Structuration mechanism of β-lactoglobulin – acacia gum assemblies in presence of quercetin |
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Authors: | Leïla Aberkane Jordane Jasniewski Claire Gaiani Raza Hussain Joël Scher Christian Sanchez |
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Affiliation: | 1. Laboratoire d’Ingénierie des Biomolécules, Nancy-Université, INPL-ENSAIA, 2 avenue de la Forêt de Haye, F-54505 Vandoeuvre-lès-Nancy cedex 5, France;2. UMR 1208 IATE, UM2-INRA-SupAgro-CIRAD, 2 place Viala, 34060 Montpellier cedex 1v, France |
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Abstract: | The interactions of β-lactoglobulin (BLG) with total Acacia gum (TAG) in presence of quercetin have been investigated in aqueous solutions at pH 4.2 and 25 °C. Isothermal titration calorimetry (ITC) has been used to determine the type and magnitude of the energies involved in the complexation process. Dynamic light scattering (DLS), electrophoretic mobility (μE), turbidity measurements (τ), optical microscopy and Fourier transform infrared spectroscopy in total attenuated reflection mode (ATR-FTIR) were used as complementary methods to better understand the sum of complicated phenomena at the origin of thermodynamic behaviour. |
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Keywords: | β-Lactoglobulin Acacia gum Quercetin Complexation Isothermal titration calorimetry FTIR |
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