Pea proteins, often marketed as hypoallergenic, merit a closer examination due to potential allergenic properties arising from proteins with structural similarity to soy and peanut proteins.

This pilot project investigated the complex process of protein-rich food digestion through a multiscale approach integrating scattering and microscopy. The influence of processing on pea allergenicity, while not fully explored, presents intriguing possibilities, hinting at potential improvements in digestion.

Large-scale facilities played a pivotal role, particularly SAXS, SANS, and SEC-SAXS techniques, for elucidating the structural evolution of pea protein systems during digestion. They allowed sufficient kinetic resolution and high-quality data to collect information on conditions of increased or obstructed digestion.

By combining complementary scattering methods with biochemical analyses, the research team ​identified a robust two-step digestion mechanism and resolved structural changes across multiple length scales, from individual proteins to the gel network. Furthermore, SEC-SAXS provided additional insight into the solution-state structure of pea protein fractions, highlighting the potential of multimodal scattering approaches at large-scale facilities for advancing the understanding of food structure–digestibility relationships.

These findings extend beyond food science, holding potential for tailored food design and even immunotherapy.

Scientific publication

February 2026 | Two-step digestion pathways of hydrogels from pea proteins | Journal of Colloid and Interface Science, Volume 703, Part 2

Pilot project contact

Davide Schirone
Malmö University
davide.schirone@mau.se