Monday, August 11, 2008
P136

Engineering Escherichia coli for Coenzyme Q10 Production

Andrew Ekins1, Corinne P. Cluis1, Adam M. Burja2, and Vincent J. J. Martin1. (1) Department of Biology, Concordia University, 7141 Sherbrooke West, Montreal, QC H4B 1R6, Canada, (2) Metabolic Engineering and Fermentation, Ocean Nutrition Canada, 101 Research Drive, Dartmouth, NS B2Y 4T6, Canada

Currently, there is a large consumer demand for coenzyme Q10 (CoQ10). CoQ is formed by the conjugation of a benzoquinone ring with an isoprenoid side chain of varying length, depending on the species. Escherichia coli naturally produces CoQ8, due to the fact that this particular bacterium expresses an octaprenyl diphosphate synthase. Thus, in order to produce CoQ10 in E. coli, it is necessary to express a decaprenyl diphosphate synthase (dps) to produce a side chain of the appropriate length. A dps has been cloned from a marine bacterium and expressed in E. coli, resulting in the production of CoQ10, as assessed by HPLC analysis. While the introduction of a dps gene into E. coli allows the production of CoQ10, it is imperative to over-produce the molecule for commercial purposes. The benzoquinone ring of CoQ10 is normally derived from the precursor molecule chorismate, and to potentially improve flux towards the production of the benzoquinone ring, sequential mutations have been made to disrupt some of the biosynthetic pathways for the production of aromatic amino acids, menaquinone, enterobactin and folic acid, which also make use of chorismate as a precursor molecule. Additionally, to increase availability of the isoprenoid side chain, a synthetic mevalonate isoprenoid pathway will be introduced; this pathway has been used in the past to dramatically increase intracellular isoprenoid pools in E. coli. Finally, the impact of the various strategies discussed here on the production of CoQ in E. coli will be assessed by HPLC analysis.


Web Page: clone.concordia.ca/vmartin/index.htm

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