Heat-induced denaturation and aggregation of beta-Lactoglobulin: kinetics of formation of hydrophobic and disulphide-linked aggregates

D Galani, Richard KO Apenten

Research output: Contribution to journalArticle

90 Citations (Scopus)

Abstract

Solutions of a whey protein mixture were subjected to various time/temperature treatments, at pH 6.7. Kinetic and thermodynamic activation parameters for the rates of irreversible denaturation/aggregation of the principal whey protein component-beta-lactoglobulin (beta-1g) were followed by gel permeation. Fast Protein Liquid Chromatography (non-dissociating, non-reducing conditions) and by SDS-PAGE (dissociating, non-reducing conditions). The rate of loss of native beta-1g owing to the formation of disulphide linked protein aggregates (k(SDS-PAGE)) and the rate of formation of aggregates via both covalent and non-covalent bonds (k(GP-FPLC)) showed similar biphasic Arrhenius plots. However, the break of the plot occurred at different points. The k(GP-FPLC) Values were higher than values of k(SDS-PAGE) for all the temperatures examined. There was a similar trend for the thermodynamic activation parameters implying that not all of the beta-1g aggregates through thiol-disulphide interactions. Hydrophobically driven associations occur within the aggregates.
Original languageEnglish
Pages (from-to)467-476
JournalInternational Journal of Food Science and Technology
Volume34
Issue number5-6
DOIs
Publication statusPublished - Oct 1999

Fingerprint Dive into the research topics of 'Heat-induced denaturation and aggregation of beta-Lactoglobulin: kinetics of formation of hydrophobic and disulphide-linked aggregates'. Together they form a unique fingerprint.

  • Cite this