Direct bioelectrocatalysis at carbon electrodes modified with quinohemoprotein alcohol dehydrogenase from Gluconobacter sp. 33
(2002) In Electroanalysis 14(1). p.43-49- Abstract
- A newly isolated, purified, and characterized PQQ-dependent alcohol dehydrogenase (a bacterial membrane-bound protein) was recently found to display a surprisingly large linear range and high selectivity towards ethanol when integrated into a conducting polymer network on a platinum electrode. These findings motivated us to study the enzyme when simply immobilized onto carbonaceous surfaces in order to establish its characteristics and suitability for sensor development, the sensor design being based on a direct-electron transfer pathway. Graphite rods and screen-printed electrodes were modified in two different ways, and were operated both in FIA and batch mode. The obtained biosensor characteristics were highly dependent on the sensor... (More)
- A newly isolated, purified, and characterized PQQ-dependent alcohol dehydrogenase (a bacterial membrane-bound protein) was recently found to display a surprisingly large linear range and high selectivity towards ethanol when integrated into a conducting polymer network on a platinum electrode. These findings motivated us to study the enzyme when simply immobilized onto carbonaceous surfaces in order to establish its characteristics and suitability for sensor development, the sensor design being based on a direct-electron transfer pathway. Graphite rods and screen-printed electrodes were modified in two different ways, and were operated both in FIA and batch mode. The obtained biosensor characteristics were highly dependent on the sensor architecture, the highest sensitivity (179 mA M-1 cm(-2)) and lowest detection limit (1 muM) being obtained for screen-printed electrodes used in a batch mode. A mechanism of the observed direct electron transfer between the enzyme's active center and the electrode is proposed. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/343909
- author
- Razumiene, J ; Niculescu, M ; Ramanavicius, A ; Laurinavicius, V and Csöregi, Elisabeth LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- screen-printed electrode, bioelectrocatalysis, PQQ-dependent alcohol dehydrogenase
- in
- Electroanalysis
- volume
- 14
- issue
- 1
- pages
- 43 - 49
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000173607000006
- scopus:0036162632
- ISSN
- 1040-0397
- DOI
- 10.1002/1521-4109(200201)14:1<43::AID-ELAN43>3.0.CO;2-5
- 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: Department of Chemistry (011001220), Analytical Chemistry (S/LTH) (011001004)
- id
- d8990ea5-dcc5-4859-bb42-1fbb8d91f6e9 (old id 343909)
- date added to LUP
- 2016-04-01 15:29:24
- date last changed
- 2022-01-28 05:38:05
@article{d8990ea5-dcc5-4859-bb42-1fbb8d91f6e9,
abstract = {{A newly isolated, purified, and characterized PQQ-dependent alcohol dehydrogenase (a bacterial membrane-bound protein) was recently found to display a surprisingly large linear range and high selectivity towards ethanol when integrated into a conducting polymer network on a platinum electrode. These findings motivated us to study the enzyme when simply immobilized onto carbonaceous surfaces in order to establish its characteristics and suitability for sensor development, the sensor design being based on a direct-electron transfer pathway. Graphite rods and screen-printed electrodes were modified in two different ways, and were operated both in FIA and batch mode. The obtained biosensor characteristics were highly dependent on the sensor architecture, the highest sensitivity (179 mA M-1 cm(-2)) and lowest detection limit (1 muM) being obtained for screen-printed electrodes used in a batch mode. A mechanism of the observed direct electron transfer between the enzyme's active center and the electrode is proposed.}},
author = {{Razumiene, J and Niculescu, M and Ramanavicius, A and Laurinavicius, V and Csöregi, Elisabeth}},
issn = {{1040-0397}},
keywords = {{screen-printed electrode; bioelectrocatalysis; PQQ-dependent alcohol dehydrogenase}},
language = {{eng}},
number = {{1}},
pages = {{43--49}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Electroanalysis}},
title = {{Direct bioelectrocatalysis at carbon electrodes modified with quinohemoprotein alcohol dehydrogenase from Gluconobacter sp. 33}},
url = {{http://dx.doi.org/10.1002/1521-4109(200201)14:1<43::AID-ELAN43>3.0.CO;2-5}},
doi = {{10.1002/1521-4109(200201)14:1<43::AID-ELAN43>3.0.CO;2-5}},
volume = {{14}},
year = {{2002}},
}