Influence of main whey protein components on the mechanism of complex coacervation with Acacia gum

•The two main components of whey protein isolate, β-lactoglobulin and α-lactalbumin, undergo complex coacervation with Acacia gum.•β-lactoglobulin has stronger binding to Acacia gum than α-lactalbumin.•A residual concentration of proteins remains in the aqueous phase in all instances. Quantification...

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Published in:Colloids and surfaces. A, Physicochemical and engineering aspects Physicochemical and engineering aspects, 2015-09, Vol.481, p.367-374
Main Authors: Ach, Delphine, Briançon, Stéphanie, Dugas, Vincent, Pelletier, Jocelyne, Broze, Guy, Chevalier, Yves
Format: Article
Language:English
Subjects:
Acacia gum
Analytical chemistry
Capillary electrophoresis
Chemical Sciences
Complex coacervation
Galenic pharmacology
Life Sciences
Material chemistry
or physical chemistry
Pharmaceutical sciences
Phase separation
Polymers
Theoretical and
Whey proteins isolate
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Summary:•The two main components of whey protein isolate, β-lactoglobulin and α-lactalbumin, undergo complex coacervation with Acacia gum.•β-lactoglobulin has stronger binding to Acacia gum than α-lactalbumin.•A residual concentration of proteins remains in the aqueous phase in all instances. Quantification of α-lac and β-lg in whey proteins/Acacia gum coacervate by capillary gel electrophoresis. [Display omitted] Complex coacervation between whey proteins isolate (WPI) and Acacia gum was investigated in order to disclose the roles and the contributions of each component of WPI to the formation of the complex coacervate. The main aim was to establish the balance of the main components of WPI, β-lactoglobulin and α-lactalbumin, during the phase separation of complex coacervate. The complex coacervation of Acacia gum and pure β-lactoglobulin, pure α-lactalbumin, and WPI have been investigated and compared together by means of macroscopic observations and capillary gel electrophoresis analyses performed along pH scans from basic to acidic medium. Coacervate composition was influenced by the protein/polysaccharide (Pr:Ps) ratio and pH. An optimum pH for best coacervation yield was found for each Pr:Ps ratio. Non-negligible concentrations of β-lactoglobulin and α-lactalbumin remain in solution in most instances. β-lactoglobulin undergoes complex coacervation stronger than α-lactalbumin in their competitive coacervation of WPI and Acacia gum.
ISSN:0927-7757
1873-4359
DOI:10.1016/j.colsurfa.2015.06.006