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Title: Production of long chain alcohols and alkanes upon coexpression of an acyl-ACP reductase and aldehyde-deformylating oxgenase with a bacterial type-I fatty acid synthase in E. coli

Abstract

Microbial long chain alcohols and alkanes are renewable biofuels that could one day replace petroleum-derived fuels. Here we report a novel pathway for high efficiency production of these products in Escherichia coli strain BL21(DE3). We first identified the acyl-ACP reductase/aldehyde deformylase combinations with the highest activity in this strain. Next, we used catalase coexpression to remove toxic byproducts and increase the overall titer. Finally, by introducing the type-I fatty acid synthase from Corynebacterium ammoniagenes, we were able to bypass host regulatory mechanisms of fatty acid synthesis that have thus far hampered efforts to optimize the yield of acyl-ACP-derived products in BL21(DE3). When all these engineering strategies were combined with subsequent optimization of fermentation conditions, we were able to achieve a final titer around 100 mg/L long chain alcohol/alkane products including a 57 mg/L titer of pentadecane, the highest titer reported in E. coli BL21(DE3) to date. The expression of prokaryotic type-I fatty acid synthases offer a unique strategy to produce fatty acid-derived products in E. coli that does not rely exclusively on the endogenous type-II fatty acid synthase system.

Authors:
 [1];  [2];  [1];  [1]
  1. Univ. of Illinois at Urbana-Champaign, Urbana, IL (United States)
  2. Brookhaven National Lab. (BNL), Upton, NY (United States)
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org.:
USDOE Advanced Research Projects Agency - Energy (ARPA-E)
OSTI Identifier:
1213363
Report Number(s):
BNL-108195-2015-JA
Journal ID: ISSN 1742-206X; MBOIBW; R&D Project: DE-AR0000206; CJ0100000
Grant/Contract Number:  
SC00112704
Resource Type:
Accepted Manuscript
Journal Name:
Molecular BioSystems
Additional Journal Information:
Journal Volume: 11; Journal Issue: 9; Journal ID: ISSN 1742-206X
Publisher:
Royal Society of Chemistry
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Coursolle, Dan, Shanklin, John, Lian, Jiazhang, and Zhao, Huimin. Production of long chain alcohols and alkanes upon coexpression of an acyl-ACP reductase and aldehyde-deformylating oxgenase with a bacterial type-I fatty acid synthase in E. coli. United States: N. p., 2015. Web. doi:10.1039/C5MB00268K.
Coursolle, Dan, Shanklin, John, Lian, Jiazhang, & Zhao, Huimin. Production of long chain alcohols and alkanes upon coexpression of an acyl-ACP reductase and aldehyde-deformylating oxgenase with a bacterial type-I fatty acid synthase in E. coli. United States. doi:10.1039/C5MB00268K.
Coursolle, Dan, Shanklin, John, Lian, Jiazhang, and Zhao, Huimin. Tue . "Production of long chain alcohols and alkanes upon coexpression of an acyl-ACP reductase and aldehyde-deformylating oxgenase with a bacterial type-I fatty acid synthase in E. coli". United States. doi:10.1039/C5MB00268K. https://www.osti.gov/servlets/purl/1213363.
@article{osti_1213363,
title = {Production of long chain alcohols and alkanes upon coexpression of an acyl-ACP reductase and aldehyde-deformylating oxgenase with a bacterial type-I fatty acid synthase in E. coli},
author = {Coursolle, Dan and Shanklin, John and Lian, Jiazhang and Zhao, Huimin},
abstractNote = {Microbial long chain alcohols and alkanes are renewable biofuels that could one day replace petroleum-derived fuels. Here we report a novel pathway for high efficiency production of these products in Escherichia coli strain BL21(DE3). We first identified the acyl-ACP reductase/aldehyde deformylase combinations with the highest activity in this strain. Next, we used catalase coexpression to remove toxic byproducts and increase the overall titer. Finally, by introducing the type-I fatty acid synthase from Corynebacterium ammoniagenes, we were able to bypass host regulatory mechanisms of fatty acid synthesis that have thus far hampered efforts to optimize the yield of acyl-ACP-derived products in BL21(DE3). When all these engineering strategies were combined with subsequent optimization of fermentation conditions, we were able to achieve a final titer around 100 mg/L long chain alcohol/alkane products including a 57 mg/L titer of pentadecane, the highest titer reported in E. coli BL21(DE3) to date. The expression of prokaryotic type-I fatty acid synthases offer a unique strategy to produce fatty acid-derived products in E. coli that does not rely exclusively on the endogenous type-II fatty acid synthase system.},
doi = {10.1039/C5MB00268K},
journal = {Molecular BioSystems},
number = 9,
volume = 11,
place = {United States},
year = {2015},
month = {6}
}

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Cited by: 7 works
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