LAUSR

Abstract The complexation between ovalbumin (OVA) and highly charged dextran sulfate (DS) was investigated employing phase behavior, zeta potential, confocal laser scanning microscope (CLSM), isothermal titration calorimetry (ITC) measurement, and dynamic rheometer analysis. The critical boundary pH values (pHc, pHφ1, pHmax) were strongly dependent on the biopolymer ratio and salt concentration. Results of the phase diagram and zeta potential showed that the formation of complexes was mainly driven by strong electrostatic interactions. As the increase of the OVA/DS ratio, the critical pH values shifted to higher values. However, the addition of NaCl has a diverse effect, lower salt concentration (CNaCl ≥ 100mM) suppress the formation of coacervates due to the shielding effect. The ITC results revealed that DS does bind to native form of OVA at pH 7.0 through the electrostatic forces and it was a spontaneous exothermic process(△G