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Amperometric sensors based on tyro sinase-modified screenprinted arrays

Sapelnikova, Svetlana LU ; Dock, Eva LU ; Ruzgas, Tautgirdas LU and Emnéus, Jenny LU (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)
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author
organization
publishing date
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
id
3e0978d9-489e-4a3c-be49-b1f2b9725b2c (old id 294759)
date added to LUP
2007-09-21 10:32:52
date last changed
2018-01-07 08:54:09
@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},
  keyword      = {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},
  volume       = {61},
  year         = {2003},
}