TY - JOUR
T1 - Efficient gamma-aminobutyric acid bioconversion by employing synthetic complex between glutamate decarboxylase and glutamate/GABA antiporter in engineered Escherichia coli
AU - Le Vo, Tam Dinh
AU - Ko, Ji Seun
AU - Park, Si Jae
AU - Lee, Seung Hwan
AU - Hong, Soon Ho
N1 - Funding Information:
This work was supported by a grant from the Next-Generation BioGreen 21 Program (SSAC, Grant Number: PJ00954904), Rural Development Administration, Republic of Korea.
PY - 2013/8
Y1 - 2013/8
N2 - 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.
AB - 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.
KW - Gamma-aminobutyric acid
KW - Glutamate decarboxylase
KW - Glutamate/GABA antiporter
KW - Synthetic protein complex
UR - http://www.scopus.com/inward/record.url?scp=84880806864&partnerID=8YFLogxK
U2 - 10.1007/s10295-013-1289-z
DO - 10.1007/s10295-013-1289-z
M3 - Article
C2 - 23729191
AN - SCOPUS:84880806864
SN - 1367-5435
VL - 40
SP - 927
EP - 933
JO - Journal of Industrial Microbiology and Biotechnology
JF - Journal of Industrial Microbiology and Biotechnology
IS - 8
ER -