Heat-induced changes in oil-in-water emulsions stabilized with soy protein isolate

Abstract

The physicochemical properties of soy proteins stabilized oil-in-water emulsions were studied after heating at two different temperatures, 75 and 95 °C. The effect of changing the order of the process (heating the solution before emulsification, or heating the emulsion) was also studied. The heating temperatures were chosen as they are known to selectively cause denaturation of the two major proteins present in the soy protein isolate: β-conglycinin and glycinin. The thermal transitions observed for soy proteins adsorbed at the interface were different from those measured in protein solutions, suggesting that some changes occur in the structure of the soy proteins upon adsorption on the oil droplet. Heating induces aggregation of the oil droplets, as shown by an increase of the particle size and the bulk viscosity of the emulsions, with a more prominent effect after heating at 95 °C. Transmission electron microscopy observations clearly demonstrate that heating induces the formation of large protein aggregates at the interface. In addition, the composition of the protein present at the interface changes depending on the order of heating and homogenization. While heating the solutions before emulsification results in all the protein subunits to be present at the interface in an aggregated form, when heating is applied after emulsification, a portion of the α and the α′ subunit of β-conglycinin as well as the acidic subunits of glycinin remain unadsorbed.