Design of techno-functional cereal protein fibrils
Population growth, prosperity increment in developing countries and sustainability issues urge the substitution of animal by plant proteins in the human diet. However, plant proteins often have inferior techno-functional properties. Protein functionality is closely related to protein structure. Under some conditions, partially unfolded proteins self-assemble into highly ordered nanofibers with a β-sheet core stabilized by intermolecular hydrogen bonds. Such fibrillar protein structures, named amyloid fibrils, have interesting gelling, foaming, emulsifying and adhesive properties. However, their potential as food structuring agents remains to be explored. This project aims to rationally design amyloid-like structures with specific techno-functional properties from various cereals namely wheat, maize and rice. Firstly, the potential presence of protein fibrils in the current human diet will be explored. Then, cereal protein fibril formation will be investigated at the molecular level. High intrinsic aggregation sequences will be identified in silico, using online available software (e.g. TANGO, PASTA, AGGRESCAN), and in vivo, by comparing fibril formation in different proteolytic digests of cereal proteins. A third part will study the impact of food processing conditions (i.e. temperature, pH, ionic strength and protein concentration) as well as the potential of seeding and cross-seeding for cereal protein fibril formation. Lastly, the relationship between cereal protein fibril morphology and techno-functional properties (i.e. gelling and foaming) will be evaluated. A better understanding of wheat, maize and rice protein fibril formation will allow the design of protein structures with various highly relevant applications including the structuring of vegan protein-rich food and gluten-free products.