Literature DB >> 26620318

Efficient production of gamma-aminobutyric acid using Escherichia coli by co-localization of glutamate synthase, glutamate decarboxylase, and GABA transporter.

Van Dung Pham1, Sivachandiran Somasundaram1, Seung Hwan Lee2, Si Jae Park3, Soon Ho Hong4.   

Abstract

Gamma-aminobutyric acid (GABA) is an important bio-product, which is used in pharmaceutical formulations, nutritional supplements, and biopolymer monomer. The traditional GABA process involves the decarboxylation of glutamate. However, the direct production of GABA from glucose is a more efficient process. To construct the recombinant strains of Escherichia coli, a novel synthetic scaffold was introduced. By carrying out the co-localization of glutamate synthase, glutamate decarboxylase, and GABA transporter, we redirected the TCA cycle flux to GABA pathway. The genetically engineered E. coli strain produced 1.08 g/L of GABA from 10 g/L of initial glucose. Thus, with the introduction of a synthetic scaffold, we increased GABA production by 2.2-fold. The final GABA concentration was increased by 21.8% by inactivating competing pathways.

Entities:  

Keywords:  Co-localization; GABA; Protein scaffold; Synthetic biology

Mesh:

Substances:

Year:  2015        PMID: 26620318     DOI: 10.1007/s10295-015-1712-8

Source DB:  PubMed          Journal:  J Ind Microbiol Biotechnol        ISSN: 1367-5435            Impact factor:   3.346


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2.  Efficient bioconversion of L-glutamate to γ-aminobutyric acid by Lactobacillus brevis resting cells.

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6.  Effect of DR1558, a Deinococcus radiodurans response regulator, on the production of GABA in the recombinant Escherichia coli under low pH conditions.

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  6 in total

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