3 Biotech

, 9:50 | Cite as

Different performance of Escherichia coli mutants with defects in the phosphoenolpyruvate: carbohydrate phosphotransferase system under low glucose condition

  • Hao Niu
  • Ruirui Li
  • Juan Gao
  • Xiangyu Fan
  • Qiang Li
  • Pengfei GuEmail author
Original Article


In Escherichia coli, the transport and phosphorylation of glucose is mainly accomplished by the phosphoenolpyruvate-dependent glucose-specific phosphotransferase system (PTSGlc), which is, therefore, frequently selected as a target for engineering to increase the intracellular level of phosphoenolpyruvate. Here we characterized the effects of a low glucose concentration on the growth, glucose consumption, and acetate secretion of individual strains with a single PTSGlc mutation. We found that most mutants accumulated similar amounts of biomass, consumed glucose at lower rates, and secreted less acetate compared with the wild-type parental strain. The exception was the growth-impaired strain MG1655I harboring a ptsI deletion. In summary, the fermentation performance of mutant strains under 5 g/L glucose was obviously different with those strains under 20 g/L glucose. This study is a good complement to the knowledge of PTSGlc in E. coli and indicates that engineering the components of PTSGlc should be carefully optimized, particularly during fermentation in the presence of low concentrations of glucose.


E. coli PTSGlc Glucose Acetate 



This work was financially supported by the National Natural Science Foundation of China (31600066, 31870105, 31600148), the Shandong Provincial Natural Science Foundation (ZR2016CB20, ZR2016CL02), and State Key Laboratory of Microbial Technology Open Projects Fund (M2016-10).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

13205_2019_1584_MOESM1_ESM.docx (347 kb)
Supplementary material 1 (DOCX 347 KB)


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Copyright information

© King Abdulaziz City for Science and Technology 2019

Authors and Affiliations

  • Hao Niu
    • 1
  • Ruirui Li
    • 1
  • Juan Gao
    • 1
  • Xiangyu Fan
    • 1
  • Qiang Li
    • 1
  • Pengfei Gu
    • 1
    Email author
  1. 1.School of Biological Science and TechnologyUniversity of JinanJinanPeople’s Republic of China

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