ArticleAMB Express2016
Extracellular expression of glutamate decarboxylase B in Escherichia coli to improve gamma-aminobutyric acid production.
Article in AMB Express, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- Predatory myxobacteria lay at the cross-roads of metallo-β-lactamase evolution.Communications biology · 2026Article
- Cloning, expression, purification, and characterization of glutamate decarboxylase (Rv3432c) from Mycobacterium tuberculosis.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- Microbial chassis design and engineering for production of gamma-aminobutyric acid.World journal of microbiology & biotechnology · 2024Review
- Expression and Transformation Characteristics of a Novel Glutamic Acid Decarboxylase LcGAD10s and Its Application on Sufu Processing.Foods (Basel, Switzerland) · 2023Article
- Effect of DR1558, a Deinococcus radiodurans response regulator, on the production of GABA in the recombinant Escherichia coli under low pH conditions.Microbial cell factories · 2020Article
- Ribosomal binding site sequences and promoters for expressing glutamate decarboxylase and producing γ-aminobutyrate in Corynebacterium glutamicum.AMB Express · 2018Article
- Non-peptide guided auto-secretion of recombinant proteins by super-folder green fluorescent protein in Escherichia coli.Scientific reports · 2017Article
- Overexpression of ppc or deletion of mdh for improving production of γ-aminobutyric acid in recombinant Corynebacterium glutamicum.World journal of microbiology & biotechnology · 2017Article
- Mechanisms of microbial-neuronal interactions in pain and nociception.Neurobiology of pain (Cambridge, Mass.)Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli overexpressing glutamate decarboxylase GadB can produce gamma-aminobutyric acid with addition of monosodium glutamate. The yield and productivity of gamma-aminobutyric acid might be significantly improved if the overexpressed GadB in E. coli cells can be excreted outside, where it can directly transforms monosodium glutamate to gamma-aminobutyric acid. In this study, GadB was fused to signal peptides TorA or PelB, respectively, and overexpressed in E. coli BL21(DE3). It was found that TorA could facilitate GadB secretion much better than PelB. Conditions for GadB secretion and gamma-aminobutyric acid production were optimized in E. coli BL21(DE3)/pET20b-torA-gadB, leading the secretion of more than half of the overexpressed GadB. Fed-batch fermentation for GadB expression and gamma-aminobutyric acid production of BL21(DE3)/pET20b-torA-gadB was sequentially performed in one fermenter; 264.4 and 313.1 g/L gamma-aminobutyric acid were obtained with addition of monosodium glutamate after 36 and 72 h, respectively.
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