Light scattering study of heat-denatured globular protein aggregates.

The structure of aggregates formed by the globular protein beta-lactoglobulin (beta-lg) after heat induced denaturation was studied using light scattering and size exclusion chromatography. The influence of varying the pH above the iso-electric point (pH 5.2) was investigated in the absence of added salt. Stable aggregates could be formed and characterized between pH 5.8 and pH 9. The large-scale structure of the aggregates was self-similar and remarkably insensitive to the pH. Below a critical association concentration, which decreased with decreasing pH from 10 to 1g/L, denatured monomers and small oligomers were formed. At higher concentrations larger so-called preaggregates formed containing roughly 100 monomers. With increasing concentration the size of the aggregates varied little until it rose sharply close to the gelation concentration that decreased with decreasing pH (50 g/L<C(g)<90 g/L). The effect of the pH on the interaction in solutions of native beta-lactoglobulin was also investigated.