Plants offer a vast variety of protein extracts, typically containing multiple species of proteins that can serve as building blocks of soft materials, like emulsions. However, the role of each protein species concerning the formation of emulsions and interfaces with diverse rheological properties is still unknown. Therefore, deciphering the role of the individual proteins in an extract is highly relevant, since it determines the optimal level of purification, and hence the sustainability aspects of the extract. Here, we will show that when oil/water emulsions were prepared with a rapeseed protein extract containing napins and cruciferins (in a mass ratio of 1:1), only napins adsorbed at the interface exhibiting a soft solid-like rheological behavior. The dominance of napins at the interface was ascribed to their small size (radius r = 1.7 nm) and its unique Janus-like structure, as 45% of the amino acids are hydrophobic and primarily located at one side of the protein. Cruciferins with a bigger size (r = 4.4 nm) and a more homogeneous distribution of the hydrophobic domains couldn’t reach the interface, but they appear to just weakly interact with the adsorbed layer of napins.

植物提供了各种各样的蛋白质提取物，通常包含多种蛋白质，这些蛋白质可以作为柔软材料（如乳液）的组成部分。但是，每种蛋白质种类在具有不同流变特性的乳液和界面形成方面的作用仍是未知的。因此，解密单个蛋白质在提取物中的作用非常重要，因为它决定了纯化的最佳水平，因此决定了提取物的可持续性。在这里，我们将显示，当使用含有萘酚和十字花青素（质量比为1：1）的菜籽蛋白提取物制备油/水乳液时，只有吸附在界面上的萘酚表现出类似软固体的流变行为。napin在界面上的优势归因于它们的小尺寸（半径r = 1。7 nm）及其独特的Janus样结构，因为45％的氨基酸是疏水性的，并且主要位于蛋白质的一侧。较大尺寸（r = 4.4 nm）且疏水结构域分布更均匀的十字花科素无法到达界面，但它们似乎与萘酚的吸附层之间存在弱相互作用。