Biosynthesis of ethylene glycol in Escherichia coli |
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Authors: | Huaiwei Liu Kristine Rose M Ramos Kris Niño G Valdehuesa Grace M Nisola Won-Keun Lee Wook-Jin Chung |
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Institution: | 1. Energy and Environment Fusion Technology Center (E2FTC), Department of Energy Science and Technology (DEST), Myongji University, Room 8807, Engineering College Building 2, San 38-2, Namdong, Cheoin-gu, Yongin, Gyeonggi, 449-728, South Korea 2. Division of Bioscience and Bioinformatics, Myongji University, Yongin, Gyeonggi, 449-728, South Korea
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Abstract: | Ethylene glycol (EG) is an important platform chemical with steadily expanding global demand. Its commercial production is currently limited to fossil resources; no biosynthesis route has been delineated. Herein, a biosynthesis route for EG production from d-xylose is reported. This route consists of four steps: d-xylose?→?d-xylonate?→?2-dehydro-3-deoxy-d-pentonate?→?glycoaldehyde?→?EG. Respective enzymes, d-xylose dehydrogenase, d-xylonate dehydratase, 2-dehydro-3-deoxy-d-pentonate aldolase, and glycoaldehyde reductase, were assembled. The route was implemented in a metabolically engineered Escherichia coli, in which the d-xylose?→?d-xylulose reaction was prevented by disrupting the d-xylose isomerase gene. The most efficient construct produced 11.7 g?L?1 of EG from 40.0 g?L?1 of d-xylose. Glycolate is a carbon-competing by-product during EG production in E. coli; blockage of glycoaldehyde?→?glycolate reaction was also performed by disrupting the gene encoding aldehyde dehydrogenase, but from this approach, EG productivity was not improved but rather led to d-xylonate accumulation. To channel more carbon flux towards EG than the glycolate pathway, further systematic metabolic engineering and fermentation optimization studies are still required to improve EG productivity. |
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