HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 21, 17635-17640, May 25, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/21/17635    most recent M010571200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Conesa, A. Articles by Punt, P. J. Search for Related Content PubMed PubMed Citation Articles by Conesa, A. Articles by Punt, P. J. Social Bookmarking                      What's this?

Expression of the Caldariomyces fumago Chloroperoxidase in Aspergillus niger and Characterization of the Recombinant Enzyme^*

Ana Conesa, Fred van de Velde^§, Fred van Rantwijk^§, Roger A. Sheldon^§, Cees A. M. J. J. van den Hondel, and Peter J. Punt^¶

From the  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.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				R. Ullrich, J. Nuske, K. Scheibner, J. Spantzel, and M. Hofrichter Novel Haloperoxidase from the Agaric Basidiomycete Agrocybe aegerita Oxidizes Aryl Alcohols and Aldehydes Appl. Envir. Microbiol., August 1, 2004; 70(8): 4575 - 4581. [Abstract] [Full Text] [PDF]

				X. Yi, A. Conesa, P. J. Punt, and L. P. Hager Examining the Role of Glutamic Acid 183 in Chloroperoxidase Catalysis J. Biol. Chem., April 11, 2003; 278(16): 13855 - 13859. [Abstract] [Full Text] [PDF]