Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations.

The protein transition motivates the use of plant proteins, but their application in food emulsions is challenging, especially when high concentrations of oil and salt are needed for formulation and sensory properties. In the present work, we connect the iso-electric point of two potato protein isolates (patatin-rich, POPI-200; protease inhibitor-rich, POPI-300) and a faba protein isolate (FPI) to the behavior in the bulk phase and at the interface, and relate this to the physical stability of 45 wt% oil-in-water (O/W) emulsions in the presence of NaCl at pH 4.0-7.0. In the absence of NaCl, a higher bulk viscosity was found at the iso-electric point (IEP), especially for the FPI. In the presence of NaCl, the viscosity of the POPI-200 solutions was highest, followed by POPI-300, and that of the FPI was lowest, irrespective of the pH. Both POPIs showed faster initial adsorption at the O/W interface in the absence of NaCl, and formed a more elastic layer compared to the FPI. For all proteins, salt addition leads to less elastic films. Interestingly, the interfaces were more elastic at a pH close to the IEP of the protein in the presence of NaCl. Both POPI-stabilized emulsions showed higher stability (smaller size and less oiling off) than the FPI-stabilized emulsions, which makes potato proteins relevant for food emulsion product formulation, even under high salt conditions.