|Title||Influence of pectin characteristics on complexation with ß-lactoglobulin|
|Source||Wageningen University. Promotor(en): Fons Voragen; Willem Norde, co-promotor(en): Henk Schols. - [S.l. : S.n. - ISBN 9789085858355 - 174|
AFSG Biobased Products
Physical Chemistry and Colloid Science
Food Chemistry Group
|Publication type||Dissertation, internally prepared|
|Keyword(s)||pectinen - bèta-lactoglobuline - ladingskenmerken - fysische eigenschappen - chemische eigenschappen - binding (scheikundig) - pectins - beta-lactoglobulin - charge characteristics - physical properties - chemical properties - bonding|
|Categories||Chemistry of Food Components|
|Abstract||Pectin and proteins are both common food constituents. The type of pectin that forms complexes with protein is known to be of great influence on the structure and stability of liquid foods. Therefore, the aim of this thesis is to investigate the influence of the overall charge and local charge density of pectin on the formation of soluble complexes with β-lactoglobulin (β-lg).
Combination of state diagrams and binding isotherms shows that a high local charge density of pectin is a prerequisite to form soluble complexes with β-lg at higher ionic strength. A high overall charge of pectin results in the close proximity of the GalA blocks. Therefore, β-Lg neighbours bind close together on pectin with a high overall charge, which leads to lateral repulsion and hence, maxima in the binding constant and the pH where insoluble complexes form with increasing ionic strength.
The formation of soluble complexes has an enthalpic driving force from electrostatic attraction and an entropic driving force from the release of small counterions from the electric double layer and water molecules from hydrophobic surroundings. A high local charge density, at low ionic strength results in complex formation dominated by an enthalpic driving force. A low local charge density gives a more even distribution between enthalpic and entropic contributions. An increase in ionic strength decreases the enthalpic contribution, with a relative increase in the entropic contribution, supporting the idea of water release from hydrophobic surroundings.
Adsorption from β-lg–pectin mixtures to a hydrophobic surface leads to low adsorption rates due to a low concentration of free protein. Sequential adsorption of β-lg and pectin shows that low overall charge pectin protrudes more into the solution than high overall charge pectin, resulting in a more negative ζ-potential for low overall charge pectin. After sequential adsorption, β-lg is most stable against wash-out with a terminal pectin layer.