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Influence of macroporous gold support and its functionalization on lactate oxidase-based biosensors response

Influence of macroporous gold support and its functionalization on lactate oxidase-based biosensors response
Influence of macroporous gold support and its functionalization on lactate oxidase-based biosensors response
A general bioanalytical platform for biosensor applications was developed based on three-dimensional ordered macroporous (3DOM) gold film modified electrodes using lactate oxidase (LOx) as a case study, within the framework of developing approaches of broad applicability. The electrode was electrochemically fabricated with an inverted opal template, making the surface area of the 3DOM gold electrode up to 18 times higher than that of bare flat gold electrodes. These new electrochemical transducers were characterized by using Field Emission Scanning Electron Microscopy (FE-SEM), Atomic Force Microscopy (AFM) and the X-ray diffraction (XRD). The biosensor was developed by immobilization of lactate oxidase (LOx), on a 3DOM gold electrode modified with a self-assembled monolayer of dithiobis-N-succinimidyl propionate (DTSP). The resulting lactate oxidase biosensor was characterized by electrochemical impedance spectroscopy (EIS). The 3DOM gold electrode not only provides a good biocompatible microenvironment but also promotes the increase of conductivity and stability. Thus, the developed lactate oxidase bioanalytical platforms showed higher mediated bioelectrocatalytic activity compared to others previously described based on polycrystalline gold transducers. The response to varying lactate concentrations has been obtained in the presence of hydroxymethylferrocene as redox mediator in solution. Under these conditions, the bioanalytical platform response for DTSP covalently bound enzyme was improved with respect to that obtained in absence of DTSP
0039-9140
328-334
Gamero, M.
66a0a836-854c-4b80-9034-43aed56914c5
Sosna, M.
36542c5a-56cc-413c-b99b-efc8493b19af
Pariente, F.
0d85db7d-3691-4dbd-b956-607027408d0a
Lorenzo, E.
7f375f69-8b89-4a9c-9fb4-cfdec9e26697
Bartlett, P.N.
d99446db-a59d-4f89-96eb-f64b5d8bb075
Alonso, C.
a03464fe-d027-4425-a631-d76db905ccf7
Gamero, M.
66a0a836-854c-4b80-9034-43aed56914c5
Sosna, M.
36542c5a-56cc-413c-b99b-efc8493b19af
Pariente, F.
0d85db7d-3691-4dbd-b956-607027408d0a
Lorenzo, E.
7f375f69-8b89-4a9c-9fb4-cfdec9e26697
Bartlett, P.N.
d99446db-a59d-4f89-96eb-f64b5d8bb075
Alonso, C.
a03464fe-d027-4425-a631-d76db905ccf7

Gamero, M., Sosna, M., Pariente, F., Lorenzo, E., Bartlett, P.N. and Alonso, C. (2012) Influence of macroporous gold support and its functionalization on lactate oxidase-based biosensors response. Talanta, 94, 328-334. (doi:10.1016/j.talanta.2012.03.051).

Record type: Article

Abstract

A general bioanalytical platform for biosensor applications was developed based on three-dimensional ordered macroporous (3DOM) gold film modified electrodes using lactate oxidase (LOx) as a case study, within the framework of developing approaches of broad applicability. The electrode was electrochemically fabricated with an inverted opal template, making the surface area of the 3DOM gold electrode up to 18 times higher than that of bare flat gold electrodes. These new electrochemical transducers were characterized by using Field Emission Scanning Electron Microscopy (FE-SEM), Atomic Force Microscopy (AFM) and the X-ray diffraction (XRD). The biosensor was developed by immobilization of lactate oxidase (LOx), on a 3DOM gold electrode modified with a self-assembled monolayer of dithiobis-N-succinimidyl propionate (DTSP). The resulting lactate oxidase biosensor was characterized by electrochemical impedance spectroscopy (EIS). The 3DOM gold electrode not only provides a good biocompatible microenvironment but also promotes the increase of conductivity and stability. Thus, the developed lactate oxidase bioanalytical platforms showed higher mediated bioelectrocatalytic activity compared to others previously described based on polycrystalline gold transducers. The response to varying lactate concentrations has been obtained in the presence of hydroxymethylferrocene as redox mediator in solution. Under these conditions, the bioanalytical platform response for DTSP covalently bound enzyme was improved with respect to that obtained in absence of DTSP

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Published date: 30 May 2012
Organisations: Electrochemistry

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Local EPrints ID: 349755
URI: http://eprints.soton.ac.uk/id/eprint/349755
ISSN: 0039-9140
PURE UUID: 71b2ac21-577e-4ff3-bfa7-02dd888e8395
ORCID for P.N. Bartlett: ORCID iD orcid.org/0000-0002-7300-6900

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Date deposited: 08 Mar 2013 17:42
Last modified: 15 Mar 2024 02:44

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Contributors

Author: M. Gamero
Author: M. Sosna
Author: F. Pariente
Author: E. Lorenzo
Author: P.N. Bartlett ORCID iD
Author: C. Alonso

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