Properties of protein solutes adsorbed on ceramic membrane by using a quartz-crystal microbalance (QCM) were evaluated
in situ. This frequency of piezoelectric AT-cut quartz resonator changed according to the amount of solute adsorbed on the quartz-crystal surface. Ceramic thin membrane, which was mainly titanium oxide (TiO
2), was coated on the QCM surface using sol-gel method. An adsorption behavior of bovine serum albumin (BSA) on the TiO
2-QCM was investigated.
The amount of BSA adsorption increased with increasing BSA concentration, and reached a maximum value near the isoelectric point of BSA solution. The cohesion force acting among BSA molecules was considered to become strongest because the electrostatic repulsion force was weakened, and then the BSA molecules were accumulated by adsorption onto the membrane surface. A higher ionic strength gave a lower BSA adsorption at a pH near the isoelectric point. The pH at maximum adsorption of BSA in a high ionic strength shifted to a more acidic pH than that in a low ionic strength. The adsorption amount of BSA increased by hydrophobilization of TiO
2 surface. The equilibrium amount of BSA adsorbed at pH4.8 could be expressed by a Freundlich type's adsorption isotherm.
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