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Title: Formation of non-native β-lactoglobulin during heat-induced denaturation
Authors: Kehoe, Joseph James
Wang, Lizhe
Morris, Edwin R
Brodkorb, Andre
Keywords: Whey proteins
Denaturation/aggregation kinetics
Stable intermediates
Issue Date: 1-Dec-2011
Publisher: Springer
Citation: Joseph James Kehoe, Lizhe Wang, Edwin R. Morris, André Brodkorb. Formation of Non-Native β-Lactoglobulin during Heat-Induced Denaturation. Food Biophysics, 2011, 6(4), 487-496. DOI: 10.1007/s11483-011-9230-3
Series/Report no.: Food Biophysics;vol 6
Abstract: A mechanism describing the denaturation and aggregation behavior during heat-treatment of pure β-lactoglobulin and β-lactoglobulin in whey protein isolate (WPI) under selected conditions (20 to 90 gL−1 in water at pH 7.0, 78 °C) is presented. A combination of reversed-phase and gel permeation chromatography was used to study the disappearance of native β-lactoglobulin and the formation of non-native intermediates in the aggregation process. The mean reaction order for pure β-lactoglobulin and β-lactoglobulin in WPI were the same, 1.4. While the rate of β-lactoglobulin denaturation was greater in WPI there was less aggregation compared to that of pure β-lactoglobulin. More of the β-lactoglobulin in WPI remained in a non-native monomer intermediate state after 30 min of heating. After an initial lag period, during which non-native monomers appeared, aggregates formed and rapidly reached a plateau in terms of their size. These aggregates were visualized using atomic force microscopy. There was no significant effect of protein concentration on either aggregate size or the number of exposed sulfhydryls in the heated solutions.
Description: peer-reviewed
This work was supported by the Food Institutional Research Measure (FIRM) of the National Development Plan 2000-2006 (Ireland). J. Kehoe was funded by the Teagasc Walsh Fellowship Scheme
URI: http://hdl.handle.net/11019/510
ISSN: 1557-1858
Appears in Collections:Food Chemistry & Technology

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