The aim of this paper was to determine the emulsification properties of protein aggregates obtained from heat pretreated yellow field pea protein concentrate (PPC). PPC dispersions were prepared in distilled water (adjusted to pH 3.0, 5.0, 7.0, or 9.0), heated in a water bath (100 °C) for 30 min, centrifuged and the supernatant passed first through a 30 kDa membrane and, then, the first retentate (>30 kDa) through a 50 kDa membrane. The 50 kDa membrane separation yielded a second retentate (>50 kDa proteins), which was isolated for emulsification studies. The near UV circular dichroic spectra of the protein samples showed more unfolded structures at pH 3.0 and 5.0 than at pH 7.0 and 9.0. The presence of small and spherical oil droplets of emulsions stabilized by the >50 kDa proteins at pH 3.0, 7.0, and 9.0 was confirmed by confocal laser scanning microscopy images. Emulsions stabilized at pH 7.0 and 9.0 had a narrower size distribution range than at pH 3.0 and 5.0. A narrow oil droplet size distribution range and lower interfacial protein concentrations of the emulsions stabilized by the >50 kDa proteins were observed at the corresponding pH of the heat treatment when compared to other pH values. Emulsions stabilized by the >50 kDa proteins exhibited a relatively low flocculation and coalescence index, which infers relative stability. The results from this work suggest that heat pretreatment of the PPC led to the formation of new protein aggregates, especially FT9 with enhanced emulsification properties, at some of the test conditions when compared to the unheated PPC.
Keywords: emulsions; heat; interfacial activity; membrane ultrafiltration; pea protein; protein aggregates.