The effect of pH and ionic strength on the equilibrium adsorptive
behavior of β-lactoglobulin onto hydrophobic and hydrophilic
silicon surfaces was studied using ellipsometry. Plots of amount
adsorbed (μg protein/cm²) as a function of protein concentration
(mg/ml) exhibited attainment of plateau values beyond a protein
concentration of 0.250 mg/ml. At a given pH and ionic strength,
plateau values associated with hydrophobic surfaces were observed
to be greater than those associated with hydrophilic surfaces.
The Langmuir adsorption isotherm was chosen as the most
appropriate model to represent the data and was used to compare
results obtained under different experimental conditions. Effects of
pH and ionic strength on protein adsorption at hydrophilic surfaces
indicate that electrostatics played a major role, while pH and ionic
strength effects on adsorption to hydrophobic surfaces reflect a
greater importance of nonelectrostatic interactions. / Graduation date: 1991
| Identifer | oai:union.ndltd.org:ORGSU/oai:ir.library.oregonstate.edu:1957/38143 |
| Date | 15 May 1990 |
| Creators | Luey, Ja-Kael |
| Contributors | Sproull, Robert D., McGuire, Joseph |
| Source Sets | Oregon State University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
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