Salt-Promoted Fibrillation of Legume Proteins Enhanced Interfacial Modulus for Stabilization of HIPEs Encapsulating Carotenoids with Improved Nutritional Performance

The thermal acidic-treatment-induced fibrillation of legume proteins isolated from cowpea and mung bean was demonstrated to be promoted by salt. Worm-like thin prefibrilar intermediates were formed in low salt concentrations (0–75 mM), which twisted to be the thick and mature amyloid-like fibrils with multistrands as the salt content was elevated (150–300 mM). Absorption of the fibrils fabricated in high salt concentrations to the oil/water interface constructed the protein layer with a significantly higher interfacial modulus compared with the one formed by the fibrils fabricated in low salt concentrations. Consequently, they showed the superiority in stabilizing high internal phase emulsions (HIPEs) with oil volume fraction ratios higher than 74%. HIPEs stabilized by the high salt-concentration-induced legume protein fibrils had stronger capabilities not only in encapsulating liposoluble carotenoids but also in protecting their stability against heating, ultraviolet, and iron ion stimulus, compared with the one stabilized by the low-salt-concentration-induced legume protein fibrils. Bioaccessibilities of the carotenoids in simulating gastrointestinal (GI) digestion were significantly improved after encapsulation by the HIPEs, which were interestingly increased with the elevation of salt concentrations utilized for preparing the legume protein fibrils. Furthermore, the carotenoids-loading-HIPEs were injectable and showed in vivo nutritional functions of mitigating colitis.