Fundamentals of unfolding, refolding and aggregation of food proteins

Protein functionality in food products strongly relies on the fact that proteins can undergo intermolecular interactions, called aggregation. It was found that very subtle dynamics inherent to the protein of interest can have consequences for the functional properties of proteins. The aim of this thesis is to explore structural features of proteins of importance to the generation of aggregation prone protein molecules. The approach selected involves chemical engineering in which functional groups of the protein are converted into a chemical group with different properties. This led to a detailed description of the structural impact of the modifications in relation to aggregate formation. It was found that the various modifications applied interact with the aggregation process in a rather diverse (but predictable) manner. The accumulation of data from this work in combination with results from literature was used to significantly improve the understanding of factors relevant to aggregation and to develop a model to predict aggregation propensity. This model can be used within the food and pharmaceutical industry to determine the aggregation propensity of proteins used in formulae and medication