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Nat Biotechnol. 1999 Jun;17(6):588-92.

Conversion of Lactococcus lactis from homolactic to homoalanine fermentation through metabolic engineering.

Author information

1
Microbial Ingredients Section, NIZO Food Research, Ede, The Netherlands. hols@gene.ucl.ac.be

Abstract

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.

PMID:
10385325
DOI:
10.1038/9902
[Indexed for MEDLINE]

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