Soybean lipophilic protein (LP) is a protein-phospholipid complex with significant development potential; however, the molecular mechanism underlying its foaming properties remains poorly understood. This study systematically elucidated the interactions between phosphatidylcholine (PC) and the three major protein components (β-conglycinin (7S), glycinin (11S), and oil body-associated proteins (OBPs)) in LP, along with their effects on air-water interface characteristics, by reconstructing binary complexes based on the actual compositional ratios found in LP. Results showed that 7S, 11S, and OBPs accounted for 26.75 %, 19.89 %, and 16.65 % of the major protein mass in LP, respectively, which also contained 28.78 mg/g phospholipids. PC spontaneously binds to all three proteins via hydrophobic interactions (ΔG < 0), with OBPs exhibiting the highest binding affinity (Ka). Upon complex formation, an increase in β-sheet content and static fluorescence quenching were observed, indicating conformational changes in the proteins. Meanwhile, surface hydrophobicity decreased for all protein-PC complexes; the ζ-potential increased for 7S/11S-PC complexes, whereas the particle size of the OBP-PC complex decreased while maintaining stable electrostatic potential; Furthermore, all complexes effectively reduced surface tension, enhanced diffusion and adsorption kinetics at the air-water interface. OBPs exhibited minimal foaming capacity due to severe self-aggregation; 7S and its complexes demonstrated superior foam capacity; whereas the 11S system formed more stable interfacial films, resulting in the most outstanding foam stability. This work provides mechanistic insights into protein-PC interactions, offering a theoretical foundation for understanding multicomponent synergy in LP and guiding the design of high-performance plant-based protein foaming agents.


扫码关注我们
求助内容:
应助结果提醒方式:

