Metabolic engineering of Escherichia coli for enhanced biosynthesis of poly(3-hydroxybutyrate) based on proteome analysis

Seung Hwan Lee, Kyoung Hee Kang, Eun Young Kim, Tong Un Chae, Young Hoon Oh, Soon Ho Hong, Bong Keun Song, Jonggeon Jegals, Si Jae Park, Sang Yup Lee

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17 Scopus citations

Abstract

We have previously analyzed the proteome of recombinant Escherichia coli producing poly(3-hydroxybutyrate) [P(3HB)] and revealed that the expression level of several enzymes in central metabolism are proportional to the amount of P(3HB) accumulated in the cells. Based on these results, the amplification effects of triosephosphate isomerase (TpiA) and fructose-bisphosphate aldolase (FbaA) on P(3HB) synthesis were examined in recombinant E. coli W3110, XL1-Blue, and W lacI mutant strains using glucose, sucrose and xylose as carbon sources. Amplification of TpiA and FbaA significantly increased the P(3HB) contents and concentrations in the three E. coli strains. TpiA amplification in E. coli XL1-Blue lacI increased P(3HB) from 0.4 to 1.6 to g/l from glucose. Thus amplification of glycolytic pathway enzymes is a good strategy for efficient production of P(3HB) by allowing increased glycolytic pathway flux to make more acetyl-CoA available for P(3HB) biosynthesis.

Original languageEnglish
Pages (from-to)1631-1637
Number of pages7
JournalBiotechnology Letters
Volume35
Issue number10
DOIs
StatePublished - Oct 2013

Bibliographical note

Funding Information:
Acknowledgments This work was supported by 2012 Research Fund of Myongji University and Priority Research Centers Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and Future Planning (MSIP) (2012-0006693). Further support from the Technology Development Program to Solve Climate Changes (Systems metabolic engineering for biorefineries) from the MSIP through the NRF (NRF-2012-C1AAA001-2012M1A2A2026556) is appreciated.

Keywords

  • FbaA
  • Poly(3-hydroxybutyrate)
  • Proteome analysis
  • Recombinant E. coli
  • TpiA

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