Napins and cruciferins in rapeseed protein extracts have complementary roles in structuring emulsion-filled gels

We investigated the complementary roles of napins and cruciferins present in a rapeseed protein mixture (RPM) structuring emulsion-filled gels (EFGs). Napins are small molecular weight albumins with high interfacial activity, while globulins that form upon heat-induced gelation. The role is to stabilize emulsion droplets, cruciferins, which were previously found interact adsorbed napin layer, can build gel network around droplets. effects oil concentration (0–30 wt%) pH (5 7) on rheological microstructural properties EFGs investigated. In absence oil, at 5, due low solubility, RPM formed heterogeneous built aggregates. At 7, was more soluble homogeneous strand-like structures higher firmness. presence firmness increased, pronounced reinforcement 5 compared 7. type did not change by droplets neither nor as suggested from confocal microscopy unchanged response large deformation. This implies really structure. being stiffer than matrix, integrated structural increased research shows two different proteins less purified extract, provides single ingredient suitable for food gels. • Less extracts contain both cruciferins. had stabilized network. affected microstructure EFGs. Napin-stabilized reinforced