Quinoa is a pseudocereal with a complete essential amino acid profile and nutritionally favourable fatty acid composition. Here, cryo-milling was used to disrupt quinoa seeds, promoting the preservation of the native oleosome structure, which was then recovered by centrifugation of the cryo-milled seed suspension. The remaining flour suspension was used to extract quinoa protein isolate; applying alkalinisation followed by precipitation with HCl, acetic acid or citric acid. Microscopy, droplet size and ζ-potential data indicated recovered oleosomes were predominantly in their native state, which was retained after acid treatment. Quinoa protein precipitated with citric acid showed a higher denaturation enthalpy compared to protein precipitated with HCl or acetic acid. The citric acid-based protein gel also had the highest final gel strength and showed a fine stranded microstructure, while the HCl-based protein gel had the lowest final gel strength and displayed a particulate microstructure. Treatment with acetic acid gave a protein gel that demonstrated a mix of both types of microstructures. This study not only introduces quinoa seed oleosomes and quinoa protein isolate with improved and tailored functionality but also demonstrates the potential of cryo-milling as a seed disruption technology that allows recovery of intact oleosomes. • Extraction of quinoa seed oleosomes (OS) and protein isolates; • Cryo-milling allowed OS recovery in the native state; • OS microstructure was not affected by acid treatment; • Precipitation with citric acid protected native protein and improved gel strength.

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.