Multilayer model for pea protein supramolecular aggregates with phospholipids studied by neutron reflectometry.

We need to build a food system that include more sustainable, plant-derived protein, substituting animal protein in our diet. This is
challenging as we are not able to control the technological functionality of these proteins in foods. We propose to study the
supramolecular aggregates formed from pea proteins in the seed, as well as in the isolates, using for the first time neutron reflectometry. We are proposing that pea proteins, in nature, have compact structures dominated by hydrogen (beta-sheet stacks) bridges and hydrophobic interactions. These supramolecular stacked aggregates structure which includes phospholipids are critical to the preservation of the protein bodies (about 3 micron size) in the seed. We are proposing that the protein in the protein body of the seed is structured in various stratified layers with a layer of phospholipids present in between the layers. This can in the seed protect the protein from a rapid dissolution. To test this hypothesis, we would like to perform neutron reflectometry experiments with phospholipid layers and extracts of different pea proteins. This will allow us to observe “formation” of these protein/lipid structures.