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Tobacco peroxidase as a new reagent for amperometric biosensors

Gazaryan, I G; Gorton, Lo LU ; Ruzgas, Tautgirdas LU ; Csöregi, Elisabeth LU ; Schuhmann, W; Lagrimini, L M; Khushpul'yan, D M and Tishkov, V I (2005) In Journal of Analytical Chemistry 60(6). p.558-566
Abstract
The results of testing a new enzyme, anionic tobacco peroxidase (TOP), in various amperometric biosensors are summarized. The biochemical and electrochemical properties of the enzyme are briefly characterized. As compared to the commonly used cationic peroxidase from horseradish roots, TOP exhibits a wider optimum stability pH range, higher stability to inactivation with hydrogen peroxide, and higher efficiency in direct electron-transfer processes. The enzyme immobilized by adsorption on graphite is effective in determining aminophenols and aromatic diamines under flow conditions with a detection limit of 10 nM. Upon immobilization on graphite by incorporation into a get of a redox-active polymer (crosslinked polyvinylimidazole with... (More)
The results of testing a new enzyme, anionic tobacco peroxidase (TOP), in various amperometric biosensors are summarized. The biochemical and electrochemical properties of the enzyme are briefly characterized. As compared to the commonly used cationic peroxidase from horseradish roots, TOP exhibits a wider optimum stability pH range, higher stability to inactivation with hydrogen peroxide, and higher efficiency in direct electron-transfer processes. The enzyme immobilized by adsorption on graphite is effective in determining aminophenols and aromatic diamines under flow conditions with a detection limit of 10 nM. Upon immobilization on graphite by incorporation into a get of a redox-active polymer (crosslinked polyvinylimidazole with osmium 4,4'-dimethylbipyridinium chloride), TOP exhibited sensitivity and stability comparable to those of horseradish peroxidase and a wider linearity range. Upon immobilization on a self-assembled thiol monolayer at a gold electrode, TOP was much superior to horseradish peroxidase in the sensitivity of determining hydrogen peroxide, regardless of the charge of the monolayer. Prospects for the further use of the native enzyme and its genetically engineered unglycosylated form are considered. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Analytical Chemistry
volume
60
issue
6
pages
558 - 566
publisher
MAIK Nauka/Interperiodica
external identifiers
  • wos:000229909800013
  • scopus:21544465904
ISSN
1608-3199
DOI
10.1007/s10809-005-0139-1
language
English
LU publication?
yes
id
ccf2a74f-1da9-44af-a278-e40e4cc842d9 (old id 151014)
date added to LUP
2007-06-26 16:20:08
date last changed
2017-08-20 03:29:56
@article{ccf2a74f-1da9-44af-a278-e40e4cc842d9,
  abstract     = {The results of testing a new enzyme, anionic tobacco peroxidase (TOP), in various amperometric biosensors are summarized. The biochemical and electrochemical properties of the enzyme are briefly characterized. As compared to the commonly used cationic peroxidase from horseradish roots, TOP exhibits a wider optimum stability pH range, higher stability to inactivation with hydrogen peroxide, and higher efficiency in direct electron-transfer processes. The enzyme immobilized by adsorption on graphite is effective in determining aminophenols and aromatic diamines under flow conditions with a detection limit of 10 nM. Upon immobilization on graphite by incorporation into a get of a redox-active polymer (crosslinked polyvinylimidazole with osmium 4,4'-dimethylbipyridinium chloride), TOP exhibited sensitivity and stability comparable to those of horseradish peroxidase and a wider linearity range. Upon immobilization on a self-assembled thiol monolayer at a gold electrode, TOP was much superior to horseradish peroxidase in the sensitivity of determining hydrogen peroxide, regardless of the charge of the monolayer. Prospects for the further use of the native enzyme and its genetically engineered unglycosylated form are considered.},
  author       = {Gazaryan, I G and Gorton, Lo and Ruzgas, Tautgirdas and Csöregi, Elisabeth and Schuhmann, W and Lagrimini, L M and Khushpul'yan, D M and Tishkov, V I},
  issn         = {1608-3199},
  language     = {eng},
  number       = {6},
  pages        = {558--566},
  publisher    = {MAIK Nauka/Interperiodica},
  series       = {Journal of Analytical Chemistry},
  title        = {Tobacco peroxidase as a new reagent for amperometric biosensors},
  url          = {http://dx.doi.org/10.1007/s10809-005-0139-1},
  volume       = {60},
  year         = {2005},
}