Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode

A new 3-dimensional (3D) network of crosslinked Horseradish Peroxidase/Carbon Nanotube (HRP/CNT) on a thiol-modified Au surface has been described in order to build up the effective electrical wiring of the enzyme units with the electrode. The synthesized 3D HRP/CNT network has been characterized wi...

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Main Authors:	A. K. M., Kafi, Naqshabandi, M., M. M., Yusoff, Crossley, Maxwell J.
Format:	Article
Language:	English
Published:	Elsevier 2018
Subjects:	Q Science (General)
Online Access:	http://umpir.ump.edu.my/id/eprint/19746/ http://umpir.ump.edu.my/id/eprint/19746/ http://umpir.ump.edu.my/id/eprint/19746/ http://umpir.ump.edu.my/id/eprint/19746/1/Improved%20peroxide%20biosensor%20based%20on%20Horseradish%20Peroxidase.pdf

id	ump-19746
recordtype	eprints
spelling	ump-197462019-04-09T03:47:21Z http://umpir.ump.edu.my/id/eprint/19746/ Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode A. K. M., Kafi Naqshabandi, M. M. M., Yusoff Crossley, Maxwell J. Q Science (General) A new 3-dimensional (3D) network of crosslinked Horseradish Peroxidase/Carbon Nanotube (HRP/CNT) on a thiol-modified Au surface has been described in order to build up the effective electrical wiring of the enzyme units with the electrode. The synthesized 3D HRP/CNT network has been characterized with cyclic voltammetry and amperometry which results the establishment of direct electron transfer between the redox active unit of HRP and the Au surface. Electrochemical measurements reveal that the high biological activity and stability is exhibited by the immobilized HRP and a quasi-reversible redox peak of the redox centre of HRP was observed at about −0.355 and −0.275 V vs. Ag/AgCl. The electron transfer rate constant, KS and electron transfer co-efficient α were found as 0.57 s−1 and 0.42, respectively. Excellent electrocatalytic activity for the reduction of H2O2 was exhibited by the developed biosensor. The proposed biosensor modified with HRP/CNT 3D network displays a broader linear range and a lower detection limit for H2O2 determination. The linear range is from 1.0 × 10−7 to 1.2 × 10−4 M with a detection limit of 2.2.0 × 10−8 M at 3 σ. The Michaelies–Menten constant Kapp M value is estimated to be 0.19 mM. Moreover, this biosensor exhibits very high sensitivity, good reproducibility and long-time stability. Elsevier 2018-11-14 Article PeerReviewed application/pdf en http://umpir.ump.edu.my/id/eprint/19746/1/Improved%20peroxide%20biosensor%20based%20on%20Horseradish%20Peroxidase.pdf A. K. M., Kafi and Naqshabandi, M. and M. M., Yusoff and Crossley, Maxwell J. (2018) Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode. Enzyme and Microbial Technology, 113. pp. 67-74. ISSN 0141-0229 https://doi.org/10.1016/j.enzmictec.2017.11.006 https://doi.org/10.1016/j.enzmictec.2017.11.006
repository_type	Digital Repository
institution_category	Local University
institution	Universiti Malaysia Pahang
building	UMP Institutional Repository
collection	Online Access
language	English
topic	Q Science (General)
spellingShingle	Q Science (General) A. K. M., Kafi Naqshabandi, M. M. M., Yusoff Crossley, Maxwell J. Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode
description	A new 3-dimensional (3D) network of crosslinked Horseradish Peroxidase/Carbon Nanotube (HRP/CNT) on a thiol-modified Au surface has been described in order to build up the effective electrical wiring of the enzyme units with the electrode. The synthesized 3D HRP/CNT network has been characterized with cyclic voltammetry and amperometry which results the establishment of direct electron transfer between the redox active unit of HRP and the Au surface. Electrochemical measurements reveal that the high biological activity and stability is exhibited by the immobilized HRP and a quasi-reversible redox peak of the redox centre of HRP was observed at about −0.355 and −0.275 V vs. Ag/AgCl. The electron transfer rate constant, KS and electron transfer co-efficient α were found as 0.57 s−1 and 0.42, respectively. Excellent electrocatalytic activity for the reduction of H2O2 was exhibited by the developed biosensor. The proposed biosensor modified with HRP/CNT 3D network displays a broader linear range and a lower detection limit for H2O2 determination. The linear range is from 1.0 × 10−7 to 1.2 × 10−4 M with a detection limit of 2.2.0 × 10−8 M at 3 σ. The Michaelies–Menten constant Kapp M value is estimated to be 0.19 mM. Moreover, this biosensor exhibits very high sensitivity, good reproducibility and long-time stability.
format	Article
author	A. K. M., Kafi Naqshabandi, M. M. M., Yusoff Crossley, Maxwell J.
author_facet	A. K. M., Kafi Naqshabandi, M. M. M., Yusoff Crossley, Maxwell J.
author_sort	A. K. M., Kafi
title	Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode
title_short	Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode
title_full	Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode
title_fullStr	Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode
title_full_unstemmed	Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode
title_sort	improved peroxide biosensor based on horseradish peroxidase/carbon nanotube on a thiol-modified gold electrode
publisher	Elsevier
publishDate	2018
url	http://umpir.ump.edu.my/id/eprint/19746/ http://umpir.ump.edu.my/id/eprint/19746/ http://umpir.ump.edu.my/id/eprint/19746/ http://umpir.ump.edu.my/id/eprint/19746/1/Improved%20peroxide%20biosensor%20based%20on%20Horseradish%20Peroxidase.pdf
first_indexed	2023-09-18T22:28:18Z
last_indexed	2023-09-18T22:28:18Z
_version_	1777416115202293760

Improved peroxide biosensor based on Horseradish Peroxidase/Carbon Nanotube on a thiol-modified gold electrode

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