Advanced

Stabilisation of tyrosinase by reversed micelles for bioelectrocatalysis in dry organic media

Shipovskov, S; Ferapontova, Elena LU ; Ruzgas, Tautgirdas LU and Levashov, A (2003) In Biochimica et Biophysica Acta. General Subjects 1620(1-3). p.119-124
Abstract
The enzymatic and bioelectrocatalytic activity of tyrosinase from mushrooms was studied in a system of reversed micelles formed by Aerosol OT (AOT) in hexane. The optimal catechol oxidising activity of tyrosinase incorporated in reversed micelles was found at a hydration degree of w(0) = 25. The catalytic activity was comparable with tyrosinase activity in aqueous media. When immobilized at an Au electrode, either directly or in reversed micelles, tyrosinase exhibited a similar efficiency of the bioelectrocatalytic reduction of O-2 mediated by catechol; however, a rapid decrease in the activity correlated with the destruction of reversed micelles and/or the removal of tyrosinase from the electrode surface. The system containing tyrosinase... (More)
The enzymatic and bioelectrocatalytic activity of tyrosinase from mushrooms was studied in a system of reversed micelles formed by Aerosol OT (AOT) in hexane. The optimal catechol oxidising activity of tyrosinase incorporated in reversed micelles was found at a hydration degree of w(0) = 25. The catalytic activity was comparable with tyrosinase activity in aqueous media. When immobilized at an Au electrode, either directly or in reversed micelles, tyrosinase exhibited a similar efficiency of the bioelectrocatalytic reduction of O-2 mediated by catechol; however, a rapid decrease in the activity correlated with the destruction of reversed micelles and/or the removal of tyrosinase from the electrode surface. The system containing tyrosinase in reversed micelles with caoutchouk, spread on the surface of the An electrode and successively covered with a Nafion(R) membrane layer, was found to result in stable tyrosinase-modified electrodes, which were resistant to inactivation in dry acetonitrile. The proposed technique offers possibilities for further development of highly active and stable surfactant/enzyme-modified electrodes for measurements carried out in organic solvents. (C) 2002 Elsevier Science B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
acetonitrile, bioelectrocatalysis in organic media, tyrosinase, reversed micelle
in
Biochimica et Biophysica Acta. General Subjects
volume
1620
issue
1-3
pages
119 - 124
publisher
Elsevier
external identifiers
  • pmid:12595080
  • wos:000181227700015
  • scopus:12244283989
ISSN
0304-4165
DOI
10.1016/S0304-4165(02)00513-5
language
English
LU publication?
yes
id
cde514f4-4dbe-4e5a-8735-63c5a7f0b9c5 (old id 317426)
date added to LUP
2007-09-21 12:48:47
date last changed
2018-05-29 11:31:33
@article{cde514f4-4dbe-4e5a-8735-63c5a7f0b9c5,
  abstract     = {The enzymatic and bioelectrocatalytic activity of tyrosinase from mushrooms was studied in a system of reversed micelles formed by Aerosol OT (AOT) in hexane. The optimal catechol oxidising activity of tyrosinase incorporated in reversed micelles was found at a hydration degree of w(0) = 25. The catalytic activity was comparable with tyrosinase activity in aqueous media. When immobilized at an Au electrode, either directly or in reversed micelles, tyrosinase exhibited a similar efficiency of the bioelectrocatalytic reduction of O-2 mediated by catechol; however, a rapid decrease in the activity correlated with the destruction of reversed micelles and/or the removal of tyrosinase from the electrode surface. The system containing tyrosinase in reversed micelles with caoutchouk, spread on the surface of the An electrode and successively covered with a Nafion(R) membrane layer, was found to result in stable tyrosinase-modified electrodes, which were resistant to inactivation in dry acetonitrile. The proposed technique offers possibilities for further development of highly active and stable surfactant/enzyme-modified electrodes for measurements carried out in organic solvents. (C) 2002 Elsevier Science B.V. All rights reserved.},
  author       = {Shipovskov, S and Ferapontova, Elena and Ruzgas, Tautgirdas and Levashov, A},
  issn         = {0304-4165},
  keyword      = {acetonitrile,bioelectrocatalysis in organic media,tyrosinase,reversed micelle},
  language     = {eng},
  number       = {1-3},
  pages        = {119--124},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta. General Subjects},
  title        = {Stabilisation of tyrosinase by reversed micelles for bioelectrocatalysis in dry organic media},
  url          = {http://dx.doi.org/10.1016/S0304-4165(02)00513-5},
  volume       = {1620},
  year         = {2003},
}