Michael T. Nickerson

TL;DR: The factors affecting the stability of emulsions using food proteins will be discussed and the use of polysaccharides to complex with proteins will also be explored in relation to enhancing emulsion stability.

TL;DR: In this article, the physicochemical properties (surface charge/hydrophobicity, protein solubility, interfacial tension, and droplet size) of chickpea (ChPI), faba bean (FbPI), lentil (LPI), and pea (PPI) protein isolates produced by isoelectric precipitation and salt extraction were investigated relative to each other and a soy protein isolate (SPI).

TL;DR: This review discusses structure–function relationships of pea protein isolates, theimpact of extraction techniques used to produce the isolate, and the impact of cultivar and environment on ingredient performance in terms of solubility, water- and oil-holding capacities, emulsifying, foaming, and gelation properties.

TL;DR: In this article, protein isolates prepared from three pea cultivars by alkali extraction/isoelectric precipitation (AE-IP), salt extraction-dialysis (SE) and micellar precipitation (MP) were assessed for their surface (charge, hydrophobicity) and functional (water/oil holding capacity, solubility, foaming and emulsion capacities/stabilities) properties.

TL;DR: Turbidity measurements were used to study the formation of soluble and insoluble complexes between pea protein isolate (PPI) and gum arabic (GA) mixtures as a function of pH and sodium chloride was found to have no effect on biopolymer interactions, but interfered with interactions at higher levels due to substantial PPI aggregation.