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Activity and stability of horse‐liver alcohol dehydrogenase in sodium dioctylsulfosuccinate/cyclohexane reverse micelles

Larsson, Karin M. ; Adlercreutz, Patrick LU orcid and Mattiasson, Bo LU (1987) In European Journal of Biochemistry 166(1). p.157-161
Abstract

Horse liver alcohol dehydrogenase (EC 1.1.1.1) solubilized in sodium dioctylsulfosuccinate (AOT)/cyclohexane reverse micelles was used for the oxidation of ethanol and reduction of cyclohexanone in a coupled substrate/coenzyme recycling system. The activity of the enzyme was studied as a function of pH and water content. The enzyme was optimally active in microemulsions prepared with buffer of pH around 8. An increase in enzymatic activity was observed as a function of increasing water content. The Km values for the substrates were calculated based on the total reaction volume. The apparent Km for ethanol in reverse micelles was about eight times lower as compared to that in buffer solution, whereas the... (More)

Horse liver alcohol dehydrogenase (EC 1.1.1.1) solubilized in sodium dioctylsulfosuccinate (AOT)/cyclohexane reverse micelles was used for the oxidation of ethanol and reduction of cyclohexanone in a coupled substrate/coenzyme recycling system. The activity of the enzyme was studied as a function of pH and water content. The enzyme was optimally active in microemulsions prepared with buffer of pH around 8. An increase in enzymatic activity was observed as a function of increasing water content. The Km values for the substrates were calculated based on the total reaction volume. The apparent Km for ethanol in reverse micelles was about eight times lower as compared to that in buffer solution, whereas the Km for cyclohexanone was almost unaltered. Storage and operational stability were investigated. It was found that the specific activity of the alcohol dehydrogenase operating in reverse micellar solution was good for at least two weeks. The steroid eticholan‐3ß‐ol‐17‐one was also used as a substrate. In this case the reaction rate was approximately five times higher in a reverse micellar solution than in buffer.

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Please use this url to cite or link to this publication:
author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
European Journal of Biochemistry
volume
166
issue
1
pages
5 pages
publisher
Wiley-Blackwell
external identifiers
  • pmid:2439336
  • scopus:0023378105
ISSN
0014-2956
DOI
10.1111/j.1432-1033.1987.tb13496.x
language
English
LU publication?
yes
id
743b4149-0d6e-4939-a2ac-0ee0d8475b12
date added to LUP
2019-06-22 19:01:19
date last changed
2024-01-01 12:30:20
@article{743b4149-0d6e-4939-a2ac-0ee0d8475b12,
  abstract     = {{<p>Horse liver alcohol dehydrogenase (EC 1.1.1.1) solubilized in sodium dioctylsulfosuccinate (AOT)/cyclohexane reverse micelles was used for the oxidation of ethanol and reduction of cyclohexanone in a coupled substrate/coenzyme recycling system. The activity of the enzyme was studied as a function of pH and water content. The enzyme was optimally active in microemulsions prepared with buffer of pH around 8. An increase in enzymatic activity was observed as a function of increasing water content. The K<sub>m</sub> values for the substrates were calculated based on the total reaction volume. The apparent K<sub>m</sub> for ethanol in reverse micelles was about eight times lower as compared to that in buffer solution, whereas the K<sub>m</sub> for cyclohexanone was almost unaltered. Storage and operational stability were investigated. It was found that the specific activity of the alcohol dehydrogenase operating in reverse micellar solution was good for at least two weeks. The steroid eticholan‐3ß‐ol‐17‐one was also used as a substrate. In this case the reaction rate was approximately five times higher in a reverse micellar solution than in buffer.</p>}},
  author       = {{Larsson, Karin M. and Adlercreutz, Patrick and Mattiasson, Bo}},
  issn         = {{0014-2956}},
  language     = {{eng}},
  month        = {{01}},
  number       = {{1}},
  pages        = {{157--161}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{European Journal of Biochemistry}},
  title        = {{Activity and stability of horse‐liver alcohol dehydrogenase in sodium dioctylsulfosuccinate/cyclohexane reverse micelles}},
  url          = {{http://dx.doi.org/10.1111/j.1432-1033.1987.tb13496.x}},
  doi          = {{10.1111/j.1432-1033.1987.tb13496.x}},
  volume       = {{166}},
  year         = {{1987}},
}