Entrapping of tyrosinase in a system of reverse micelles

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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.

Details

Authors
  • Stepan Shipovskov
  • A Levashov
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences
Original languageEnglish
Pages (from-to)57-60
JournalBiocatalysis and Biotransformation
Volume22
Issue number1
Publication statusPublished - 2004
Publication categoryResearch
Peer-reviewedYes