(Amyloid) Protein Aggregates from β-Lactoglobulin and Their Behavior Along the Process Chain

Amyloid aggregates are anisotropic protein aggregates that comprise a recurrent alpha-helix or beta-sheet motif. These aggregates can vary in shapes or morphologies ranging from rigid, semi-flexible fibrils with a high aspect ratio to short, worm-like or curly and flexible structures. Their specific properties lead to enhanced functionalities suitable for food and non-food industries. However, exploration of their processing stability is currently insufficient. We hypothesize, that the (food) processing chain leads to an overlapping of assembly and disassembly mechanisms of amyloid structures within a process, which can have positive and negative effects on the resulting aggregate structure, its functionality as well as its formation kinetics. To produce protein aggregates with particular morphologies and target functionality we investigated the assembly process of proteins from the nanoscale (protein structures) to the mesoscale (aggregate morphologies) to the macroscale (network formation) across the processing chain of the production of foams, emulsions and films. These results will allow us to better control the formation and process behavior of these functional aggregates leading to targeted applications.