Physicochemical options to augment the functionality of plant proteins for food applications

Use of plant proteins in food formulations is key to drive the reduction of the carbon footprint from the global food system. Most protein sources are derived from crops used to produce non-protein ingredients such as oils or starches. Applying more gentle extraction methods enables preserving the functionality potential of the plant proteins, but this lecture will show additional examples where physicochemical processes can augment protein initial functionality.

Firstly, the use of high-pressure homogenization will be described for improving the solubility and foaming properties of commercial pea protein isolate. The shear induced by the process enables to break interactions occurring in protein powder, leading to free and aggregated pea protein fractions. In addition, we will show that a controlled heat aggregation induced by calcium addition can generate protein aggregates able to reduce drainage in aqueous foams.

Then, the formation of electrostatic complexes and coacervates between pea protein isolate and pectins will be considered at various pH and mixing ratios, enabling production of concentrated biopolymer dispersions with remarkable rheological and binding properties which can be used in meat analogues.

Finally, the formation of fibrous soy protein wet extrudates will be discussed, with special emphasis on triggering the microstructure and texture of the extrudate by proper selection of the protein concentrates based on their solubility and water binding properties.

All these examples will demonstrate the ability of plant protein ingredients to be widely used in complex food products when their functionality is wisely controlled.