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

doi:10.1016/j.cap.2009.06.050

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

Department of Physics

Research output: Contribution to journal › Article › peer-review

31 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	e263-e265
Journal	Current Applied Physics
Volume	9
Issue number	4 SUPPL.
DOIs	https://doi.org/10.1016/j.cap.2009.06.050
Publication status	Published - 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)

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10.1016/j.cap.2009.06.050

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title = "Immobilization of horseradish peroxidase on multi-walled carbon nanotubes and its enzymatic stability",

abstract = "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{\texttrademark} - 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.",

author = "Kim, {Bum Joon} and Kang, {Bong Keun} and Bahk, {Young Yil} and Yoo, {Kyung Hwa} and Lim, {Kook Jin}",

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.",

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AU - Bahk, Young Yil

AU - Yoo, Kyung Hwa

AU - Lim, Kook Jin

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N2 - 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.

AB - 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.

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

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

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