Tobacco peroxidase as a new reagent for amperometric biosensors
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/151014
- author
- 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
- organization
- publishing date
- 2005
- 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
- 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
- ccf2a74f-1da9-44af-a278-e40e4cc842d9 (old id 151014)
- date added to LUP
- 2016-04-01 11:40:49
- date last changed
- 2022-04-28 18:22:36
@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 = {{https://lup.lub.lu.se/search/files/2591851/625291.pdf}}, doi = {{10.1007/s10809-005-0139-1}}, volume = {{60}}, year = {{2005}}, }