Structural, techno-functional and thermal properties of protein fractions from Inga jinicuil seeds: An underexplored legume protein source

• Albumin fraction exhibited high solubility and emulsifying capacity a wide pH range. • Globulin showed superior thermal stability and resistance to denaturation. • Glutelins and prolamins unfolded structures with enhanced water and oil retention. • Jinicuil proteins show potential and functional ingredient for food applications Inga jinicuil seeds are an underutilized legume with high protein content, a favorable fatty acid profile (ω-6/ω-3 = 1.97), and low sodium (35.25 mg/100 g). Osborne fractionation was applied for the first time to obtain albumins, globulins, prolamins, and glutelins, each with protein contents above 80%. Structural analysis showed that prolamins and glutelins exhibited predominantly unfolded conformations, with disordered regions, β-turns, exposed aromatic amino acids, and smaller particle sizes, contributing to higher water and oil holding capacities. Albumins displayed superior techno-functional properties, including high solubility (75–93%), emulsifying activity (27–35 m²/g), and foaming capacity (58–64%) across a wide pH range, while globulins showed intermediate behavior. The total protein isolate exhibited complex structural organization, high denaturation temperature (>90°C), high enthalpy, and low thermal degradation, indicating strong functional and thermal stability and supporting their potential as innovative ingredients in advanced food formulations.