Adsorption of proteins occurs on a variety of solid-liquid interfaces. There are many instances where the protein adsorption is desirable, whereas in many instances it results in undesirable effects. Surface-induced thrombosis due to adsorption of plasma proteins, fouling of membranes used in food and beverage processing, and performance degradation in analytical protein liquid chromatography are some of the undesirable effects of protein adsorption (1). In this work Bovine Serum Albumin Adsorption (BSA) was investigated on two surfaces, namely TiO₂ and SiO₂. The adsorption equilibrium and kinetic experiments were studied for 20, 30 and 40°C at solution pH of 4, 5 and 10. The experimental adsorption equilibrium data were compared with Langmuir and Freundlich adsorption isotherm models. It was observed that BSA has no appreciable adsorption onto SiO₂ over the temperature and solution pH range studied. The adsorption capacity of BSA on TiO₂ was highest at 40°C and at solution pH of 4. Adsorption of BSA on TiO₂ followed the first order kinetics. BSA adsorption was strongly affected by pH, the composition of the BSA solution, temperature, surface charge and the surface properties of the adsorbents.

REFERENCES

1.Bru, M.R., Giralt, F., Cohen, Y., "Protein adsorption onto zirconia modified with terminally grafted polyvinylpyrrolidone", Journal of Colloid and Interface Science, 235, 70-79 (2001).