Biotechnology Letters, Vol.34, No.5, 889-893, 2012
Accumulation of pyruvate by changing the redox status in Escherichia coli
Pyruvate was produced from glucose by BW25113 that contained formate dehydrogenase (FDH) from . In aerobic shake-flask culture ( (L) = 4.9 min(-1)), the recombinant strain produced 6.7 g pyruvate l(-1) after 24 h with 4 g sodium formate l(-1) and a yield of 0.34 g pyruvate g glucose(-1). These values were higher than those of the original strain (0.2 g l(-1) pyruvate and 0.02 g pyruvate g glucose(-1)). Based on the reaction mechanism of FDH, the introduction of FDH into . enhances the accumulation of pyruvate by the regeneration of NADH from NAD(+) since NAD(+) is a shared cosubstrate with the pyruvate dehydrogenase complex, which decarboxylates pyruvate to acetyl-CoA and CO2. The oxygenation level was enough high to inactivate lactate dehydrogenase, which was of benefit to pyruvate accumulation without lactate as a by-product.