Adsorption Behavior Of Lysozyme Research Articles

Use of Fourier Transform Infrared/Attenuated Total Reflectance Spectroscopy for the Study of Surface Adsorption of Proteins

The adsorption behavior of lysozyme and immunoglobulin G (IgG) onto a ZnSe crystal surface has been detected by the FT-IR/ATR technique. With this technique we are able to detect the protein adsorption process at a very low concentration (0.0005 mg/mL). The equation of Sperline et al. [Langmuir 3, 198 (1987)] was successfully applied to calculate the adsorption density of protein from an aqueous solution on a real-time basis. The monolayer formation of lysozyme was observed at a concentration range of 10−7 M to 10−5 M. A monolayer-to-multilayer adsorption transition of lysozyme was clearly observed from the adsorption isotherm plot at 35 μM. A differential adsorption density was observed for IgG that could be explained on the basis of its differential size and surface charge.

Photocontrolled adsorption chromatography for lysozyme using azoaromatic polymer

Photoresponsive polymeric adsorbents containing an azobenzene moiety were prepared, and adsorption behavior of lysozyme onto the adsorbents was studied. In the dark the amount of lysozyme adsorbed increased with increasing hydrophobicity of the surface of the adsorbents. Therefore, it is suggested that hydrophobic interaction between lysozyme and the adsorbents plays an important role in their adsorption behavior. On irradiation with UV light, the amount of lysozyme adsorbed decreased. This result is due to increased polarity of the surface of the adsorbent induced by UV irradiation and the resultant reduction in hydrophobic interaction with lysozyme. When a column chromatography of lysozyme was carried out using the photoresponsive polymeric adsorbent as a packing material, lysozyme was eluted by photoirradiation in a system using water as the single solvent.