Efficient gamma-aminobutyric acid bioconversion by employing synthetic complex between glutamate decarboxylase and glutamate/GABA antiporter in engineered Escherichia coli

Tam Dinh Le Vo, Ji Seun Ko, Si Jae Park, Seung Hwan Lee, Soon Ho Hong

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

Gamma-aminobutyric acid (GABA) is a precursor of one of the most promising heat-resistant biopolymers, Nylon-4, and can be produced by the decarboxylation of monosodium glutamate (MSG). In this study, a synthetic protein complex was applied to improve the GABA conversion in engineered Escherichia coli. Complexes were constructed by assembling a single protein-protein interaction domain SH3 to the glutamate decarboxylase (GadA and GadB) and attaching a cognate peptide ligand to the glutamate/GABA antiporter (GadC) at the N-terminus, C-terminus, and the 233rd amino acid residue. When GadA and GadC were co-overexpressed via the C-terminus complex, a GABA concentration of 5.65 g/l was obtained from 10 g/l MSG, which corresponds to a GABA yield of 93 %. A significant increase of the GABA productivity was also observed where the GABA productivity increased 2.5-fold in the early culture period due to the introduction of the synthetic protein complex. The GABA pathway efficiency and GABA productivity were enhanced by the introduction of the complex between Gad and glutamate/GABA antiporter.

Original languageEnglish
Pages (from-to)927-933
Number of pages7
JournalJournal of Industrial Microbiology and Biotechnology
Volume40
Issue number8
DOIs
StatePublished - Aug 2013

Keywords

  • Gamma-aminobutyric acid
  • Glutamate decarboxylase
  • Glutamate/GABA antiporter
  • Synthetic protein complex

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