Paul L DubinFlanagan, Sean E2024-04-262013-10-122014-020210.7275/4702015https://hdl.handle.net/20.500.14394/44622Coacervation 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.CoacervationHetero-Protein CoacervationProtein-Protein InteractionsComplex EquilibriumLactoferrinβ-lactoglobulinAnalytical ChemistryBiochemistryFood ChemistryPhysical ChemistryPolymer ChemistryThesis (Campus Access Only)