合亲和力，并导致其二级结构发生最大变化。分子对接分析阐明了它们之间的驱动力，包括疏水相互作用、氢键和范德华力。与QUE或RES结合会引起RP的结构变化，增加复合物的粒径。多酚和蛋白质的协同作用还增强了复合物的自由基清除能力。与纯蛋白相比，所有复合物均成功制备出粒径更小（378 - 395 nm对470 nm）、绝对电位更高（37.43 - 38.26 mV对35.62 mV）且通过改变蛋白质构象具有更高脂质氧化稳定性的乳液。
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