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Heat induced aggregation of b-lactoglobulin studied by dynamic light scattering

In English

Författare

Summary, in English

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 concentration. The changes in time scale of the aggregation process agreed with changes in amount of unfolded β-lactoglobulin, assuming a two-state model of the denaturation. The pH dependence reflected the midpoint unfolding temperature and not the sulphydryl group reactivity, suggesting that this reactivity was not rate limiting in the aggregation. The aggregation process was modelled numerically with FuchsSmoluchowski kinetics.

Avdelning/ar

  • Department of Food Technology, Engineering and Nutrition

Publiceringsår

1996

Språk

Engelska

Sidor

343-357

Publikation/Tidskrift/Serie

International Dairy Journal

Volym

6

Issue

4

Dokumenttyp

Artikel i tidskrift

Förlag

Elsevier

Ämne

  • Food Engineering

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0958-6946