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Cellobiose dehydrogenase hosted in lipidic cubic phase to improve catalytic activity and stability

Grippo, Valentina; Ma, Su; Ludwig, Roland; Gorton, Lo LU and Bilewicz, Renata (2017) In Bioelectrochemistry
Abstract

Lipidic cubic phase systems (LCPs) are excellent carriers for immobilized enzymes due to their biocompatibility and well-defined nanoporous structure. Lipidic cubic phases act as a convenient matrix to incorporate enzymes and hold them in the vicinity of electrode surfaces in their fully active forms. Corynascus thermophilus cellobiose dehydrogenase (CtCDH) was trapped in a monoolein cubic phase, which increased not only its stability, but also its catalytic performance with both enhanced mediated and direct electron transfer with electrodes. For studies of mediated electron transfer, three mediators with different formal potentials (E°') were employed: horse-heart cytochrome c (cyt c), electron acceptor active with the cytochrome... (More)

Lipidic cubic phase systems (LCPs) are excellent carriers for immobilized enzymes due to their biocompatibility and well-defined nanoporous structure. Lipidic cubic phases act as a convenient matrix to incorporate enzymes and hold them in the vicinity of electrode surfaces in their fully active forms. Corynascus thermophilus cellobiose dehydrogenase (CtCDH) was trapped in a monoolein cubic phase, which increased not only its stability, but also its catalytic performance with both enhanced mediated and direct electron transfer with electrodes. For studies of mediated electron transfer, three mediators with different formal potentials (E°') were employed: horse-heart cytochrome c (cyt c), electron acceptor active with the cytochrome domain of CtCDH, and 2,6-dichlorophenolindophenol (DCPIP) as well as hexaammineruthenium(II) chloride [Ru(NH3)Cl2] both electron acceptors with the dehydrogenase domain. Ru(NH3)Cl2, having the most negative E°' of -0.138V vs. Ag|AgCl at pH7.5, gave a catalytic current for lactose oxidation of 32.10μAcm-2 in MOPS buffer at pH7.5. The process carried out in the same solution but under direct electron conditions transfer resulted in a catalytic current of 9.22μAcm-2. Electrodes covered with CtCDH in a LCP film retained their catalytic activity after 28days showing a slightly increased current density after 6days.

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author
organization
publishing date
type
Contribution to journal
publication status
epub
subject
keywords
Cellobiose dehydrogenase, Cubic phase, DET, MET
in
Bioelectrochemistry
publisher
Elsevier
external identifiers
  • scopus:85033400744
ISSN
1567-5394
DOI
10.1016/j.bioelechem.2017.10.003
language
English
LU publication?
yes
id
c8178857-1d74-40f6-841d-296686184f93
date added to LUP
2017-11-21 09:33:48
date last changed
2018-01-07 12:26:18
@article{c8178857-1d74-40f6-841d-296686184f93,
  abstract     = {<p>Lipidic cubic phase systems (LCPs) are excellent carriers for immobilized enzymes due to their biocompatibility and well-defined nanoporous structure. Lipidic cubic phases act as a convenient matrix to incorporate enzymes and hold them in the vicinity of electrode surfaces in their fully active forms. Corynascus thermophilus cellobiose dehydrogenase (CtCDH) was trapped in a monoolein cubic phase, which increased not only its stability, but also its catalytic performance with both enhanced mediated and direct electron transfer with electrodes. For studies of mediated electron transfer, three mediators with different formal potentials (E°') were employed: horse-heart cytochrome c (cyt c), electron acceptor active with the cytochrome domain of CtCDH, and 2,6-dichlorophenolindophenol (DCPIP) as well as hexaammineruthenium(II) chloride [Ru(NH<sub>3</sub>)Cl<sub>2</sub>] both electron acceptors with the dehydrogenase domain. Ru(NH<sub>3</sub>)Cl<sub>2</sub>, having the most negative E°' of -0.138V vs. Ag|AgCl at pH7.5, gave a catalytic current for lactose oxidation of 32.10μAcm<sup>-2</sup> in MOPS buffer at pH7.5. The process carried out in the same solution but under direct electron conditions transfer resulted in a catalytic current of 9.22μAcm<sup>-2</sup>. Electrodes covered with CtCDH in a LCP film retained their catalytic activity after 28days showing a slightly increased current density after 6days.</p>},
  author       = {Grippo, Valentina and Ma, Su and Ludwig, Roland and Gorton, Lo and Bilewicz, Renata},
  issn         = {1567-5394},
  keyword      = {Cellobiose dehydrogenase,Cubic phase,DET,MET},
  language     = {eng},
  month        = {10},
  publisher    = {Elsevier},
  series       = {Bioelectrochemistry},
  title        = {Cellobiose dehydrogenase hosted in lipidic cubic phase to improve catalytic activity and stability},
  url          = {http://dx.doi.org/10.1016/j.bioelechem.2017.10.003},
  year         = {2017},
}