The adsorption equilibrium and kinetic behavior exhibited
by β-lactoglobulin at silanized silicon surfaces of varying
hydrophobicity were examined using ellipsometry. Adsorption
equilibrium results were used to construct adsorption
isotherms; the adsorbed mass of β-lactoglobulin was observed
to increase with increasing surface hydrophobicity, within a
defined range of hydrophobicity. Adsorption kinetics recorded
for β-lactoglobulin on each surface were compared to the
kinetic behavior predicted by a simple model for protein
adsorption. The model described the data well in all cases,
enabling interpretation of the kinetic behavior in terms of
contact surface hydrophobicity influences on rate constants
affecting protein attachment and unfolding at the interface.
In particular, both experimental and simulation results seem
to be in support of a hypothesis that rate constants defining
protein arrival and conversion to an irreversibly adsorbed
state increase with increasing surface hydrophobicity, while
the rate constant defining desorption of protein from a
reversibly adsorbed state decreases with increasing surface
hydrophobicity. Contact surface hydrophobicity was quantified
using contact angle analysis to determine the polar component
of the work required to remove water from unit area of
surface. Quantitative consideration of possible mass transfer
influences on the observed adsorption rates supports the
notion that the experiments were not conducted in a transport-limited
regime; i.e., true kinetics were measured. / Graduation date: 1992
| Identifer | oai:union.ndltd.org:ORGSU/oai:ir.library.oregonstate.edu:1957/36056 |
| Date | 11 December 1991 |
| Creators | Krisdhasima, Viwat |
| Contributors | McGuire, J., Sproull, R.D. |
| Source Sets | Oregon State University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
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