Protein–polysaccharide complexes are used to improve protein stability and encapsulate high-value ingredients, yet the influence of different salts on their formation has not been investigated. Using light scattering and turbidimetry, effects of chloride, sulphate and thiocyanate salts on β-lactoglobulin and pectin complexes (protein/pectin ratio = 2:1 and 4:1) were determined in relation to effects of pH and ionic strength. Effects of anions on complex formation were significant at 25 mmol kg−1 added ionic strength. Cation effects were not significant. At 100 mmol kg−1 ionic strength, pH of complex formation increased with sulphate salts (pH 5.1) relative to chloride and thiocyanate salts (pH 4.9), while pH of coacervation increased with sulphate salts (pH 4.7) and decreased with thiocyanate salts (pH 4.4) relative to chloride salts (pH 4.6). Pure β-lactoglobulin stability was otherwise reduced with thiocyanate salts below pH 5, implying a significant effect of pectin interactions.