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Access Type
Campus Access
Document Type
thesis
Degree Program
Chemistry
Degree Type
Master of Science (M.S.)
Year Degree Awarded
2014
Month Degree Awarded
February
Keywords
Coacervation, Hetero-Protein Coacervation, Protein-Protein Interactions, Complex Equilibrium, Lactoferrin, β-lactoglobulin
Abstract
Coacervation between the milk proteins β-lactoglobulin (BLG) and Lactoferrin (LF) was studied as a model system for hetero-protein coacervation (HPC). Equilibria among BLG/LF complexes and the corresponding speciation were found to control coacervation, which can be quantitatively monitored by turbidimetry. Several methods were used to assess complexation as a function of LF : BLG (mol/mol) mixing ratio (r). Proton release, calculated from a shift in pH when LF is added to BLG, was used to identify regions of complexation. Dynamic light scattering (DLS) was used to determine regions of complexation by relating complex size to stoichiometry. Isothermal titration calorimetry (ITC) was used to measure enthalpies of binding upon addition of LF to BLG. These results are used to show that coacervation is related to speciation, with the LF(BLG2)2 complex as the coacervating species.
DOI
https://doi.org/10.7275/4702015
First Advisor
Paul L Dubin