Efficient production of gamma-aminobutyric acid using Escherichia coli by co-localization of glutamate synthase, glutamate decarboxylase, and GABA transporter. (1st January 2016)

• Record Type: Journal Article
• Authors: Dung Pham, Van; Somasundaram, Sivachandiran; Lee, Seung Hwan; Park, Si Jae; Hong, Soon Ho
• Is Part Of: Journal of industrial microbiology & biotechnology. Volume 43:Number 1(2016)
• Page Start: 79
• Page End: 86
• Publication Date: 2016-01-01
• Subjects: Co-localization -- GABA -- Protein scaffold -- Synthetic biology; Industrial microbiology -- Periodicals; 660.62
• DOI: 10.1007/s10295-015-1712-8
• Languages: English
• ISSNs: 1367-5435

Abstract

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.