The antigenic response of ß-lactoglobulin is modulated by thermally induced aggregation

Publikations-Art

Zeitschriftenbeitrag

Autoren

Kleber, N.; Krause, I.; Illgner, S.; Hinrichs, J.

Erscheinungsjahr

2004

Veröffentlicht in

European Food Research and Technology

Band/Volume

Vol. 219, July 2004/2

Seite (von - bis)

105-110

Schlagworte

aggregation, denaturation, epitope, Hitzebehandlung, ß-lactoglobulin

The antigenic response of thermally denatured and aggregated ß-lactoglobulin was determined by an indirect competitive enzyme-linked immunosorbent assay using polyclonal antibodies from the egg yolk of chicken immunized with heat-denatured ß-lactoglobulin as a measure for the potential antigenicity/allergenicity. The heat denaturation and the aggregation of heated whey protein isolate solutions were followed by reversed-phase high-performance liquid chromatography and photon correlation spectroscopy. Thermally modified whey proteins showed a remarkable increase of antigenicity when heated to 90 °C, possibly as a consequence of the exposure or formerly hidden epitopes. Above 90 °C, the antigenic response decreased owing to the loss of conformational epitopes and masking of sequential epitopes in the course of aggregation to particles. When large and compact particles were formed, the antigenicity was reduced remarkably. Depending on the heating condition applied, the structure and the size of whey protein particles and thus the potential allergenicity may be modulated in a wide range.