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Issue 22, 2009
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Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors

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Abstract

The encapsulation of chloroperoxidase from Caldariomyces fumago (CPO) in block copolymer polymersomes is reported. Fluorescence and electron microscopy show that when the encapsulating conditions favour self-assembly of the block copolymer, the enzyme is incorporated with concentrations that are 50 times higher than the enzyme concentration before encapsulation. The oxidation of two substrates by the encapsulated enzyme was studied: i) pyrogallol, a common substrate used to assay CPO enzymatic activity and ii) thioanisole, of which the product, (R)-methyl phenyl sulfoxide, is an important pharmaceutical intermediate. The CPO-loaded polymersomes showed distinct reactivity towards these substrates. While the oxidation of pyrogallol was limited by diffusion of the substrate into the polymersome, the rate-limiting step for the oxidation of thioansiole was the turnover by the enzyme.

Graphical abstract: Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors

  • This article is part of the themed collection: Biocatalysis
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Publication details

The article was received on 10 Jun 2009, accepted on 29 Jul 2009 and first published on 03 Sep 2009


Article type: Paper
DOI: 10.1039/B911370C
Citation: Org. Biomol. Chem., 2009,7, 4604-4610
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    Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors

    H. M. de Hoog, M. Nallani, J. J. L. M. Cornelissen, A. E. Rowan, R. J. M. Nolte and I. W. C. E. Arends, Org. Biomol. Chem., 2009, 7, 4604
    DOI: 10.1039/B911370C

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