Co-localization of GABA shunt enzymes for the efficient production of gamma-aminobutyric acid via GABA shunt pathway in escherichia coli

Van Dung Pham, Sivachandiran Somasundaram, Si Jae Park, Seung Hwan Lee, Soon Ho Hong

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Gamma-aminobutyric acid (GABA) is a non-protein amino acid, which is an important inhibitor of neurotransmission in the human brain. GABA is also used as the precursor of biopolymer Nylon-4 production. In this study, the carbon flux from the tricarboxylic acid cycle was directed to the GABA shunt pathway for the production of GABA from glucose. The GABA shunt enzymes succinate-semialdehyde dehydrogenase (GabD) and GABA aminotransferase (GabT) were co-localized along with the GABA transporter (GadC) by using a synthetic scaffold complex. The co-localized enzyme scaffold complex produced 0.71 g/l of GABA from 10 g/l of glucose. Inactivation of competing metabolic pathways in mutant E. coli strains XBM1 and XBM6 increased GABA production 13% to reach 0.80 g/l GABA by the enzymes co-localized and expressed in the mutant strains. The recombinant E. coli system developed in this study demonstrated the possibility of the pathway of the GABA shunt as a novel GABA production pathway.

Original languageEnglish
Pages (from-to)710-716
Number of pages7
JournalJournal of Microbiology and Biotechnology
Volume26
Issue number4
DOIs
StatePublished - 28 Apr 2016

Keywords

  • Carbon flux
  • Co-localization
  • Gamma-aminobutyric acid
  • Glucose
  • Recombinant DNA
  • Scaffold complex

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