Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Use of celite-immobilised chloroperoxidase in predominantly organic media

Andersson, Mats LU ; Samra, Babinder K. ; Holmberg, Hans and Adlercreutz, Patrick LU orcid (1999) In Biocatalysis and Biotransformation 17(4). p.293-303
Abstract

It is possible to use the chloroperoxidase from Caldariomyces fumago to catalyse the oxidation of benzyl alcohol to benzaldehyde in predominantly organic media, even at water activities below 1.0, if the oxidant is tert-butyl hydroperoxide. The enzyme activity increased with increasing water activity and no enzyme activity was observed at water activities below 0.6. Hydrophobic solvents such as cyclohexane showed the highest initial activities. It was beneficial in terms of obtainable yield to use high concentrations of the peroxide due to the kinetics of the system. The apparent K(m) for benzyl alcohol in cyclohexane was estimated to be 13 mM while the initial reaction rate increased almost linearly up to 250 mM tert-butyl... (More)

It is possible to use the chloroperoxidase from Caldariomyces fumago to catalyse the oxidation of benzyl alcohol to benzaldehyde in predominantly organic media, even at water activities below 1.0, if the oxidant is tert-butyl hydroperoxide. The enzyme activity increased with increasing water activity and no enzyme activity was observed at water activities below 0.6. Hydrophobic solvents such as cyclohexane showed the highest initial activities. It was beneficial in terms of obtainable yield to use high concentrations of the peroxide due to the kinetics of the system. The apparent K(m) for benzyl alcohol in cyclohexane was estimated to be 13 mM while the initial reaction rate increased almost linearly up to 250 mM tert-butyl hydroperoxide.

(Less)
Please use this url to cite or link to this publication:
author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Alcohol oxidation, CPO, Organic solvents
in
Biocatalysis and Biotransformation
volume
17
issue
4
pages
11 pages
publisher
Taylor & Francis
external identifiers
  • scopus:0032586515
ISSN
1024-2422
DOI
10.3109/10242429909015232
language
English
LU publication?
yes
id
d1c0e369-adb3-43b0-8625-e4a993b1d48d
date added to LUP
2019-06-20 15:36:00
date last changed
2022-01-31 22:13:21
@article{d1c0e369-adb3-43b0-8625-e4a993b1d48d,
  abstract     = {{<p>It is possible to use the chloroperoxidase from Caldariomyces fumago to catalyse the oxidation of benzyl alcohol to benzaldehyde in predominantly organic media, even at water activities below 1.0, if the oxidant is tert-butyl hydroperoxide. The enzyme activity increased with increasing water activity and no enzyme activity was observed at water activities below 0.6. Hydrophobic solvents such as cyclohexane showed the highest initial activities. It was beneficial in terms of obtainable yield to use high concentrations of the peroxide due to the kinetics of the system. The apparent K(m) for benzyl alcohol in cyclohexane was estimated to be 13 mM while the initial reaction rate increased almost linearly up to 250 mM tert-butyl hydroperoxide.</p>}},
  author       = {{Andersson, Mats and Samra, Babinder K. and Holmberg, Hans and Adlercreutz, Patrick}},
  issn         = {{1024-2422}},
  keywords     = {{Alcohol oxidation; CPO; Organic solvents}},
  language     = {{eng}},
  month        = {{01}},
  number       = {{4}},
  pages        = {{293--303}},
  publisher    = {{Taylor & Francis}},
  series       = {{Biocatalysis and Biotransformation}},
  title        = {{Use of celite-immobilised chloroperoxidase in predominantly organic media}},
  url          = {{http://dx.doi.org/10.3109/10242429909015232}},
  doi          = {{10.3109/10242429909015232}},
  volume       = {{17}},
  year         = {{1999}},
}