Stabilisation of tyrosinase by reversed micelles for bioelectrocatalysis in dry organic media
(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:
https://lup.lub.lu.se/record/317426
- author
- Shipovskov, S ; Ferapontova, Elena LU ; Ruzgas, Tautgirdas LU and Levashov, A
- organization
- publishing date
- 2003
- 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
- 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
- cde514f4-4dbe-4e5a-8735-63c5a7f0b9c5 (old id 317426)
- date added to LUP
- 2016-04-01 16:11:19
- date last changed
- 2022-01-28 17:55:31
@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}},
keywords = {{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}},
doi = {{10.1016/S0304-4165(02)00513-5}},
volume = {{1620}},
year = {{2003}},
}