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Itaconic acid, an unsaturated C5-dicarboxylic acid, is a biobased building block for the polymer industry. The purpose of this study was to establish proof of principle for an anaerobic fermentation process for the production of itaconic acid by modification of the mixed acid fermentation pathway of  E. coli .  E. coli  BW25113 (DE3) and the phosphate acetyltransferase ( pta ) and lactate dehydrogenase ( ldhA ) deficient strain  E. coli  BW25113 (DE3) Δ pta -Δ ldhA  were used to study anaerobic itaconate production in  E. coli . Heterologous expression of the gene encoding  cis -aconitate decarboxylase ( cadA)  from  A. terreus  in  E. coli  BW25113 (DE3) did not result in itaconate production under anaerobic conditions, but 0.08 mM of itaconate was formed when the genes encoding citrate synthase ( gltA ) and aconitase ( acnA ) from  Corynebacterium glutamicum  were also expressed. The same amount was produced when  cadA  was expressed in  E. coli  BW25113 (DE3) Δ pta -Δ ldhA . The titre increased 8 times to 0.66 mM (1.2 % Cmol) when  E. coli  BW25113 (DE3) Δ pta -Δ ldhA  also expressed  gltA  and  acnA . In addition, this strain produced 8.5 mM (13 % Cmol) of glutamate. The use of a nitrogen-limited growth medium reduced the accumulation of glutamate by nearly 50 % compared to the normal medium, and also resulted in a more than 3-fold increase of the itaconate titre to 2.9 mM. These results demonstrated that  E. coli  has potential to produce itaconate and glutamate under anaerobic conditions, closing the redox balance by co-production of succinate or ethanol with H 2  and CO 2 .

Metabolic engineering of the mixed-acid fermentation pathway of Escherichia coli for anaerobic production of glutamate and itaconate