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Improved operational stability of chloroperoxidase through use of antioxidants.

Grey, Carl LU ; Rundbäck, Fabian LU and Adlercreutz, Patrick LU (2008) In Journal of Biotechnology 135(2). p.196-201
Abstract
Chloroperoxidase (CPO) from Caldariomyces fumago is a potentially very useful enzyme due to its ability to catalyze a large variety of stereoselective oxidation reactions, but poor operational stability is a main limitation for commercial use. In the present study, the possibility of increasing the operational stability by use of antioxidants was investigated using the oxidation of indole as model reaction. Caffeic acid was the antioxidant showing the strongest positive effects, reaching a total turnover number (TTN) of 135,000 at pH 4 and 4mM hydrogen peroxide, compared to 28,700 in the absence of antioxidant. Portion-wise addition of hydrogen peroxide in the presence of caffeic acid caused a further increase in TTN to 171,000. An... (More)
Chloroperoxidase (CPO) from Caldariomyces fumago is a potentially very useful enzyme due to its ability to catalyze a large variety of stereoselective oxidation reactions, but poor operational stability is a main limitation for commercial use. In the present study, the possibility of increasing the operational stability by use of antioxidants was investigated using the oxidation of indole as model reaction. Caffeic acid was the antioxidant showing the strongest positive effects, reaching a total turnover number (TTN) of 135,000 at pH 4 and 4mM hydrogen peroxide, compared to 28,700 in the absence of antioxidant. Portion-wise addition of hydrogen peroxide in the presence of caffeic acid caused a further increase in TTN to 171,000. An alternative way to reach high TTN was to use tert-butyl hydroperoxide as oxidant instead of hydrogen peroxide: a TTN of 600,000 was achieved although the reaction was quite slow. In this case, antioxidants did not have any positive effect. Possible mechanisms for the observed inactivation of CPO are discussed. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Enzyme catalysis, Oxidation, Chelates, Antioxidants, Chloroperoxidase
in
Journal of Biotechnology
volume
135
issue
2
pages
196 - 201
publisher
Elsevier
external identifiers
  • wos:000257037900011
  • pmid:18479771
  • scopus:43849098043
ISSN
1873-4863
DOI
10.1016/j.jbiotec.2008.03.015
language
English
LU publication?
yes
id
da1448f9-0ddf-4b59-aa5b-6c827fd3c3f5 (old id 1154144)
date added to LUP
2008-10-08 11:52:53
date last changed
2017-01-01 05:07:58
@article{da1448f9-0ddf-4b59-aa5b-6c827fd3c3f5,
  abstract     = {Chloroperoxidase (CPO) from Caldariomyces fumago is a potentially very useful enzyme due to its ability to catalyze a large variety of stereoselective oxidation reactions, but poor operational stability is a main limitation for commercial use. In the present study, the possibility of increasing the operational stability by use of antioxidants was investigated using the oxidation of indole as model reaction. Caffeic acid was the antioxidant showing the strongest positive effects, reaching a total turnover number (TTN) of 135,000 at pH 4 and 4mM hydrogen peroxide, compared to 28,700 in the absence of antioxidant. Portion-wise addition of hydrogen peroxide in the presence of caffeic acid caused a further increase in TTN to 171,000. An alternative way to reach high TTN was to use tert-butyl hydroperoxide as oxidant instead of hydrogen peroxide: a TTN of 600,000 was achieved although the reaction was quite slow. In this case, antioxidants did not have any positive effect. Possible mechanisms for the observed inactivation of CPO are discussed.},
  author       = {Grey, Carl and Rundbäck, Fabian and Adlercreutz, Patrick},
  issn         = {1873-4863},
  keyword      = {Enzyme catalysis,Oxidation,Chelates,Antioxidants,Chloroperoxidase},
  language     = {eng},
  number       = {2},
  pages        = {196--201},
  publisher    = {Elsevier},
  series       = {Journal of Biotechnology},
  title        = {Improved operational stability of chloroperoxidase through use of antioxidants.},
  url          = {http://dx.doi.org/10.1016/j.jbiotec.2008.03.015},
  volume       = {135},
  year         = {2008},
}