Functional aspects of cellobiose dehydrogenase Applications for biosensor development
(2005)- Abstract
- Electrochemcial investigations were conducted for elucidating
and understanding the relation between the various electron transfer processes occurring in
cellobiose dehydrogenase (CDH) bound to an electrode surface. Substrate inhibition caused by
cellobiose was proven to act in competition with the electron transfer to a two-electron acceptor
and under a partial inhibition mechanism for the internal electron transfer process. The
implications of these findings have been discussed in relation to what has been stated previously
but also exploited for analytical purposes by adjusting the sensitivity of the CDH based... (More) - Electrochemcial investigations were conducted for elucidating
and understanding the relation between the various electron transfer processes occurring in
cellobiose dehydrogenase (CDH) bound to an electrode surface. Substrate inhibition caused by
cellobiose was proven to act in competition with the electron transfer to a two-electron acceptor
and under a partial inhibition mechanism for the internal electron transfer process. The
implications of these findings have been discussed in relation to what has been stated previously
but also exploited for analytical purposes by adjusting the sensitivity of the CDH based biosensor
for catecholamines.
Different thiols were used to form self-assembled monolayers (SAM) on gold electrodes and these
have been used to electrochemically investigate and characterise the direct electron transfer
reaction of CDH from two white-rot fungi (Phanerochaete sordida and Trametes villosa), and one
soft-rot fungus (Myriococcum thermophilum) in the absence and presence of cellobiose.
The high efficiency of the direct electron transfer between Phanerochaete sordida CDH and
Trametes villosa CDH and SAM modified Au electrodes was emphasised, and a potential
application of these enzymes was demonstrated by development of a third-generation biosensor for
lactose determination.
Toxic waste-water quinone type pollutants were also determined using a Phanerochaete
chrysosporium CDH based biosensor, working under a mediated electron transfer mechanism. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/544363
- author
- Stoica, Leonard LU
- supervisor
-
- Lo Gorton LU
- opponent
-
- Professor Scheller, Frieder W., Dept. of Analytical Biochemistry, Potsdam University, Golm, Germany
- organization
- publishing date
- 2005
- type
- Thesis
- publication status
- published
- subject
- keywords
- Elektrokemi, Electrochemistry, Analytisk kemi, Analytical chemistry, bioelectrochemistry, direct electron transfer, lactose biosensor
- pages
- 184 pages
- publisher
- Department of Analytical Chemistry, Lund University
- defense location
- Centre for Chemistry and Chemical Engineering, Sölvegatan 39, Lund, Hall B
- defense date
- 2004-03-04 10:30:00
- ISBN
- 91-7422-073-X
- 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
- 412d265b-0190-4b37-8421-574f68e404ce (old id 544363)
- date added to LUP
- 2016-04-04 12:10:26
- date last changed
- 2018-11-21 21:09:24
@phdthesis{412d265b-0190-4b37-8421-574f68e404ce,
abstract = {{Electrochemcial investigations were conducted for elucidating<br/><br>
<br/><br>
and understanding the relation between the various electron transfer processes occurring in<br/><br>
<br/><br>
cellobiose dehydrogenase (CDH) bound to an electrode surface. Substrate inhibition caused by<br/><br>
<br/><br>
cellobiose was proven to act in competition with the electron transfer to a two-electron acceptor<br/><br>
<br/><br>
and under a partial inhibition mechanism for the internal electron transfer process. The<br/><br>
<br/><br>
implications of these findings have been discussed in relation to what has been stated previously<br/><br>
<br/><br>
but also exploited for analytical purposes by adjusting the sensitivity of the CDH based biosensor<br/><br>
<br/><br>
for catecholamines.<br/><br>
<br/><br>
Different thiols were used to form self-assembled monolayers (SAM) on gold electrodes and these<br/><br>
<br/><br>
have been used to electrochemically investigate and characterise the direct electron transfer<br/><br>
<br/><br>
reaction of CDH from two white-rot fungi (Phanerochaete sordida and Trametes villosa), and one<br/><br>
<br/><br>
soft-rot fungus (Myriococcum thermophilum) in the absence and presence of cellobiose.<br/><br>
<br/><br>
The high efficiency of the direct electron transfer between Phanerochaete sordida CDH and<br/><br>
<br/><br>
Trametes villosa CDH and SAM modified Au electrodes was emphasised, and a potential<br/><br>
<br/><br>
application of these enzymes was demonstrated by development of a third-generation biosensor for<br/><br>
<br/><br>
lactose determination.<br/><br>
<br/><br>
Toxic waste-water quinone type pollutants were also determined using a Phanerochaete<br/><br>
<br/><br>
chrysosporium CDH based biosensor, working under a mediated electron transfer mechanism.}},
author = {{Stoica, Leonard}},
isbn = {{91-7422-073-X}},
keywords = {{Elektrokemi; Electrochemistry; Analytisk kemi; Analytical chemistry; bioelectrochemistry; direct electron transfer; lactose biosensor}},
language = {{eng}},
publisher = {{Department of Analytical Chemistry, Lund University}},
school = {{Lund University}},
title = {{Functional aspects of cellobiose dehydrogenase Applications for biosensor development}},
year = {{2005}},
}