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Title: Surface functionalization of polypyrrole film with glucose oxidase and viologen
Authors: Cen, L. 
Neoh, K.G. 
Kang, E.T. 
Keywords: Covalent immobilization
Glucose oxidase
Surface functionalization
Issue Date: 1-Apr-2003
Citation: Cen, L., Neoh, K.G., Kang, E.T. (2003-04-01). Surface functionalization of polypyrrole film with glucose oxidase and viologen. Biosensors and Bioelectronics 18 (4) : 363-374. ScholarBank@NUS Repository.
Abstract: A surface modification technique was developed for the functionalization of polypyrrole (PPY) film with glucose oxidase (GOD) and viologen moieties. The PPY film was first graft copolymerized with acrylic acid (AAc) and GOD was then covalently immobilized through the amide linkage formation between the amino groups of the GOD and the carboxyl groups of the grafted AAc polymer chains in the presence of a water-soluble carbodiimide. Viologen moieties could also be attached to the PPY film via graft-copolymerization of vinyl benzyl chloride with the PPY film surface followed by reaction with 4,4′-bipyridine and α,α′-dichloro-p-xylene. X-ray photoelectron spectroscopy (XPS) was used to characterize the PPY films after each surface modification step. Increasing the AAc graft concentration would allow a greater amount of GOD to be immobilized but this would decrease the electrical conductivity of the PPY film. The activity of the immobilized GOD was compared with that of free GOD and the kinetic effects were also studied. The immobilized GOD was found to be less sensitive to temperature deactivation as compared to the free GOD. The results showed that the covalent immobilization technique offers advantages over the technique involving the entrapment of GOD in PPY films during electropolymerization. The presence of viologen in the vicinity of the immobilized GOD also enabled the GOD-catalyzed oxidation of glucose to proceed under UV irradiation in the absence of O2. © 2002 Elsevier Science B.V. All rights reserved.
Source Title: Biosensors and Bioelectronics
ISSN: 09565663
DOI: 10.1016/S0956-5663(02)00149-5
Appears in Collections:Staff Publications

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