| Abstract
| - The amounts of negatively charged bovine serum albumin and positively charged lysozyme adsorbed onalumina, silica, titania, and zirconia particles (diameters 73 to 271 nm) in aqueous suspensions are measured.The adsorbed proteins change the ζ potentials and the isoelectric points (IEP) of the oxide particles. Theadded to adsorbed protein ratios at pH 7.5 are compared with the protein treated particle ζ potentials. It isfound that the amounts of adsorbed proteins on the alumina, silica, and titania (but not on the zirconia)particle surfaces are highly correlated with the ζ potential. For the slightly less hydrophilic zirconia particleshigh amounts of protein adsorption are observed even under repulsive electrostatic conditions. One reasoncould be that the hydrophobic effect plays a more important role for zirconia than electrostatic interaction.
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