Designing foods for the future requires innovative approaches. At the KU Leuven Laboratory of Food Chemistry and Biochemistry (LFCB) we believe that proteins play a key role in the development of healthy and sustainable food products. In this context, amyloid fibrils are a specific protein structure with the potential of delivering specific techno-functionality (e.g. gelling and foaming) in food products. While amyloid fibrils were initially associated with neurodegenerative diseases, it is known now that they are utilized by several organisms (e.g. bacteria, plants and mammals) with a functional role.
The aim of our project is to study the formation, techno-function and nutrition of cereal and egg protein fibrils (amyloids). Our work forms a scientific base to improve the techno-functionality of food proteins in industry and is part of the ProFibFun project (“Tailoring food protein functionality by rational design of fibrillar structures”). ProFibFun is an SBO-project (Strategic Base Research) with six research groups (four at KU Leuven and two at Ghent University) housing 4 PhD students, 1 postdoc and 2 half-time lab technicians.
Over the last years, the LFCB has extensively studied the formation of amyloid(-like) fibrils from egg white and cereal proteins under relevant food processing conditions. In addition, several analytical methods have been optimized to characterized amyloid (-like) fibrils derived from food-related matrixes. Now, we face the challenge of evaluating the impact of different types of protein and other food constituents (e.g. salt, starch, sugar, etc.) on protein fibrillation. In addition, the presence or absence of amyloid fibrils in commercial food products will be screened. Furthermore, the rheological properties (e.g. waterbinding, gelling, foaming, etc.) of the formed structures will be studied in-depth. In a final step, the well-chosen protein mixtures and conditions will form a base for the manufacturing of some selected food products.
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