Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/91383
Title: Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors
Authors: Madhavan Nallani
Hans-Peter M. de Hoog
Jeroen J. L. M. Cornelissen
Alan E. Rowan
Roeland J. M. Nolte
Isabel W. C. E. Arends
Keywords: DRNTU::Engineering::Materials::Biomaterials
Issue Date: 2009
Source: Madhavan, N., Hans-Peter, M. H., Jeroen, J. L. M. C., Alan, E. R., Roeland, J. M. N., & Isabel, W. C. E. A. (2009). Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors. Organic and biomolecular chemistry, 7, 4604-4610.
Series/Report no.: Organic and biomolecular chemistry
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.
URI: https://hdl.handle.net/10356/91383
http://hdl.handle.net/10220/6788
ISSN: 1477-0520
DOI: http://dx.doi.org/10.1039/b911370c
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:MSE Journal Articles

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