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Entrapping of tyrosinase in a system of reverse micelles

Shipovskov, Stepan LU and Levashov, A (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)
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author
organization
publishing date
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
2007-07-09 16:26:42
date last changed
2017-02-26 03:30:13
@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},
  volume       = {22},
  year         = {2004},
}