Dynamic Interfacial Architectures: Cruciferin‐Stabilized Oil/Water Interfaces for Sustainable Emulsions

Abstract Stabilizing oil‐water interfaces in emulsions by plant‐based proteins provides sustainable and tunable ways for designing emulsions with specific properties, for food, healthcare, and pharmaceuticals. Cruciferin, a protein from rapeseed, has great potential as green emulsifier, but details about its structure and mobility at oil‐water interfaces are largely unknown. Here, these properties are studied with small angle neutron and x‐ray scattering, and neutron spin echo spectroscopy, analyzed by atomistic modelling of scattering curves and coarse‐grained modelling, to gain insight into interface coverage, and molecular conformation and mobility at the interface. Cruciferin assumes trimeric conformations at the interface, as in solution, but with its protrusions from the central core of the subunits (“arms”) more compressed. Interfacial mobility is only marginally lower than in solution, indicating the arms still transiently extend and preserve a network, for the first time revealing the mechanism how cruciferin forms highly elastic 2d gel‐like oil‐water interfaces, as observed in macroscopic rheology. The high interfacial mobility may help in self‐repairing non‐stabilized interfacial fractions, reducing coalescence. These findings provide a deeper molecular level understanding of proteins at oil‐water interfaces, which can stimulate development of new plant‐based emulsion products, and contribute to the global protein transition.