The influence of electrostatic interaction on the structure and the shear modulus of heat-set globular protein gels

Abstract

Gels formed by the globular protein β-lactoglobulin after heat denaturation were studied using light scattering, turbidity and shear oscillation measurements. The structure of the gels was characterized in terms of the amplitude and the correlation length of concentration fluctuations. The strength of electrostatic interactions was varied by changing the pH in the absence of added salt or by changing the NaCl concentration at pH 7. A very strong increase of the heterogeneity of the gels was observed when decreasing the pH towards the isoelectric point or when increasing the salt concentration. The structural change was interpreted in terms of a decrease of the net repulsion between the growing aggregates leading to increased concentration fluctuations and finally microscopic phase separation. The elastic shear modulus increased with decreasing pH and showed a maximum as a function of the NaCl concentration. No direct correlation between the change in the structure and the elastic modulus was found.