Lysine and glutamate production by Corynebacterium glutamicum on glucose, fructose and sucrose: Roles of malic enzyme and fructose-1,6-bisphosphatase

Georgi, Tobias; Rittmann, Doris; Wendisch, Volker F.

doi:10.1016/j.ymben.2005.05.001

Cited by 150 publications

(107 citation statements)

References 55 publications

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“…We could recently show that overexpression of the malE gene encoding malic enzyme in the genetically defined C. glutamicum strain DM1730 has no positive effect on lysine production on glucose, fructose, glucose/fructose, or sucrose (Georgi et al 2005). Whereas overexpression of fbp in this strain did not effect lysine production on glucose, fructose, or a glucose/fructose mixture, the lysine yield on sucrose was increased twofold (Georgi et al 2005).…”

Section: Introductionmentioning

confidence: 95%

“…As fructose is transported into the cell as fructose-1-phosphate by a PEP-dependent phosphotransferase system and enters glycolysis after phosphorylation to fructose-1,6-bisphosphate (Kotrba et al 2001;Parche et al 2001), overexpression of the fructose-1,6-bisphosphatase gene fbp (Rittmann et al 2003) was alternatively proposed to increase the PPP flux as well as lysine production on fructose (Kiefer et al 2004;Pons et al 1996). We could recently show that overexpression of the malE gene encoding malic enzyme in the genetically defined C. glutamicum strain DM1730 has no positive effect on lysine production on glucose, fructose, glucose/fructose, or sucrose (Georgi et al 2005). Whereas overexpression of fbp in this strain did not effect lysine production on glucose, fructose, or a glucose/fructose mixture, the lysine yield on sucrose was increased twofold (Georgi et al 2005).…”

Section: Introductionmentioning

confidence: 99%

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Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves l-lysine formation

Kabus

Georgi

Wendisch

et al. 2007

Appl Microbiol Biotechnol

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124

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A critical factor in the biotechnological production of L-lysine with Corynebacterium glutamicum is the sufficient supply of NADPH. The membrane-integral nicotinamide nucleotide transhydrogenase PntAB of Escherichia coli can use the electrochemical proton gradient across the cytoplasmic membrane to drive the reduction of NADP + via the oxidation of NADH. As C. glutamicum does not possess such an enzyme, we expressed the E. coli pntAB genes in the genetically defined C. glutamicum lysineproducing strain DM1730, resulting in membrane-associated transhydrogenase activity of 0.7 U/mg protein. When cultivated in minimal medium with 10% (w/v) carbon source, the presence of transhydrogenase slightly reduced glucose consumption, whereas the consumption of fructose, glucose plus fructose, and, in particular, sucrose was stimulated. Biomass was increased by pntAB expression between 10 and 30% on all carbon sources tested. Most importantly, the lysine concentration was increased in the presence of transhydrogenase by ∼10% on glucose, ∼70% on fructose, ∼50% on glucose plus fructose, and even by ∼300% on sucrose. Thus, the presence of a proton-coupled transhydrogenase was shown to be an efficient way to improve lysine production by C. glutamicum. In contrast, pntAB expression had a negative effect on growth and glutamate production of C. glutamicum wild type.

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Section: Introductionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves l-lysine formation

Kabus

Georgi

Wendisch

et al. 2007

Appl Microbiol Biotechnol

Self Cite

124

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“…However, overexpression of the malic enzyme gene did not result in improved lysine production independent from the carbon source tested [134].…”

Section: Metabolic Fluxes Of Nadph Metabolismmentioning

confidence: 84%

Analysis and Engineering of Metabolic Pathway Fluxes in Corynebacterium glutamicum

Wittmann

2010

Biosystems Engineering I

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The Gram-positive soil bacterium Corynebacterium glutamicum was discovered as a natural overproducer of glutamate about 50 years ago. Linked to the steadily increasing economical importance of this microorganism for production of glutamate and other amino acids, the quest for efficient production strains has been an intense area of research during the past few decades. Efficient production strains were created by applying classical mutagenesis and selection and especially metabolic engineering strategies with the advent of recombinant DNA technology. Hereby experimental and computational approaches have provided fascinating insights into the metabolism of this microorganism and directed strain engineering. Today, C. glutamicum is applied to the industrial production of more than 2 million tons of amino acids per year. The huge achievements in recent years, including the sequencing of the complete genome and efficient post genomic approaches, now provide the basis for a new, fascinating era of research -analysis of metabolic and regulatory properties of C. glutamicum on a global scale towards novel and superior bioprocesses.

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“…A deletion of the phosphoglucose isomerase gene drives the complete flux from glucose-6-phosphate into the pentose phosphate pathway and was shown to increase L-lysine production but to the cost of reduced growth (Marx et al, 2003). Redirection of the glycolytic flux towards the entry of the pentose phosphate pathway was furthermore achieved by overexpression of the fructose-bisphosphatase gene (Becker et al, 2005, Georgi et al, 2005 as well as use of feedback resistant variants of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase (Becker et al, 2007, Ohnishi et al, 2005. Also the increase of NADP availability by overexpression of a NAD kinase gene resulted in increased L-lysine production (Lindner et al, 2010).…”

Section: Amino Acidsmentioning

confidence: 99%

Use of Glycerol in Biotechnological Applications

Wendisch¹,

Lindner²,

Meiswinkel³

2011

Biodiesel- Quality, Emissions and by-Products

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Lysine and glutamate production by Corynebacterium glutamicum on glucose, fructose and sucrose: Roles of malic enzyme and fructose-1,6-bisphosphatase

Cited by 150 publications

References 55 publications

Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves l-lysine formation

Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves l-lysine formation

Analysis and Engineering of Metabolic Pathway Fluxes in Corynebacterium glutamicum

Use of Glycerol in Biotechnological Applications

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