Biocatalytic oxidation by chloroperoxidase from caldariomyces fumago in polymersome nanoreactors

H.M. de Hoog, M. Nallani, Jeroen Johannes Lambertus Maria Cornelissen, A.E. Rowan, J.M. Nolte, I.W.C.E. Arends

Research output: Contribution to journalArticleAcademicpeer-review

26 Citations (Scopus)

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
Original languageUndefined
Pages (from-to)4604-4610
Number of pages7
JournalOrganic & biomolecular chemistry
Volume7
DOIs
Publication statusPublished - 2009

Keywords

  • IR-77781
  • METIS-263223

Cite this

@article{477a2d390ef3413da3ea277f353ddc25,
title = "Biocatalytic oxidation by chloroperoxidase from caldariomyces fumago in polymersome nanoreactors",
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",
keywords = "IR-77781, METIS-263223",
author = "{de Hoog}, H.M. and M. Nallani and Cornelissen, {Jeroen Johannes Lambertus Maria} and A.E. Rowan and J.M. Nolte and I.W.C.E. Arends",
year = "2009",
doi = "10.1039/B911370C",
language = "Undefined",
volume = "7",
pages = "4604--4610",
journal = "Organic & biomolecular chemistry",
issn = "1477-0520",
publisher = "Royal Society of Chemistry",

}

Biocatalytic oxidation by chloroperoxidase from caldariomyces fumago in polymersome nanoreactors. / de Hoog, H.M.; Nallani, M.; Cornelissen, Jeroen Johannes Lambertus Maria; Rowan, A.E.; Nolte, J.M.; Arends, I.W.C.E.

In: Organic & biomolecular chemistry, Vol. 7, 2009, p. 4604-4610.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Biocatalytic oxidation by chloroperoxidase from caldariomyces fumago in polymersome nanoreactors

AU - de Hoog, H.M.

AU - Nallani, M.

AU - Cornelissen, Jeroen Johannes Lambertus Maria

AU - Rowan, A.E.

AU - Nolte, J.M.

AU - Arends, I.W.C.E.

PY - 2009

Y1 - 2009

N2 - 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

AB - 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

KW - IR-77781

KW - METIS-263223

U2 - 10.1039/B911370C

DO - 10.1039/B911370C

M3 - Article

VL - 7

SP - 4604

EP - 4610

JO - Organic & biomolecular chemistry

JF - Organic & biomolecular chemistry

SN - 1477-0520

ER -