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Originally published In Press as doi:10.1074/jbc.M010571200 on February 22, 2001

J. Biol. Chem., Vol. 276, Issue 21, 17635-17640, May 25, 2001
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Expression of the Caldariomyces fumago Chloroperoxidase in Aspergillus niger and Characterization of the Recombinant Enzyme*

Ana ConesaDagger , Fred van de Velde§, Fred van Rantwijk§, Roger A. Sheldon§, Cees A. M. J. J. van den HondelDagger , and Peter J. PuntDagger

From the Dagger  Department of Applied Microbiology and Gene Technology, TNO Nutrition and Food Research Institute, Utrechtseweg 48, 3704 HE Zeist, The Netherlands and the § Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands

The Caldariomyces fumago chloroperoxidase was successfully expressed in Aspergillus niger. The recombinant enzyme was produced in the culture medium as an active protein and could be purified by a three-step purification procedure. The catalytic behavior of recombinant chloroperoxidase (rCPO) was studied and compared with that of native CPO. The specific chlorination activity (47 units/nmol) of rCPO and its pH optimum (pH 2.75) were very similar to those of native CPO. rCPO catalyzes the oxidation of various substrates in comparable yields and selectivities to native CPO. Indole was oxidized to 2-oxindole with 99% selectivity and thioanisole to the corresponding R-sulfoxide (enantiomeric excess >98%). Incorporation of 18O from labeled H218O2 into the oxidized products was 100% in both cases.


* This work was supported in part by Dutch Innovation Oriented Program on Catalysis Grant IKA94013.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. E-mail: ppunt@voeding.tno.nl.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.