Conversion of Lactococcus lactis from homolactic to homoalanine fermentation through metabolic engineering
(1999) Nature Biotechnology — Vol. 17, n° 6, p. 588-592 (1999)
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- We report the engineering of Lactococcus lactis to produce the amino acid L-alanine. The primary end product of sugar metabolism in wild-type L. lactis is lactate (homolactic fermentation). The terminal enzymatic reaction (pyruvate + NADH-->L-lactate + NAD(+)) is performed by L-lactate dehydrogenase (L-LDH). We rerouted the carbon flux toward alanine by expressing the Bacillus sphaericus alanine dehydrogenase (L-AlaDH; pyruvate + NADH + NH4+-->L-alanine + NAD(+) + H2O). Expression of L-AlaDH in an L-LDH-deficient strain permitted production of alanine as the sole end product (homoalanine fermentation). Finally, stereospecific production (>99%) of L-alanine was achieved by disrupting the gene encoding alanine racemase, opening the door to the industrial production of this stereoisomer in food products or bioreactors.
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Hols, P., Kleerebezem, M., Schanck, A., Ferain, T., Hugenholtz, J., Delcour, J., & de Vos, W. (1999). Conversion of Lactococcus lactis from homolactic to homoalanine fermentation through metabolic engineering. Nature Biotechnology, 17(6), 588-592. https://doi.org/10.1038/9902 (Original work published 1999)