Chen Nannan, Zhao Ziliang, Wang Yong, Dimova Rumiana
Guangdong Saskatchewan Oilseed Joint Laboratory, Department of Food Science and Engineering, Jinan University, 510632 Guangzhou, China.
Max Planck Institute of Colloids and Interfaces, Department of Theory and Bio-Systems, Science Park Golm, 14424 Potsdam, Germany.
ACS Macro Lett. 2020 Dec 15;9(12):1844-1852. doi: 10.1021/acsmacrolett.0c00709. Epub 2020 Dec 6.
Self-coacervation of animal-derived proteins has been extensively investigated while that of plant proteins remains largely unexplored. Here, we study the process of soy glycinin self-coacervation and transformation into hollow condensates. The protein hexameric structure composed of hydrophilic and hydrophobic polypeptides is crucial for coacervation. The process is driven by charge screening of the intrinsically disordered region of acidic polypeptides, allowing for weak hydrophobic interactions between exposed hydrophobic polypeptides. We find that the coacervate surface exhibits order, which stabilizes the coacervate shape during hollow-condensate formation. The latter process occurs via nucleation and growth of protein-poor phase in the coacervate interior, during which another ordered layer at the inner surface is formed. Aging enhances the stability of both coacervates and hollow condensates. Understanding plant protein coacervation holds promises for fabricating novel functional materials.
动物源蛋白质的自凝聚现象已得到广泛研究，而植物蛋白的自凝聚现象在很大程度上仍未被探索。在此，我们研究了大豆球蛋白的自凝聚过程以及向中空凝聚物的转变。由亲水性和疏水性多肽组成的蛋白质六聚体结构对凝聚至关重要。该过程由酸性多肽内在无序区域的电荷筛选驱动，使得暴露的疏水性多肽之间能够发生弱疏水相互作用。我们发现凝聚物表面呈现出有序性，这在中空凝聚物形成过程中稳定了凝聚物的形状。后一过程通过凝聚物内部贫蛋白相的成核和生长发生，在此期间内表面形成了另一层有序层。老化增强了凝聚物和中空凝聚物的稳定性。了解植物蛋白凝聚有望制造新型功能材料。
