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Stabilisation of chloroperoxidase towards peroxide dependent inactivation

Andersson, Mats LU ; Andersson, Maria M. LU and Adlercreutz, Patrick LU (2000) In Biocatalysis and Biotransformation 18(6). p.457-469
Abstract


The addition of polyethyleneimine with a molecular weight of 2000 to chloroperoxidase from Caldariomyces fumago dramatically improved the stability of the enzyme towards peroxide dependent inactivation. The rate constant for the H
2
O
2
-dependent inactivation of chloroperoxidase decreased from 0.0016s
-1
to 1.1 * 10
-5
s
-1
in the... (More)


The addition of polyethyleneimine with a molecular weight of 2000 to chloroperoxidase from Caldariomyces fumago dramatically improved the stability of the enzyme towards peroxide dependent inactivation. The rate constant for the H
2
O
2
-dependent inactivation of chloroperoxidase decreased from 0.0016s
-1
to 1.1 * 10
-5
s
-1
in the presence of 1% polyethyleneimine. The stabilising effect towards tert-butyl hydroperoxide was even more impressive. The half-life of the chloroperoxidase when exposed to a solution of 40 mM tert-butyl hydroperoxide increased from 3.2 minutes to ≥ 70 hours in presence of 0.1% polyethyleneimine.

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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
keywords
Chloroperoxidase, Polyethyleneimine, Protein stabilisation
in
Biocatalysis and Biotransformation
volume
18
issue
6
pages
13 pages
publisher
Taylor & Francis
external identifiers
  • scopus:0034527222
ISSN
1024-2422
DOI
10.3109/10242420009015263
language
English
LU publication?
yes
id
b127d60d-ecfd-4183-b6b8-8aaf3c69a8b3
date added to LUP
2019-06-20 15:53:19
date last changed
2020-01-13 02:04:14
@article{b127d60d-ecfd-4183-b6b8-8aaf3c69a8b3,
  abstract     = {<p><br>
                            The addition of polyethyleneimine with a molecular weight of 2000 to chloroperoxidase from Caldariomyces fumago dramatically improved the stability of the enzyme towards peroxide dependent inactivation. The rate constant for the H<br>
                            <sub>2</sub><br>
                            O<br>
                            <sub>2</sub><br>
                            -dependent inactivation of chloroperoxidase decreased from 0.0016s<br>
                            <sup>-1</sup><br>
                             to 1.1 * 10<br>
                            <sup>-5</sup><br>
                             s<br>
                            <sup>-1</sup><br>
                             in the presence of 1% polyethyleneimine. The stabilising effect towards tert-butyl hydroperoxide was even more impressive. The half-life of the chloroperoxidase when exposed to a solution of 40 mM tert-butyl hydroperoxide increased from 3.2 minutes to ≥ 70 hours in presence of 0.1% polyethyleneimine.<br>
                        </p>},
  author       = {Andersson, Mats and Andersson, Maria M. and Adlercreutz, Patrick},
  issn         = {1024-2422},
  language     = {eng},
  month        = {01},
  number       = {6},
  pages        = {457--469},
  publisher    = {Taylor & Francis},
  series       = {Biocatalysis and Biotransformation},
  title        = {Stabilisation of chloroperoxidase towards peroxide dependent inactivation},
  url          = {http://dx.doi.org/10.3109/10242420009015263},
  doi          = {10.3109/10242420009015263},
  volume       = {18},
  year         = {2000},
}