Entrapping of tyrosinase in a system of reverse micelles
(2004) In Biocatalysis and Biotransformation 22(1). p.57-60- Abstract
- The enzymatic activity of tyrosinase was studied both in aqueous and organic media. In the latter case tyrosinase was entrapped in a system of reverse micelles of Aerosol OT in octane. At hydration degree 25, when the inner cavity of the reverse micelles was comparable with the size of a tetrameric tyrosinase form known for aqueous solutions, an optimum level of catalytic activity was observed. Another peak of catalytic activity of tyrosinase was observed at hydration degree 12, when the size of the inner cavity of the reverse micelles was consistent with a monomeric form of tyrosinase. Thus, the system of reverse micelles can be exploited as a medium for the investigation of the monomeric form of tyrosinase, which is unstable in aqueous... (More)
- The enzymatic activity of tyrosinase was studied both in aqueous and organic media. In the latter case tyrosinase was entrapped in a system of reverse micelles of Aerosol OT in octane. At hydration degree 25, when the inner cavity of the reverse micelles was comparable with the size of a tetrameric tyrosinase form known for aqueous solutions, an optimum level of catalytic activity was observed. Another peak of catalytic activity of tyrosinase was observed at hydration degree 12, when the size of the inner cavity of the reverse micelles was consistent with a monomeric form of tyrosinase. Thus, the system of reverse micelles can be exploited as a medium for the investigation of the monomeric form of tyrosinase, which is unstable in aqueous solution. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/139409
- author
- Shipovskov, Stepan LU and Levashov, A
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biocatalysis and Biotransformation
- volume
- 22
- issue
- 1
- pages
- 57 - 60
- publisher
- Taylor & Francis
- external identifiers
-
- wos:000220089200008
- scopus:1842483900
- ISSN
- 1024-2422
- DOI
- 10.1080/1024242310001634755
- language
- English
- LU publication?
- yes
- id
- b84ea181-a437-4b32-8004-32db0d0aab2c (old id 139409)
- date added to LUP
- 2016-04-01 11:55:32
- date last changed
- 2022-01-26 20:16:09
@article{b84ea181-a437-4b32-8004-32db0d0aab2c,
abstract = {{The enzymatic activity of tyrosinase was studied both in aqueous and organic media. In the latter case tyrosinase was entrapped in a system of reverse micelles of Aerosol OT in octane. At hydration degree 25, when the inner cavity of the reverse micelles was comparable with the size of a tetrameric tyrosinase form known for aqueous solutions, an optimum level of catalytic activity was observed. Another peak of catalytic activity of tyrosinase was observed at hydration degree 12, when the size of the inner cavity of the reverse micelles was consistent with a monomeric form of tyrosinase. Thus, the system of reverse micelles can be exploited as a medium for the investigation of the monomeric form of tyrosinase, which is unstable in aqueous solution.}},
author = {{Shipovskov, Stepan and Levashov, A}},
issn = {{1024-2422}},
language = {{eng}},
number = {{1}},
pages = {{57--60}},
publisher = {{Taylor & Francis}},
series = {{Biocatalysis and Biotransformation}},
title = {{Entrapping of tyrosinase in a system of reverse micelles}},
url = {{http://dx.doi.org/10.1080/1024242310001634755}},
doi = {{10.1080/1024242310001634755}},
volume = {{22}},
year = {{2004}},
}