Off-campus UMass Amherst users: To download campus access theses, please use the following link to log into our proxy server with your UMass Amherst user name and password.

Non-UMass Amherst users: Please talk to your librarian about requesting this thesis through interlibrary loan.

Theses that have an embargo placed on them will not be available to anyone until the embargo expires.

Access Type

Campus Access

Document Type


Degree Program


Degree Type

Master of Science (M.S.)

Year Degree Awarded


Month Degree Awarded



Coacervation, Hetero-Protein Coacervation, Protein-Protein Interactions, Complex Equilibrium, Lactoferrin, β-lactoglobulin


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