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|Title:||Observation of salt-induced β-lactoglobulin aggregation using sedimentation field-flow fractionation|
|Keywords:||Biochemistry, Genetics and Molecular Biology;Chemistry|
|Citation:||Analytical and Bioanalytical Chemistry. Vol.386, No.6 (2006), 1681-1688|
|Abstract:||Sedimentation field-flow fractionation (SdFFF) was applied in order to characterize particle sizes of β-lactoglobulin aggregates induced by Ca2+or Zn2+. Aggregation induced by Zn2+was faster than that induced by Ca2+. Effects of Zn2+and β-lactoglobulin concentrations, as well as contact time, on the aggregation of β-lactoglobulin were examined. All factors exhibited a combined effect on the size of aggregates, whereby larger aggregates were obtained at increased concentrations of Zn2+and β-lactoglobulin. At fixed concentrations of 2% (w/v) β-lactoglobulin and 10 mM Zn2+, the particle size of the aggregates increased from 0.19 μm (at 15 min) to 0.38 μm (at 2880 min). Further, a hyphenated technique of SdFFF and inductively coupled plasma-optical emission spectrometry (ICP-OES) was used to examine whether intermolecular ionic bridges take part in salt-induced β-lactoglobulin aggregation. With SdFFF-ICP-OES, protein-cation-protein cross-linkages were observed for β-lactoglobulin aggregation induced by Zn2+, but not for that induced by Ca2+. © Springer-Verlag 2006.|
|Appears in Collections:||Scopus 2006-2010|
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