print

Phospholipids on a pea

Neutron reflectometry provides valuable insights into the molecular intricacies of plant-based food

To this day, one of humankind’s greatest challenges is to provide universal, stable access to food around the globe. While we currently rely heavily on animal-derived products, in particular to cover our protein requirements, numerous problems associated with an overconsumption of meat and dairy call for a switch to more sustainable protein sources.

Peas are sometimes considered a Swiss Army knife amongst alternatives to animal protein. They can be grown in various climate zones, cause few allergies and have a high protein content. Two types of pea proteins - legumin and vicilin, which differ strongly in their chemical properties - have been identified as being of particular interest for plant-based food. Their appeal is due to their ability to form films at oil-water interfaces. This implies that they help mix water-soluble components with oils and fats or create foams, which is highly appreciated in plant-based desserts or cappuccino. A detailed, molecular-level understanding of pea protein adsorption to fatty molecules is crucial for optimising the formulation, texture and mouthfeel of plant-based food.

“Studies of the associations of biological molecules to phospholipids are one of the specialties of neutron reflectometry”, says Alexey Vorobiev, the main responsible of ILL’s neutron reflectometer SuperADAM. “In a neutron reflectometry experiment, we direct a beam of neutrons onto a very flat surface. The way the neutrons are reflected off the surface gives us precise insights on its roughness, composition and how different molecules adsorb to it.” Neutrons are particularly suited for these kinds of studies since they are non-destructive and penetrate deeply into matter. In addition, they are extraordinarily sensitive to hydrogen, a critical component of biomolecules.

Teaming up with Vorobiev, a research group from Sweden, Denmark and Italy performed a series of detailed experiments on SuperADAM to understand how legumin and vicilin behave in the presence of phospholipids, a well-studied class of fats. “We deposited thin films of phospholipids commonly used in research on a silicon wafer and then added solutions of legumin and vicilin”, explains Gökhan Uğur Atıl, the first author of the study.

“Interestingly, we saw that legumin did not seem to interact with the phospholipid film, even if we changed its composition.” Vicilin, on the other hand, changed its structure while also attaching to the phospholipid film. “When we constructed a mathematical model of our data, we were able to deduce that vicilin formed soluble molecular complexes with the phospholipid molecules”, adds Atıl.

This study, providing molecular-level insights into protein behaviour at lipid interfaces, is an important step towards a more general understanding of the hidden nature of plant-based foods. “With plant proteins becoming increasingly important alternatives to animal-based food, such research will help us guide the design of delicious, appealing plant-based products”, says Tommy Nylander, principal investigator of the study together with Milena Corredig.


Reference: Gökhan Uğur Atıl, Marshall R. Machingauta, Alessandra Luchini, Alexey Vorobiev, Milena Corredig, Tommy Nylander. "Pea protein isolates adsorption on phospholipid bilayer interfaces: a quartz crystal microbalance and neutron reflectometry study". Food Hydrocolloids 172 (2026) 111842.

https://doi.org/10.1016/j.foodhyd.2025.111842

ILL instrument:SuperADAM

ILL contact person: Alexey Vorobiev