Please use this identifier to cite or link to this item:
https://doi.org/10.1016/j.bios.2003.08.010
DC Field | Value | |
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dc.title | Enzymatic activity of glucose oxidase covalently wired via viologen to electrically conductive polypyrrole films | |
dc.contributor.author | Liu, X. | |
dc.contributor.author | Neoh, K.G. | |
dc.contributor.author | Cen, L. | |
dc.contributor.author | Kang, E.T. | |
dc.date.accessioned | 2014-06-17T07:40:22Z | |
dc.date.available | 2014-06-17T07:40:22Z | |
dc.date.issued | 2004-03-15 | |
dc.identifier.citation | Liu, X., Neoh, K.G., Cen, L., Kang, E.T. (2004-03-15). Enzymatic activity of glucose oxidase covalently wired via viologen to electrically conductive polypyrrole films. Biosensors and Bioelectronics 19 (8) : 823-834. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bios.2003.08.010 | |
dc.identifier.issn | 09565663 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/63857 | |
dc.description.abstract | The surface functionalization of an electrically conductive polypyrrole film (PPY) with a viologen, (N-(2-carboxyl-ethyl)-N′-(4-vinylbenzyl)-4, 4′-bipyridinium dichloride, or CVV) for the covalent immobilization of glucose oxidase (GOD) has been carried out. The viologen was first synthesized and graft polymerized on PPY film. It then served as an anchor via its carboxyl groups for the covalent immobilization of GOD. The surface composition of the as-functionalized substrates was characterized by X-ray photoelectron spectroscopy (XPS). The effects of the CVV monomer concentration on the CVV-graft polymer concentration and the amount of GOD immobilized on the surface were investigated. The activity of the immobilized GOD was compared with that of free GOD and the kinetic effects were also obtained. The cyclic voltammetric (CV) response of the GOD-functionalized PPY substrates was studied in a phosphate buffer solution under an argon atmosphere. The CV results support the mechanism in which CVV acts as a mediator to transfer electron between the electrode and enzyme, and hence regenerating the enzyme in the enzymatic reaction with glucose. High sensitivity and linear response of the enzyme electrode was observed with glucose concentration ranging from 0 to 20mM. © 2003 Elsevier B.V. All rights reserved. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bios.2003.08.010 | |
dc.source | Scopus | |
dc.subject | Covalent immobilization | |
dc.subject | Electrical wiring of enzyme | |
dc.subject | Glucose oxidase | |
dc.subject | Polypyrrole | |
dc.subject | Viologen | |
dc.type | Article | |
dc.contributor.department | CHEMICAL & BIOMOLECULAR ENGINEERING | |
dc.description.doi | 10.1016/j.bios.2003.08.010 | |
dc.description.sourcetitle | Biosensors and Bioelectronics | |
dc.description.volume | 19 | |
dc.description.issue | 8 | |
dc.description.page | 823-834 | |
dc.description.coden | BBIOE | |
dc.identifier.isiut | 000189220900006 | |
Appears in Collections: | Staff Publications |
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