4.4 Article

Biological functionality of active enzyme structures immobilized on various solid surfaces

期刊

CURRENT APPLIED PHYSICS
卷 9, 期 6, 页码 1454-1458

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.cap.2009.03.023

关键词

Biological functionality; HRP; Biotin-avidin interaction; Non-specific adsorption; LBL assembly

资金

  1. MEST [2008-00656]
  2. KRF [KRF-2008-005-J00703]
  3. KOSEF [R31-2008-000-10029-0]
  4. Ministry of Education, Science & Technology (MoST), Republic of Korea [2008-00656] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
  5. National Research Foundation of Korea [2008-005-J00703] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

向作者/读者索取更多资源

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. (C) 2009 Elsevier B.V. All rights reserved.

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