Adsorption kinetic data recorded for α-lactalbumin, β-casein, β-lactoglobulin, bovine
serum albumin and lysozyme at silianized silica surfaces of low and high hydrophobicity,
along with a simple model for adsorption and surfactant-mediated elution of protein, were
used to analyze the removal of each protein by sodium dodecylsulfate (SDS) and
dodecyltrimethylammonium bromide (DTAB) at each surface. The model relates
resistance to surfactant elution to two rate constants: one governing conversion of
removable protein to a nonremovable form (s₁), and one governing removal of protein by
the surfactant (k [subscript s]). Elution of each protein from hydrophobic silica with SDS was
interpreted as providing information relevant to protein-surface binding strength, or si;
i.e., protein-specific differences in removal were a result of SDS adsorption to the surface
and displacement of surface-bound protein, as opposed to solubilization driven by SDS
binding to the protein. SDS-mediated removal of protein from surfaces of lower
hydrophobicity were interpreted as generally proceeding according to a similar,
displacement mechanism. The model indicated that data recorded for DTAB-mediated
elution at each surface were generally less representative of protein-surface behavior, and
more a function of k [subscript s], where differences in surfactant attachment to protein and
solubilization appeared to play an important role in protein removal. Under controlled
conditions use of the model would allow identification of cases where k [subscript s] in particularly
protein specific, and illustrates the point that in such cases surfactant-mediated elution of a
protein may reveal little about its surface behavior. / Graduation date: 1996
| Identifer | oai:union.ndltd.org:ORGSU/oai:ir.library.oregonstate.edu:1957/25993 |
| Date | 27 September 1995 |
| Creators | Vinaraphong, Pravina |
| Contributors | McGuire, Joseph |
| Source Sets | Oregon State University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
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