Study of the mechanism of complex coacervation between beta-lactoglobulin and the major fractions of acacia gum - comparaison with the unfractionnated acacia gum

Abstract : The complex coacervation mechanism, an associative phase separation mainly induced by electrostatic interactions, between - lactoglobulin (BLG, animal protein) and Acacia gum (AG, vegetal polysaccharide) was studied in this work. The most significant difficulty to understand complex coacervation between BLG and AG at the molecular level is the molecular weight polydispersity of AG. From there, the main motivation of this research was to better understand and control the interactions between BLG and the major molecular fractions of AG, FI (~88% of AG) and FII (~10% of AG) using isothermal titration calorimetry, static and dynamic light scattering, electrophoretic mobility, Granulo-Polarimetry and optical microscopy. Higher energy of interaction, lower stoichiometry of association and then favorable complexation were shown between BLG and FII in relation with higher accessibility and density of charges for FII. The major results of this study reveal then different roles of AG fractions in complex coacervation with BLG
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Suzanna Akil. Study of the mechanism of complex coacervation between beta-lactoglobulin and the major fractions of acacia gum - comparaison with the unfractionnated acacia gum. Food and Nutrition. Institut National Polytechnique de Lorraine, 2007. English. ⟨NNT : 2007INPL020N⟩. ⟨tel-01752840⟩

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