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Homofermentative production of D- or L-lactate in metabolically engineered Escherichia coli RR1

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  • L-Lactate Dehydrogenase
  • Lactic Acid
  • Escherichia Coli
  • Lactate Dehydrogenase
  • Reduced Nicotinamide Adenine Dinucleotide
  • Bacterial Metabolism
  • Bacterium Culture
  • Glycolysis
  • Lactobacillus Casei
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We investigated metabolic engineering of fermentation pathways in Escherichia coli for production of optically pure D- or L-lactate. Several pta mutant strains were examined, and a pta mutant of E. coli RR1 which was deficient in the phosphotransacetylase of the Pta-AckA pathway was found to metabolize glucose to D-lactate and to produce a small amount of succinate by-product under anaerobic conditions. An additional mutation in ppc made the mutant produce D-lactate like a homofermentative lactic acid bacterium. When the pta ppc double mutant was grown to higher biomass concentrations under aerobic conditions before it shifted to the anaerobic phase of D-lactate production, more than 62.2 g of D-lactate per liter was produced in 60 h, and the volumetric productivity was 1.04 g/liter/h. To examine whether the blocked acetate flux could be reoriented to a nonindigenous L-lactate pathway, an L-lactate dehydrogenase gene from Lactobacillus casei was introduced into a pta ldhA strain which lacked phosphotransacetylase and D- lactate dehydrogenase. This recombinant strain was able to metabolize glucose to L-lactate as the major fermentation product, and up to 45 g of L-lactate per liter was produced in 67 h. These results demonstrate that the central fermentation metabolism of E. coli can be reoriented to the production of D- lactate, an indigenous fermentation product, or to the production of L- lactate, a nonindigenous fermentation product.

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