Fermentative production of short-chain fatty acids in Escherichia coli

Escherichia coli was engineered for the production of even- and odd-chain fatty acids (FAs) by fermentation. Co-production of thiolase, hydroxybutyryl-CoA dehydrogenase, crotonase and trans-enoyl-CoA reductase from a synthetic operon allowed the production of butyrate, hexanoate and octanoate. Elimi...

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Bibliographic Details
Published in:Microbiology (Society for General Microbiology) 2014-07, Vol.160 (Pt 7), p.1513-1522
Main Authors: Volker, Alexandra R, Gogerty, David S, Bartholomay, Christian, Hennen-Bierwagen, Tracie, Zhu, Huilin, Bobik, Thomas A
Format: Article
Language:English
Subjects:
Bacterial Proteins - genetics
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Biosynthetic Pathways
Butyrates - metabolism
Escherichia coli - genetics
Escherichia coli - metabolism
Fatty Acids, Volatile - chemistry
Fatty Acids, Volatile - metabolism
Fermentation
Glucose - metabolism
Metabolic Engineering
Recombinant Proteins
Time Factors
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Summary:Escherichia coli was engineered for the production of even- and odd-chain fatty acids (FAs) by fermentation. Co-production of thiolase, hydroxybutyryl-CoA dehydrogenase, crotonase and trans-enoyl-CoA reductase from a synthetic operon allowed the production of butyrate, hexanoate and octanoate. Elimination of native fermentation pathways by genetic deletion (ΔldhA, ΔadhE, ΔackA, Δpta, ΔfrdC) helped eliminate undesired by-products and increase product yields. Initial butyrate production rates were high (0.7 g l(-1) h(-1)) but quickly levelled off and further study suggested this was due to product toxicity and/or acidification of the growth medium. Results also showed that endogenous thioesterases significantly influenced product formation. In particular, deletion of the yciA thioesterase gene substantially increased hexanoate production while decreasing the production of butyrate. E. coli was also engineered to co-produce enzymes for even-chain FA production (described above) together with a coenzyme B12-dependent pathway for the production of propionyl-CoA, which allowed the production of odd-chain FAs (pentanoate and heptanoate). The B12-dependent pathway used here has the potential to allow the production of odd-chain FAs from a single growth substrate (glucose) in a more energy-efficient manner than the prior methods.
ISSN:1350-0872
1465-2080
DOI:10.1099/mic.0.078329-0