Lactobacillus plantarum ldhL gene: overexpression and deletion.

Ferain, T.;Garmyn, D.;Bernard, N.;Hols, Pascal;Delcour, Jean
(1994) Journal of bacteriology — Vol. 176, n° 3, p. 596-601 (1994)

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Authors
  • Ferain, T.
    Author
  • Garmyn, D.
    Author
  • Bernard, N.
    Author
  • Hols, Pascalorcid-logoUCLouvain
    Author
  • Delcour, JeanUCLouvain
    Author
Abstract
Lactobacillus plantarum is a lactic acid bacterium that converts pyruvate to L-(+)- and D-(-)-lactate with stereospecific enzymes designated L-(+)- and D-(-)-lactate dehydrogenase (LDH), respectively. A gene (designated ldhL) that encodes L-(+)-lactate dehydrogenase from L. plantarum DG301 was cloned by complementation in Escherichia coli. The nucleotide sequence of the ldhL gene predicted a protein of 320 amino acids closely related to that of Lactobacillus pentosus. A multicopy plasmid bearing the ldhL gene without modification of its expression signals was introduced in L. plantarum. L-LDH activity was increased up to 13-fold through this gene dosage effect. However, this change had hardly any effect on the production of L-(+)- and D-(-)-lactate. A stable chromosomal deletion in the ldhL gene was then constructed in L. plantarum by a two-step homologous recombination process. Inactivation of the gene resulted in the absence of L-LDH activity and in exclusive production of the D isomer of lactate. However, the global concentration of lactate in the culture supernatant remained unchanged.
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Citations

Ferain, T., Garmyn, D., Bernard, N., Hols, P., & Delcour, J. (1994). Lactobacillus plantarum ldhL gene: overexpression and deletion. Journal of bacteriology, 176(3), 596-601. https://hdl.handle.net/2078.5/135145 (Original work published 1994)