Evaluation of techno-functional properties of hen egg white and wheat gluten amyloid-like fibrils formed under food-relevant conditions

Amyloid-like fibrils are ordered protein aggregates formed by moderate heating under acidic conditions. In order to implement them in the food industry, more knowledge has been gathered regarding their formation under more food-relevant conditions (i.e. heating at neutral pH and combined heat-enzymatic treatment at neutral pH). As such, ovalbumin fibrils were formed with distinct morphology and each of them showed either good gelling, emulsifying or encapsulating properties. Additionally, more complex food protein sources such as hen egg white and wheat gluten were also evaluated for their fibril formation and subsequent emulsifying properties. Lastly, the impact of several proces conditions (pH, emulsification, ionic strength, shear) has been studied on the formation of (additional) fibrils. This research contributed to the potential replacement of animal proteins by plant proteins or proteins with an improved functionality in several food applications