The processing conditions used to prepare pulse protein ingredients could be directly responsible for their solubility and functional properties in food products. Freeze-dried soluble and insoluble fractions of faba bean protein (FBP) and pea protein (PP) concentrates, isolates and de-flavoured fractions were prepared and characterized for their structure-functional properties. FBP showed a significant drop in oil-water interfacial tension compared to PP. The FBP and PP isolates showed higher protein content but lesser solubility in water compared to the concentrates, which could be attributed to their processing conditions. Oil-in-water model salad dressing emulsions were prepared with 40% oil and an aqueous phase containing 2% proteins and 0.25% xanthan gum using a high-shear mixer. Emulsions were stored for two weeks and characterized by droplet size, zeta potential, rheology, and accelerated stability analysis using a photocentrifuge. All emulsions were stable without any visible phase separation at pH 7, while at pH 2, except the emulsions stabilized by FBP fractions, phase separation occurred, leaving a clear aqueous phase at the bottom. There was a significant reduction in the droplet diameter of all emulsions at pH two compared to the emulsions at pH 7. Protein fractions with coarser particle size formed larger emulsion droplets compared to the finer fractions. All emulsions at pH 2, except the ones prepared with FBP fractions, showed a large drop in apparent viscosity compared to pH 7. Overall, processing conditions and preparation methods of protein ingredients influence their structure and physicochemical properties, which could be used to predict their emulsification behaviour.