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Enhancement of enzymatic activity and catalytic current of cellobiose dehydrogenase by calcium ions

Schulz, Christopher LU ; Ludwig, Roland; Micheelsen, Pernille O.; Silow, Maria; Toscano, Miguel D. and Gorton, Lo LU (2012) In Electrochemistry Communications 17. p.71-74
Abstract
Cellobiose dehydrogenase (CDH) has recently become a redox enzyme at focus in bioelectrochemistry especially for the construction of sugar biosensors and biofuel cell anodes. The present study shows that an increase in the CaCl2 concentration to up to 100 mM led to an increase in the maximal catalytic current generated by two different Ascomycete and one Basidiomycete CDH immobilised on a spectroscopic graphite electrode. For the Ascomycete Myriococcum therrnophilum CDH the catalytic current was increased 5.1 fold, whereas Ascomycete Humicola insolens CDH showed a four-fold increase and Basidiomycete Phanerochaete chrysosporium CDH showed an increase by a factor of 2.4. On the other hand, the addition of a monovalent cation salt, KCl (up... (More)
Cellobiose dehydrogenase (CDH) has recently become a redox enzyme at focus in bioelectrochemistry especially for the construction of sugar biosensors and biofuel cell anodes. The present study shows that an increase in the CaCl2 concentration to up to 100 mM led to an increase in the maximal catalytic current generated by two different Ascomycete and one Basidiomycete CDH immobilised on a spectroscopic graphite electrode. For the Ascomycete Myriococcum therrnophilum CDH the catalytic current was increased 5.1 fold, whereas Ascomycete Humicola insolens CDH showed a four-fold increase and Basidiomycete Phanerochaete chrysosporium CDH showed an increase by a factor of 2.4. On the other hand, the addition of a monovalent cation salt, KCl (up to 100 mM), to the buffers increased the catalytic currents only up to 2-fold for Myriococcum thermophilum CDH. Activity assays in solution with cyt c accepting solely the electrons from the CYTCDH domain also revealed an increased activity in the presence of CaCl2. Experiments with the isolated DHCDH domain from Humicola insolens have shown that the catalytic turnover is totally independent on the addition of KCl or CaCl2 to the solution. The results indicate a positive effect of metal cations, particularly Ca2+, on the electron transfer between the DHCDH and the CYTCDH domains or between the CYTCDH domain and the final electron acceptor, whereas the first hypothesis is favoured. These findings are of interest both for the construction of 3 rd generation biosensors and biofuel cell anodes, and also for a deeper understanding of the electron transfer mechanism in CDH. (C) 2012 Elsevier B.V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Activation, Cellobiose dehydrogenase, Catalytic activity, CaCl2, KCl, Ionic strength
in
Electrochemistry Communications
volume
17
pages
71 - 74
publisher
Elsevier
external identifiers
  • wos:000303227000019
  • scopus:84858725321
ISSN
1388-2481
DOI
10.1016/j.elecom.2012.01.031
language
English
LU publication?
yes
id
140e73b9-b902-4154-af39-0504b7627e1c (old id 2570333)
date added to LUP
2012-06-01 13:45:00
date last changed
2017-09-24 03:13:59
@article{140e73b9-b902-4154-af39-0504b7627e1c,
  abstract     = {Cellobiose dehydrogenase (CDH) has recently become a redox enzyme at focus in bioelectrochemistry especially for the construction of sugar biosensors and biofuel cell anodes. The present study shows that an increase in the CaCl2 concentration to up to 100 mM led to an increase in the maximal catalytic current generated by two different Ascomycete and one Basidiomycete CDH immobilised on a spectroscopic graphite electrode. For the Ascomycete Myriococcum therrnophilum CDH the catalytic current was increased 5.1 fold, whereas Ascomycete Humicola insolens CDH showed a four-fold increase and Basidiomycete Phanerochaete chrysosporium CDH showed an increase by a factor of 2.4. On the other hand, the addition of a monovalent cation salt, KCl (up to 100 mM), to the buffers increased the catalytic currents only up to 2-fold for Myriococcum thermophilum CDH. Activity assays in solution with cyt c accepting solely the electrons from the CYTCDH domain also revealed an increased activity in the presence of CaCl2. Experiments with the isolated DHCDH domain from Humicola insolens have shown that the catalytic turnover is totally independent on the addition of KCl or CaCl2 to the solution. The results indicate a positive effect of metal cations, particularly Ca2+, on the electron transfer between the DHCDH and the CYTCDH domains or between the CYTCDH domain and the final electron acceptor, whereas the first hypothesis is favoured. These findings are of interest both for the construction of 3 rd generation biosensors and biofuel cell anodes, and also for a deeper understanding of the electron transfer mechanism in CDH. (C) 2012 Elsevier B.V. All rights reserved.},
  author       = {Schulz, Christopher and Ludwig, Roland and Micheelsen, Pernille O. and Silow, Maria and Toscano, Miguel D. and Gorton, Lo},
  issn         = {1388-2481},
  keyword      = {Activation,Cellobiose dehydrogenase,Catalytic activity,CaCl2,KCl,Ionic strength},
  language     = {eng},
  pages        = {71--74},
  publisher    = {Elsevier},
  series       = {Electrochemistry Communications},
  title        = {Enhancement of enzymatic activity and catalytic current of cellobiose dehydrogenase by calcium ions},
  url          = {http://dx.doi.org/10.1016/j.elecom.2012.01.031},
  volume       = {17},
  year         = {2012},
}