Biological functionality of active enzyme structures immobilized on various solid surfaces

다국어 초록 (Multilingual Abstract)

We have investigated biological functionality of immobilized enzyme structures according to the immobilizing
routes and the surface properties. Horse radish peroxidase (HRP) was immobilized on various
solid surfaces such as gold, SiO2, sapphire and anodized aluminum oxide (AAO) membrane via non-specific
adsorption, avidin-mediated and biotin/avidin-mediated layer-by-layer (LBL) assembly. The catalytic
activity as a measure of biological functionality, of the biotin-HRP immobilized by avidin-mediated LBL
assembly was found to be better than that of the directly adsorbed HRP on the surfaces of gold, SiO2, sapphire
and AAO due to the easy accessibility of reactants to active sites as well as the retention of three
dimensional native structure of enzyme for bioactive functionality. In addition, the catalytic activity of
the biotin-HRP in LBL-assembled avidin/biotin-HRP on AAO membrane was found to be highly better
than that on other substrates due to the increasing amount of immobilized HRP which can be attributed
to the high surface area of the substrate. SEM images show that the functional avidin/biotin-HRP enzyme
structures were successfully realized by a sequential process of non-specific adsorption and LBL assembly
via biotin–avidin interaction.

참고문헌 (Reference)

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