Immobilization of lysozyme onto pore-engineered mesoporous AISBA-15.
In this research, hydrothermally stable mesoporous AISBA-15 materials have been used as adsorbents for systematic research on the lysozyme adsorption. Stability of the AISBA-15 adsorbents and the lysozyme molecules after the adsorption experiments for several days in aqueous solutions were confirmed by X-ray diffraction (XRD) measurement and FT-IR spectroscopy, respectively. The amount of the lysozyme adsorption can easily be controlled by the pore diameter and pore volume the mesoporous adsorbent, but an unreasonable effect of the surface area on the protein adsorption capacity was observed. The results of the effect of the pore diameter on the lysozyme adsorption suggest that the adsorption might partially be influenced by kinetically favorable edge-on type orientation on the confined mesopore. However, the final adsorption amount of the lysozyme can be well regenerated by models based on the side-on adsorption in dense packing. The present research also confirms the importance of appropriate "pore-engineering" for immobilization of bio-function on mesoporous materials.
Miyahara
Masahiko
M
Supermolecules Group, National Institute for Materials Science, 1-1 Namiki, Tsukuba 305-0044, Japan.
Vinu
Ajayan
A
Ariga
Katsuhiko
K
D000327:Adsorption; D000538:Aluminum Silicates / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods*; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties; D014961:X-Ray Diffraction
C505110:AISBA 15; D000538:Aluminum Silicates; D004800:Enzymes, Immobilized; D009113:Muramidase