Immobilization of horseradish peroxidase on multi-walled carbon nanotubes and its enzymatic stability

Bum Joon Kim, Bong Keun Kang, Young Yil Bahk, Kyung Hwa Yoo, Kook Jin Lim

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)


We here demonstrate the use of multi-walled carbon nanotubes (MWNTs) as a platform matrix for immunoassay using horseradish peroxidase (HRP) as a model protein. After immobilization of HRP onto MWNTs using 1-pyrenebutanoic acid, succinimidyl ester as a cross-linker, the protein-loading capacity of MWNTs was determined by measuring the enzyme activity of immobilized HRP. We also compared the protein binding capacity of MaxiSorp™ - a commercially available polystyrene based microplate - with that of MWNTs. In addition, we assayed the enzyme activity of immobilized HRP in various pH or at high temperature (90 °C) in order to examine whether the stability of the immobilized HRP in harsh environments would be changed depending upon the polymer used as a matrix.

Original languageEnglish
Pages (from-to)e263-e265
JournalCurrent Applied Physics
Issue number4 SUPPL.
Publication statusPublished - 2009 Jul

Bibliographical note

Funding Information:
This work has been supported by grants from National Core Research Center for Nano Medical Technology, Yonsei University (Grant R15-2004-024-02002-0). We would like to thank Young Wook Chang for helpful discussion.

All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Physics and Astronomy(all)


Dive into the research topics of 'Immobilization of horseradish peroxidase on multi-walled carbon nanotubes and its enzymatic stability'. Together they form a unique fingerprint.

Cite this