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Accumulation of pyruvate by changing the redox status in Escherichia coli

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Abstract

Pyruvate was produced from glucose by Escherichia coli BW25113 that contained formate dehydrogenase (FDH) from Mycobacterium vaccae. In aerobic shake-flask culture (K L a = 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 E. coli 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.

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Acknowledgment

We thank Dr. Kurihara of Kyoto University for kindly providing the pFDHADH plasmid.

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Correspondence to Masahito Taya.

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Ojima, Y., Suryadarma, P., Tsuchida, K. et al. Accumulation of pyruvate by changing the redox status in Escherichia coli . Biotechnol Lett 34, 889–893 (2012). https://doi.org/10.1007/s10529-011-0842-y

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  • DOI: https://doi.org/10.1007/s10529-011-0842-y

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