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 (6.0-1.5), salt concentration (NaCl, 0-50 mM), and protein-polysaccharide weight mixing ratio (1:4 to 10:1 w/w). For mixtures in the absence of salt and at a 1:1 mixing ratio, two structure-forming transitions were observed as a function of pH. The first event occurred at a pH of 4.2, with the second at pH 3.7, indicating the formation of soluble and insoluble complexes, respectively. Sodium chloride (<or=7.5 mM) was found to have no effect on biopolymer interactions, but interfered with interactions at higher levels (>7.5 mM) due to substantial PPI aggregation. The pH at which maximum PPI-GA interactions occurred was 3.5 and was independent of NaCl levels. As PPI-GA ratios increased, structure-forming transitions shifted to higher pH.