Abstract
The influence of the ionic strength on the structure of β-lactoglobulin aggregates formed after heating at pH 7 has been studied using static and dynamic light scattering. The native protein depletion has been monitored using size exclusion chromatography. Above a critical association concentration (CAC) well-defined clusters are formed containing about 100 monomers. The CAC increases with decreasing ionic strength. The so-called primary aggregates associate to form self similar semi-flexible aggregates with a large scale structure that is only weakly dependent on the ionic strength. The local density of the aggregates increases with increasing ionic strength. At a critical gel concentration, C g, the size of the aggregates diverges. C g decreases from 100 g/l without added salt to 1 g/l at 0.4 M NaCl. For C> C g the system gels except at high ionic strength close to C g where the gels collapse under gravity and a precipitate is formed.
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