Functional expression of mammalian NADPH-cytochrome P450 oxidoreductase on the cell surface of Escherichia coli

Cited 25 time in scopus
Metadata Downloads
Title
Functional expression of mammalian NADPH-cytochrome P450 oxidoreductase on the cell surface of Escherichia coli
Author(s)
S K Yim; Heung Chae Jung; Jae Gu Pan; H S Kang; T Ahn; C H Yun
Bibliographic Citation
Protein Expression and Purification, vol. 49, no. 2, pp. 292-298
Publication Year
2006
Abstract
To develop a whole-cell oxidoreductase system without the practical limitation of substrate/product transport, easy preparation, stability of enzymes, and low expression levels, we here report the development of a whole cell biocatalyst displaying rat NADPH-cytochrome P450 oxidoreductase (CPR, 77-kDa) on the surface of Escherichia coli by using ice-nucleation protein from Pseudomonas syringae. Surface localization and functionality of the CPR were verified by flow cytometry, electron microscopy, and measurements of enzyme activities. The results of this study comprise the first report of microbial cell-surface display of diflavin-containing mammalian enzymes. This system will allow us to select and develop oxidoreductases, containing bulky and complex prosthetic groups of FAD and FMN, into practically useful whole-cell biocatalysts for broad biological and biotechnological applications including the selective synthesis of new chemicals and pharmaceuticals, bioconversion, bioremediation, and bio-chip development.
Keyword
diflavin-containing mammalian enzymeoxidoreductasereductionsurface displaywhole-cell biocatalyst
ISSN
1046-5928
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.pep.2006.05.013
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.