The aggregation of proteins is of fundamental relevance in a number of daily phenomena, as important and diverse as blood coagulation, medical diseases, or cooking an egg in the kitchen. Colloidal food systems, in particular, are examples that have great significance for protein aggregation, not only for their importance and implications, which touches on everyday life, but also because they allow the limits of the colloidal science analogy to be tested in a much broader window of conditions, such as pH, ionic strength, concentration and temperature. Thus, studying the aggregation and self-assembly of proteins in foods challenges our understanding of these complex systems from both the molecular and statistical physics perspectives. Last but not least, food offers a unique playground to study the aggregation of proteins in three, two and one dimensions, that is to say, in the bulk, at air/water and oil/water interfaces and in protein fibrillation phenomena. In this review we will tackle this very ambitious task in order to discuss the current understanding of protein aggregation in the framework of foods, which is possibly one of the broadest contexts, yet is of tremendous daily relevance.

An interfacial rheometer for both stress- and strain-controlled measurements of shear rheological properties at liquid/liquid and gas/liquid interfaces is presented. The device is based on a rotating or oscillating biconical bob design in combination with a low friction electronically commutated motor system. The interfacial shear stress, viscosity, and dynamic moduli are obtained by solving the Stokes equations (low Reynolds number) along with the Boussinesq–Scriven interfacial stress tensor, which is used for the boundary conditions at the interface. An improved and simple numerical method for the calculation of the velocity distribution in the measuring cell is presented. The scope and limitations of the rheometer are discussed. Results from steady shear and oscillatory experiments as well as creep recovery and stress relaxation tests at both oil/water and air/water interfaces with adsorbed films of a globular protein (ovalbumin) and spread films of a surfactant (sorbitan tristearate) are presented.