| Abstract
| - The aggregates in heated bovine β-lactoglobulin solutions wereseparated by high-performance size-exclusion chromatography, and molecular characteristics were measuredon-line using multianglelaser-light scattering detection (SEC-MALLS). This technique wasproven to be a very useful andvaluable approach for characterization of heat-inducedβ-lactoglobulin aggregates. Using TSK G2000SWXL and TSK G4000 SWXL silica gel columnsconnected in series, aggregates up to a molecularmass of 4 × 106 Da could be separated, and completemolecular mass distributions were derived.Up to a molecular mass of 1.5 × 106 Da the molecularmasses calculated by the MALLS agreedvery well with the results obtained by conventional calibration.The measured molecular massdistributions of the heat-induced β-lactoglobulin aggregates variedstrongly with experimentalheating conditions (β-lactoglobulin concentration, pH, heatingtemperature, ionic strength). Theresults obtained with several β-lactoglobulin concentrations atneutral pH were consistent with akinetic aggregation model based on thiol/disulfide exchange reactions.The average molecular massand the radius of gyration of the heat-induced β-lactoglobulinaggregates increased with increasinginitial β-lactoglobulin concentration. Keywords: β-Lactoglobulin; aggregation; size-exclusion chromatography;light scattering; molecularsize
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