Protein-stabilized interfaces in multiphase food: comparing structure-function relations of plant-based and animal-based proteins

• Animal-based globular proteins form stiff viscoelastic solid layers at interfaces. • Plant protein-based layers appear to be less stiff and more ductile. • Differences in protein conformation at the interface appear responsible for this. • Synchrotron radiation techniques are ideal to study the link microstructure-rheology. • Insights into this relation allow to find optimal modification routes for plant proteins. Proteins are an important category of stabilizers for multiphase food systems such as foams and emulsions. In recent years, a growing interest can be observed in replacing animal-based by plant-based proteins to stabilize such products. Often, these plant-based proteins have inferior functionality compared to animal-based proteins. In this review, we will discuss recent insights into possible reasons for the differences in behavior between animal-based and plant-based proteins, and present an overview of strategies to improve the performance of plant-based extracts. Improving plant-protein functionality may ultimately allow us to engineer interfaces with properties tailored to specific applications.