Speaker
Description
Pea proteins have gained interest due to their potential to become a sustainable alternative to animal derived food proteins. Today most development work is focused on the protein fraction but requires further studies on the interaction between different components. Of particular interest are the interactions with lipids, as there is lack of fundamental knowledge despite their key role in the plant seed architecture and their importance in obtaining palatable products. In earlier work, we have shown by using neutron reflectometry that these proteins interact with model lipid membranes produced with synthetic phospholipids (1). Recently we have been able to show that the native polar lipid fraction from pea self-assemble into well-defined lipid bilayers on a silicon block. We here used for the first time, magnetic reference layers and polarized neutrons (2) to study native pea lipids bilayers. This allowed us not only to characterise the bilayer structure but how purified pea proteins, i.e. legumin and vicilin, interact with this natural lipid extract. We noted that vicilin show stronger interaction, i.e., denser protein layer, with the lipid bilayer than legumin. We discuss how such an interaction might be facilitated by the compact structure of pea proteins, which is dominated by hydrogen (beta-sheet stacks) bridges and hydrophobic interactions.
1. G. U. Atül, M. R. Machingauta, A. Luchini, A. Vorobiev, M. Corredig, T. Nylander. Food Hydrocolloids, 2026, 172, 111842.
2. O. Dikaia, A. Luchini, T. Nylander, A. Grunin, A. Vorobiev, A.Goikhman. J. Appl. Cryst. 2024, 57, 1145–1153.