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.