Amperometric sensors based on tyro sinase-modified screenprinted arrays

Research output: Contribution to journalArticle

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.

Details

Authors
  • Svetlana Sapelnikova
  • Eva Dock
  • Tautgirdas Ruzgas
  • Jenny Emnéus
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Analytical Chemistry

Keywords

  • screen-printed arrays, tyrosinase, amperometric biosensor
Original languageEnglish
Pages (from-to)473-483
JournalTalanta
Volume61
Issue number4
Publication statusPublished - 2003
Publication categoryResearch
Peer-reviewedYes

Bibliographic note

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)