Advanced

Investigation of graphite electrodes modified with cellobiose dehydrogenase from the ascomycete Myriococcum thermophilum

Harreither, Wolfgang ; Coman, Vasile LU ; Ludwig, Roland ; Haltrich, Dietmar and Gorton, Lo LU (2007) In Electroanalysis 19(2-3). p.172-180
Abstract
The catalytic properties of cellobiose dehydrogenase (CDH) from the ascomycete fungus Myriococcum thermophilum adsorbed on a graphite electrode were investigated for a large variety of carbohydrate substrates. The effects of applied potential, pH and buffer composition were tested and optimized, and the most suitable conditions were used to evaluate the detection limit, linear range, and sensitivity of the sensor for different carbohydrates in the flow injection mode. Subsequently, the long term stability of the modified electrodes was determined. Additionally, the direct and mediated electron transfer between the active site of the enzyme and the electrode has been investigated by amperometric flow injection measurements in the absence... (More)
The catalytic properties of cellobiose dehydrogenase (CDH) from the ascomycete fungus Myriococcum thermophilum adsorbed on a graphite electrode were investigated for a large variety of carbohydrate substrates. The effects of applied potential, pH and buffer composition were tested and optimized, and the most suitable conditions were used to evaluate the detection limit, linear range, and sensitivity of the sensor for different carbohydrates in the flow injection mode. Subsequently, the long term stability of the modified electrodes was determined. Additionally, the direct and mediated electron transfer between the active site of the enzyme and the electrode has been investigated by amperometric flow injection measurements in the absence and presence of the mediator 1,4-benzoquinone in the presence of cellobiose or lactose. (Less)
Please use this url to cite or link to this publication:
author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
cellobiose dehydrogenase, flow injection analysis, biosensor, carbohydrate, direct electron transfer, mediated electron transfer
in
Electroanalysis
volume
19
issue
2-3
pages
172 - 180
publisher
John Wiley and Sons
external identifiers
  • wos:000244220700008
  • scopus:34547587876
ISSN
1040-0397
DOI
10.1002/elan.200603688
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
cd343a1c-e845-4498-b6a6-d5bb48cdfb7d (old id 674666)
date added to LUP
2016-04-01 15:20:47
date last changed
2021-01-06 05:38:49
@article{cd343a1c-e845-4498-b6a6-d5bb48cdfb7d,
  abstract     = {The catalytic properties of cellobiose dehydrogenase (CDH) from the ascomycete fungus Myriococcum thermophilum adsorbed on a graphite electrode were investigated for a large variety of carbohydrate substrates. The effects of applied potential, pH and buffer composition were tested and optimized, and the most suitable conditions were used to evaluate the detection limit, linear range, and sensitivity of the sensor for different carbohydrates in the flow injection mode. Subsequently, the long term stability of the modified electrodes was determined. Additionally, the direct and mediated electron transfer between the active site of the enzyme and the electrode has been investigated by amperometric flow injection measurements in the absence and presence of the mediator 1,4-benzoquinone in the presence of cellobiose or lactose.},
  author       = {Harreither, Wolfgang and Coman, Vasile and Ludwig, Roland and Haltrich, Dietmar and Gorton, Lo},
  issn         = {1040-0397},
  language     = {eng},
  number       = {2-3},
  pages        = {172--180},
  publisher    = {John Wiley and Sons},
  series       = {Electroanalysis},
  title        = {Investigation of graphite electrodes modified with cellobiose dehydrogenase from the ascomycete Myriococcum thermophilum},
  url          = {http://dx.doi.org/10.1002/elan.200603688},
  doi          = {10.1002/elan.200603688},
  volume       = {19},
  year         = {2007},
}