Truncated protein extraction modulates pea protein–carbohydrate thermal co-gelation

Conventional methods of pea protein extraction are resource-intensive, involving multiple purification steps that remove co-existing components such as starch. In contrast, we investigate how minimally processed yellow pea protein extracts that retain residual carbohydrates form thermally induced gels. Contrast-variation small-angle neutron scattering, rheology, and differential scanning calorimetry show that salt-extracted samples form a unified gel matrix through co-gelation of protein and carbohydrate components, as evidenced by a shared contrast match point in the final network. Ultra-small-angle neutron scattering reveals mesoscale heterogeneity, with structural features persisting up to 2 μ m, indicative of a particulate, protein-rich network within the composite gel. Rheological and calorimetric analyses suggest that gelation proceeds via a kinetic pathway in which protein aggregation precedes unfolding, ultimately shaping network architecture and viscoelastic properties. These findings demonstrate that minimal processing can yield structurally integrated protein–starch gels and clarify how composition and processing determine network architecture and mechanical performance. • We study the thermal gelation of pea protein and carbohydrates from truncated extraction. • Co-gelation is evidenced via contrast-variation small-angle neutron scattering. • Model fitting and data-driven decomposition evidence multi-scale structures. • The gelation process is further monitored by rheology and calorimetry. • Protein-carbohydrate co-gelation seems promising for sustainable protein extraction.