Heat induced aggregation of b-lactoglobulin studied by dynamic light scattering
The in situ heat-induced aggregation of commercial β-lactoglobulin as such, or after further purification, was followed to a z-average hydrodynamic diameter of 15–20 nm at 59–63 °C by dynamic light scattering. In this temperature range, measurable increase of hydrodynamic diameter occurred after an apparent lag period, which was strongly dependent on heating temperature, pH and initial protein con