Protein production by Escherichia coli wild-type and DeltaptsG mutant strains with IPTG induction at the onset.
During Escherichia coli growth on glucose, uptake exceeds the requirement of flux to precursors and the surplus is excreted as acetate. Beside the loss of carbon source, the excretion of a weak acid may result in increased energetic demands and hence a decreased yield. The deletion of ptsG, the gene coding for one of the components (IICB(Glc)) of the glucose-phosphoenolpyruvate phosphotransferase system (Glc-PTS) reduced glucose consumption and acetate excretion. Induction of protein production at the onset of cultivation decreased growth rate and glucose consumption rate for both the WT and the mutant strains. The mutant strain produced beta-galactosidase at higher rates than the wild-type strain while directing more carbon into biomass and CO(2) and less into acetate.
Picon
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SILS, BioCentrum Amsterdam, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV Amsterdam, The Netherlands. apicon@inia.es
de Mattos
M J Teixeira
MJ
Postma
P W
PW
D018533:Biomass; D019149:Bioreactors; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D005818:Genetic Engineering; D005947:Glucose / Q000378:metabolism; D007544:Isopropyl Thiogalactoside / Q000378:metabolism*; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000235:genetics* / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism*
D007544:Isopropyl Thiogalactoside; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C031629:phosphoenolpyruvate-glucose phosphotransferase; D001616:beta-Galactosidase; D005947:Glucose