Abstract
Adsorption kinetics of myoglobin on silica was investigated using the quartz crystal microbalance (QCM) and the optical waveguide light-mode spectroscopy (OWLS). Measurements were carried out for the NaCl concentration of 0.01 M and 0.15 M. A quantitative analysis of the kinetic adsorption and desorption runs acquired from QCM allowed to determine the maximum coverage of irreversibly bound myoglobin molecules. At a pH of 3.5-4 this was equal to 0.60 mg m(-2) and 1.3 mg m(-2) for a NaCl concentration of 0.01 M and 0.15 M, respectively, which agrees with the OWLS measurements. The latter value corresponds to the closely packed monolayer of molecules predicted from the random sequential adsorption approach. The fraction of reversibly bound protein molecules and their biding energy were also determined. It is observed that at larger pHs, the myoglobin adsorption kinetics was much slower. This behavior was attributed to the vanishing net charge that decreased the binding energy of molecules with the substrate. These results can be exploited to develop procedures for preparing myoglobin layers at silica substrates of well-controlled coverage useful for biosensing purposes.