An effective surface design based on a conjugated polymer and silver nanowires for the detection of paraoxon in tap water and milk

Date

2016-06-02

Author

Turan, Janset
Kesik, Melis
SÖYLEMEZ, SANİYE
Goker, Seza
Coskun, Sahin
Ünalan, Hüsnü Emrah
Toppare, Levent Kamil

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

10
views

0
downloads

Cite This

In this study, a novel approach for the fabrication of a biosensor utilizing a conducting polymer and silver nanowires is reported. To obtain immobilization platform for butyrylcholinesterase (BChE), a graphite electrode was modified with the poly(5,6-bis(octyloxy)-4,7-di(thieno[3][3,2-b]thiophen-2yl)benzo[c][1,2,5]oxoadiazole) (PTTBO) which has a hydrophobic alkyl chain as the pendant group providing hydrophobic nature to the matrix. Since biomolecules contain both hydrophobic and hydrophilic parts in their structure, alkyl chains interact with the proteins which provide an enhanced stability. Biosensor performance was improved through the deposition of silver nanowires on the polymer coated surfaces which enhances the charge transfer rate. This enabled the development of rapid, highly sensitive and stable amperometric sensors for the quantitative determination of organophosphorus pesticide; paraoxon. Fabricated biosensor showed two linear ranges between 0.5-8 mu M and 10-120 mu M with a low detection limit of 0.212 mu M when butyryl thiocholine iodide is used as the substrate. Surface modifications were monitored by scanning electron microscope (SEM) and cyclic voltammetry (CV) techniques. Under optimal operational parameters, fabricated sensors were tested for paraoxon detection in milk and tap water based on the inhibition of the enzyme molecules, where recovery tests proved the applicability of the designed system.

Subject Keywords

Amperometric biosensor, Amperometric biosensor, Conducting polymer, Silver nanowire, Pesticide biosensor, Butyrylcholinesterase

URI

https://hdl.handle.net/11511/46597

Collections

Department of Metallurgical and Materials Engineering, Article