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Differences in heat stability and ligand binding among β-lactoglobulin genetic variants A, B and C using (1)H NMR and

Julia K Keppler1, Frank D Sönnichsen2, Peter-Christian Lorenzen3

  • 1Christian-Albrechts-Universität zu Kiel, Department of Food Technology, Institute of Human Nutrition and Food Science, Heinrich-Hecht Platz 10, D-24118 Kiel, Germany.

Biochimica Et Biophysica Acta
|March 5, 2014
PubMed

Keywords:
Epigallocatechingallate bindingFluorescence quenchingGenetic variantProtein heat stabilityProtein–ligand interactionRetinol bindingβ-Lactoglobulin

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