Enhanced stabilization of oil-in-water (O/W) emulsions by fibrillar gel particles from lentil proteins

Pulse proteins as a sustainable protein source have attracted increasing interest in food development, but pulse proteins are generally less surface active than dairy proteins. This work introduces lentil protein (LP)-based fibrillar gel particles (FGPs) fabricated from heat-induced LP fibrillar aggregates by 1, 4, 8, and 16 h of heating, followed by particle reduction using sonication. The heating time significantly impacts the FGPs particle size and surface hydrophobicity. The FGP prepared by 4 h of heating (FGP-4) showed a small size (<200 nm) and homogeneous size distribution while possessing significantly increased surface hydrophobicity compared to untreated LP. Such structural features made FGP-4 better adsorb at the O/W interface and then completely covered the oil droplet surface, leading to homogeneous emulsions of small size (22.33 μm) and superior long-term stability without creaming for 30 days. In addition, the dispersed FGP in the bulk phase could develop interactions among each other, leading to improved emulsion viscosity and texture without oil droplet size change. This finding suggests that constructing fibril-type gel particles can provide a new strategy for forming superior O/W emulsions with improved stability from plant proteins.