Activity and stability of horse‐liver alcohol dehydrogenase in sodium dioctylsulfosuccinate/cyclohexane reverse micelles
Larsson, Karin M. ; Adlercreutz, Patrick LU
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.
(Less)
- author
- Larsson, Karin M.
; Adlercreutz, Patrick
LU
and Mattiasson, Bo
LU
- organization
- publishing date
- 1987-01-01
- 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
-
- scopus:0023378105
- pmid:2439336
- 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}},
}