Pea proteins are widely used as a food ingredient, especially in sustainable food formulations. The seed itself consists of many proteins with different structures and properties that determine their structure-forming properties in food matrices, such as emulsions, foams, and gels. This review discusses the current insights into the structuring properties of pea protein mixtures (concentrates, isolates) and the resulting individual fractions (globulins, albumins). The structural molecular features of the proteins found in pea seeds are discussed and based on this information, different structural length scales relevant to foods are reviewed. The main finding of this article is that the different pea proteins are able to form and stabilize structural components found in foods such as air-water and oil-water interfaces, gels, and anisotropic structures. Current research reveals that each individual protein fraction has unique structure-forming properties and that tailored breeding and fractionation processes will be required to optimize these properties. Especially the use of albumins, globulins, and mixed albumin-globulins proved to be useful in specific food structures such as foams, emulsions, and self-coacervation, respectively. These new research findings will transform how pea proteins are processed and being used in novel sustainable food formulations in the future.
Keywords: Alternative protein; coacervate; extrusion; legumin; meat alternative; plant-based; vicilin.