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Biological Functionality of Active Enzyme Structures Immobilized on Various Solid Surfaces by Dong Chung Kim; A-Rang Jang; Dae Joon Kang is a Materials Science article available to read on EtoBox.

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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, SiO 2 , 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, SiO 2 , 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 n

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Author

Dong Chung Kim; A-Rang Jang; Dae Joon Kang

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1567-1739)

Published

2009

Language

EN

Field

Materials Science (Physical Sciences)