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Study of the complex coacervation mechanism between the major fractions of Acacia gum and β-lactoglobulin - Comparaison with the unfractionated Acacia gum

Abstract : The complex coacervation mechanism, an associative phase separation mainly induced by electrostatic interactions, between ß-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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https://tel.archives-ouvertes.fr/tel-00190002
Contributor : Suzanna Akil <>
Submitted on : Thursday, November 22, 2007 - 7:49:57 PM
Last modification on : Monday, April 16, 2018 - 10:42:01 AM
Long-term archiving on: : Monday, April 12, 2010 - 3:20:25 AM

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Suzanna Akil. Study of the complex coacervation mechanism between the major fractions of Acacia gum and β-lactoglobulin - Comparaison with the unfractionated Acacia gum. Other. Institut National Polytechnique de Lorraine - INPL, 2007. English. ⟨tel-00190002⟩

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