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

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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.
Publisher
Amer Soc Microbiology
Issue Date
1999-04
Language
English
Article Type
Article
Keywords

NUCLEOTIDE-SEQUENCE; DEHYDROGENASE GENE; FERMENTATION; MUTANTS; DERIVATIVES; EXPRESSION; CLONING; LACKING

Citation

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, v.65, no.4, pp.1384 - 1389

ISSN
0099-2240
URI
http://hdl.handle.net/10203/72315
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