Interactions between β-lactoglobulin and dextran sulfate at near neutral pH and their effect on thermal stability

The effect of interactions between β-lactoglobulin (β-LG) and dextran sulfate (DS) on thermal stability at near neutral pH was investigated. Samples containing 6% w/w β-LG and DS (M_w = 5–500 kDa) at different biopolymer weight ratios, pH (5.6–6.2), and NaCl concentrations (0–30 mM) were heated at 85 °C for 15 min. Turbidity results showed that the presence of DS at appropriate biopolymer weight ratio and pH significantly lowered the turbidity of heated β-LG. Solutions containing DS:β-LG weight ratios of 0.02 or less showed improved heat stability as indicated by decreased turbidity. Analysis of the unheated mixture by size exclusion chromatography coupled with multi-angle laser light scattering (SEC–MALLS) showed an interaction between β-LG and DS. The size of the aggregates increased as pH decreased. The β-LG–DS aggregates had a greater negative charge as seen from electrophoretic mobility measurement. Addition of 30 mM NaCl inhibited complex formation and the effect of DS on reducing the turbidity of heated β-LG, suggesting that the interaction was electrostatic in nature. Other than charge property, the amount and size of native aggregates appeared to be the major factor in determining how DS altered heat-induced aggregation. The presence of DS decreased denaturation temperature of β-LG, indicating that DS did not improve thermal stability of β-LG by stabilizing its native state but rather by altering its aggregation. The results provide information that will facilitate the application of whey proteins and polysaccharides as functional ingredients in foods and beverages.