Electrochemical investigation of cellobiose dehydrogenase from new fungal sources on Au electrodes
(2005) In Biosensors & Bioelectronics 20(10). p.2010-2018- Abstract
- Following previous electrochemical investigations of cellobiose dehydrogenase (CDH), the present investigation reports on the initial screening of the electrochemistry of three new CDHs, two from the white rot basidiomycetes Trametes villosa and Phanerochaete sordida and one from the soft rot ascomycete Myriococcum thermophilum, for their ability to directly exchange electrons with 10 different alkanethiol-modified Au electrodes. Direct electron transfer (DET) between the enzymes and some of the modified Au electrodes was shown, both, in the presence and in the absence of cellobiose. However, the length and the head functionality of the alkanethiols drastically influenced the efficiency of the DET reaction and also influenced the effect of... (More)
- Following previous electrochemical investigations of cellobiose dehydrogenase (CDH), the present investigation reports on the initial screening of the electrochemistry of three new CDHs, two from the white rot basidiomycetes Trametes villosa and Phanerochaete sordida and one from the soft rot ascomycete Myriococcum thermophilum, for their ability to directly exchange electrons with 10 different alkanethiol-modified Au electrodes. Direct electron transfer (DET) between the enzymes and some of the modified Au electrodes was shown, both, in the presence and in the absence of cellobiose. However, the length and the head functionality of the alkanethiols drastically influenced the efficiency of the DET reaction and also influenced the effect of pH on the biocatalyfic/redox currents, suggesting the importance of structural/sequence differences between these CDH enzymes. In this respect, the white rot CDHs exhibit excellent biocatalytic and redox currents, whereas for the soft rot CDH the DET communication is much less efficient. Cyclic voltammograms indicate that the heme domain of the CDHs is the part of the enzymes that most readily exchanges electrons with the electrode. However, for R sordida CDH on 11-mercaptoundecanol or dithiopropionic acid-modified Au electrodes, a second voltammetric wave was noticed suggesting that for some orientations of the enzyme, DET communication with the FAD cofactor can also be obtained. (c) 2004 Elsevier B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/151093
- author
- Stoica, Leonard LU ; Dimcheva, N ; Haltrich, D ; Ruzgas, Tautgirdas LU and Gorton, Lo LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biosensors & Bioelectronics
- volume
- 20
- issue
- 10
- pages
- 2010 - 2018
- publisher
- Elsevier
- external identifiers
-
- wos:000227845700016
- pmid:15741070
- scopus:14644411719
- ISSN
- 1873-4235
- DOI
- 10.1016/j.bios.2004.09.018
- 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
- 4da06f58-6abf-46a1-a1af-d78a387f5df6 (old id 151093)
- date added to LUP
- 2016-04-01 16:33:10
- date last changed
- 2022-01-28 20:28:38
@article{4da06f58-6abf-46a1-a1af-d78a387f5df6,
abstract = {{Following previous electrochemical investigations of cellobiose dehydrogenase (CDH), the present investigation reports on the initial screening of the electrochemistry of three new CDHs, two from the white rot basidiomycetes Trametes villosa and Phanerochaete sordida and one from the soft rot ascomycete Myriococcum thermophilum, for their ability to directly exchange electrons with 10 different alkanethiol-modified Au electrodes. Direct electron transfer (DET) between the enzymes and some of the modified Au electrodes was shown, both, in the presence and in the absence of cellobiose. However, the length and the head functionality of the alkanethiols drastically influenced the efficiency of the DET reaction and also influenced the effect of pH on the biocatalyfic/redox currents, suggesting the importance of structural/sequence differences between these CDH enzymes. In this respect, the white rot CDHs exhibit excellent biocatalytic and redox currents, whereas for the soft rot CDH the DET communication is much less efficient. Cyclic voltammograms indicate that the heme domain of the CDHs is the part of the enzymes that most readily exchanges electrons with the electrode. However, for R sordida CDH on 11-mercaptoundecanol or dithiopropionic acid-modified Au electrodes, a second voltammetric wave was noticed suggesting that for some orientations of the enzyme, DET communication with the FAD cofactor can also be obtained. (c) 2004 Elsevier B.V. All rights reserved.}},
author = {{Stoica, Leonard and Dimcheva, N and Haltrich, D and Ruzgas, Tautgirdas and Gorton, Lo}},
issn = {{1873-4235}},
language = {{eng}},
number = {{10}},
pages = {{2010--2018}},
publisher = {{Elsevier}},
series = {{Biosensors & Bioelectronics}},
title = {{Electrochemical investigation of cellobiose dehydrogenase from new fungal sources on Au electrodes}},
url = {{http://dx.doi.org/10.1016/j.bios.2004.09.018}},
doi = {{10.1016/j.bios.2004.09.018}},
volume = {{20}},
year = {{2005}},
}