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Document Type

Campus Access

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.

First Advisor

Paul L Dubin

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