Journal Article PreJuSER-59150

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L-Valine Production with Pyruvate Dehydrogenase Complex-Deficient Corynebacterium glutamicum

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2007
Soc. Washington, DC [u.a.]

Applied and environmental microbiology 73, 2079 - 2084 () [10.1128/AEM.02826-06]

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Abstract: Corynebacterium glutamicum was engineered for the production of L-valine from glucose by deletion of the aceE gene encoding the E1p enzyme of the pyruvate dehydrogenase complex and additional overexpression of the ilvBNCE genes encoding the L-valine biosynthetic enzymes acetohydroxyacid synthase, isomeroreductase, and transaminase B. In the absence of cellular growth, C. glutamicum DeltaaceE showed a relatively high intracellular concentration of pyruvate (25.9 mM) and produced significant amounts of pyruvate, L-alanine, and L-valine from glucose as the sole carbon source. Lactate or acetate was not formed. Plasmid-bound overexpression of ilvBNCE in C. glutamicum DeltaaceE resulted in an approximately 10-fold-lower intracellular pyruvate concentration (2.3 mM) and a shift of the extracellular product pattern from pyruvate and L-alanine towards L-valine. In fed-batch fermentations at high cell densities and an excess of glucose, C. glutamicum DeltaaceE(pJC4ilvBNCE) produced up to 210 mM L-valine with a volumetric productivity of 10.0 mM h(-1) (1.17 g l(-1) h(-1)) and a maximum yield of about 0.6 mol per mol (0.4 g per g) of glucose.

Keyword(s): Alanine: biosynthesis (MeSH) ; Corynebacterium glutamicum: metabolism (MeSH) ; Fermentation (MeSH) ; Isoleucine: biosynthesis (MeSH) ; Lysine: biosynthesis (MeSH) ; Pyruvate Dehydrogenase Complex: genetics (MeSH) ; Pyruvate Dehydrogenase Complex: physiology (MeSH) ; Pyruvic Acid: metabolism (MeSH) ; Valine: biosynthesis (MeSH) ; Pyruvate Dehydrogenase Complex ; Pyruvic Acid ; Alanine ; Lysine ; Valine ; Isoleucine ; J


Note: Record converted from VDB: 12.11.2012

Research Program(s):
  1. Biotechnologie (PBT)

Appears in the scientific report 2007
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 Record created 2012-11-13, last modified 2019-06-25


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