Unravelling the potential of food protein fibrils: their extraction, engineering and functionality

Altering the structure of proteins impacts their functionality. Amyloid fibrils (AFs) are compact and rigid protein structures which are much studied in the context of diseases such as Alzheimer. Under specific conditions, different food proteins can form AFs. Their presence in daily-consumed food products and structure-function relationship in food remains unknown. This project will extract and characterize AFs from boiled hen egg white. The potential of cereal proteins to form AFs will be investigated. Protein sequences with high propensity to form such structures, the amyloid core regions, will be identified for both egg white and cereal proteins. Here, in silico methods will be helpful at predicting and selecting promising proteins and their sequences. The abundance and morphology of egg white and cereal AFs will be steered by changing the conditions (pH, temperature, heating mode,…) and by adding seeds of pre-formed fibrils. In addition to the study of AFs from one protein source, fibrils will be also made in mixed protein systems. The gelling, foaming and emulsifying properties of different food protein fibrils will be tested. Last but not least, I hope to be able to deliver a proof-of-concept that AFs can impact on the quality of a real food product, i.e. egg noodles.