Amperometric sensors based on tyro sinase-modified screenprinted arrays
(2003) In Talanta 61(4). p.473-483- Abstract
- This paper describes the design, development and characteristics of a tyrosinase (polyphenol oxidase) modified amperometric screen-printed biosensor array, with the enzyme cross-linked in a redox-hydrogel namely the PVI13-dmeOs polymer. Two types of Au-screen-printed four-channel electrode arrays, differing in design and insulating layer, were compared and investigated. Au-, graphite-coated-Au- and Carbopack C-coated-Au-surfaces, serving as the basis for tyrosinase immobilisation, were investigated and the performances of the different arrays were evaluated and compared in terms of their electrocatalytic characteristics, as well as operational- and storage stability using catechol as model substrate. It was found that the Carbopack... (More)
- This paper describes the design, development and characteristics of a tyrosinase (polyphenol oxidase) modified amperometric screen-printed biosensor array, with the enzyme cross-linked in a redox-hydrogel namely the PVI13-dmeOs polymer. Two types of Au-screen-printed four-channel electrode arrays, differing in design and insulating layer, were compared and investigated. Au-, graphite-coated-Au- and Carbopack C-coated-Au-surfaces, serving as the basis for tyrosinase immobilisation, were investigated and the performances of the different arrays were evaluated and compared in terms of their electrocatalytic characteristics, as well as operational- and storage stability using catechol as model substrate. It was found that the Carbopack C-coated array was the best choice for tyrosinase immobilisation procedure mainly due to a higher mechanical stability of the deposited enzyme layer, combined with good sensitivity and stability for up to 6 months of use. In the batch mode the biosensors responded linearly to catechol up to 30 muM with limits of detection from 0.14 muM. Parameters from cyclic voltammograms indicated that the reversibility of the direct electrochemical reaction for catechol on the three types of electrode surfaces (no tyrosinase modification) was not the limiting factor for the construction and performance of tyrosinase biosensors. (C) 2003 Elsevier B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/294759
- author
- Sapelnikova, Svetlana LU ; Dock, Eva LU ; Ruzgas, Tautgirdas LU and Emnéus, Jenny LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- screen-printed arrays, tyrosinase, amperometric biosensor
- in
- Talanta
- volume
- 61
- issue
- 4
- pages
- 473 - 483
- publisher
- Elsevier
- external identifiers
-
- wos:000186557500008
- pmid:18969209
- scopus:0242390203
- ISSN
- 1873-3573
- DOI
- 10.1016/S0039-9140(03)00314-X
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004)
- id
- 3e0978d9-489e-4a3c-be49-b1f2b9725b2c (old id 294759)
- date added to LUP
- 2016-04-01 15:56:07
- date last changed
- 2022-01-28 08:06:07
@article{3e0978d9-489e-4a3c-be49-b1f2b9725b2c,
abstract = {{This paper describes the design, development and characteristics of a tyrosinase (polyphenol oxidase) modified amperometric screen-printed biosensor array, with the enzyme cross-linked in a redox-hydrogel namely the PVI13-dmeOs polymer. Two types of Au-screen-printed four-channel electrode arrays, differing in design and insulating layer, were compared and investigated. Au-, graphite-coated-Au- and Carbopack C-coated-Au-surfaces, serving as the basis for tyrosinase immobilisation, were investigated and the performances of the different arrays were evaluated and compared in terms of their electrocatalytic characteristics, as well as operational- and storage stability using catechol as model substrate. It was found that the Carbopack C-coated array was the best choice for tyrosinase immobilisation procedure mainly due to a higher mechanical stability of the deposited enzyme layer, combined with good sensitivity and stability for up to 6 months of use. In the batch mode the biosensors responded linearly to catechol up to 30 muM with limits of detection from 0.14 muM. Parameters from cyclic voltammograms indicated that the reversibility of the direct electrochemical reaction for catechol on the three types of electrode surfaces (no tyrosinase modification) was not the limiting factor for the construction and performance of tyrosinase biosensors. (C) 2003 Elsevier B.V. All rights reserved.}},
author = {{Sapelnikova, Svetlana and Dock, Eva and Ruzgas, Tautgirdas and Emnéus, Jenny}},
issn = {{1873-3573}},
keywords = {{screen-printed arrays; tyrosinase; amperometric biosensor}},
language = {{eng}},
number = {{4}},
pages = {{473--483}},
publisher = {{Elsevier}},
series = {{Talanta}},
title = {{Amperometric sensors based on tyro sinase-modified screenprinted arrays}},
url = {{http://dx.doi.org/10.1016/S0039-9140(03)00314-X}},
doi = {{10.1016/S0039-9140(03)00314-X}},
volume = {{61}},
year = {{2003}},
}