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

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Galani, D and Apenten, Richard KO (1999) Heat-induced denaturation and aggregation of beta-Lactoglobulin: kinetics of formation of hydrophobic and disulphide-linked aggregates. INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY , 34 (5-6). pp. 467-476. [Journal article]

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URL: http://www3.interscience.wiley.com/journal/119095028/abstract

DOI: 10.1046/j.1365-2621.1999.00314.x

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.

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Northern Ireland Centre for Food and Health (NICHE)
ID Code:14692
Deposited By:Dr Richard Owusu-Apenten
Deposited On:03 Aug 2010 08:50
Last Modified:28 Jan 2014 14:46

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