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Sivachandiran Somasundaram,Jaehoon Jeong,Ganesh Irisappan,김태완,홍순호 한국생물공학회 2020 Biotechnology and Bioprocess Engineering Vol.25 No.1
To produce malic acid from non-oxidative pathway route in Escherichia coli using two key enzymes and synthetic scaffold complex. E. coli was engineered to produce malic acid from glucose by co-localization of two key enzymes phosphoenolpyruvate carboxylase (Ppc) and malate dehydrogenase (MdhA) with synthetic scaffold complex. Scaffold plasmid has produced the maximum concentration of 3.51 g/L malic acid from 10 g/L glucose in 48 h of culture. pH 5.5 and temperature 30°C were optimum for malic acid production without any engineering of competing metabolic pathways. E. coli mutant strains and different concentrations of glucose also tested. When 50 g/L glucose was used as substrate, 20.4 g/L of malic acid was produced.
( Sivachandiran Somasundaram ),( Murali Kannan Maruthamuthu ),( Irisappan Ganesh ),( Gyeong Tae Eom ),( Soon Ho Hong ) 한국미생물생명공학회(구 한국산업미생물학회) 2017 Journal of microbiology and biotechnology Vol.27 No.9
Gamma-aminobutyric acid is a precursor of nylon-4, which is a promising heat-resistant biopolymer. GABA can be produced from the decarboxylation of glutamate by glutamate decarboxylase. In this study, a synthetic scaffold complex strategy was employed involving the Neurospora crassa glutamate decarboxylase (GadB) and Escherichia coli GABA antiporter (GadC) to improve GABA production. To construct the complex, the SH3 domain was attached to the N. crassa GadB, and the SH3 ligand was attached to the N-terminus, middle, and C-terminus of E. coli GadC. In the C-terminus model, 5.8 g/l of GABA concentration was obtained from 10 g/l glutamate. When a competing pathway engineered strain was used, the final GABA concentration was further increased to 5.94 g/l, which corresponds to 97.5% of GABA yield. With the introduction of the scaffold complex, the GABA productivity increased by 2.9 folds during the initial culture period.
홍순호,( Sivachandiran Somasundaram ),석정욱,정재훈 한국공업화학회 2016 한국공업화학회 연구논문 초록집 Vol.2016 No.1
GABA can be used for the production of pharmaceuticals and functional foods. Due to the increasing demand of GABA, it is essential to create an effective alternative pathway for the GABA production. In this study, Escherichia coli were engineered to produce GABA from glucose via GABA shunt, which consists of succinate dehydrogenase, succinate- semialdehyde dehydrogenase and GABA aminotransferase. The three enzymes were physically attached each other through synthetic scaffold, and the Krebs cycle flux was redirected to GABA pathway. By introduction of synthetic scaffold, 0.75 g/l of GABA was produced from 10 g/l of glucose at 30oC and pH 6.5. The inactivation of competing metabolic pathways provided 15.4% increase of the final GABA concentration. <sup>**</sup>This work was supported by a grant from the Next-Generation BioGreen 21 Program (SSAC, grant number: PJ011116) by RDA, and Basic Science Research Program by the Ministry of Education (NRF- 2014R1A1A2054726).
Pham, Van Dung,Somasundaram, Sivachandiran,Lee, Seung Hwan,Park, Si Jae,Hong, Soon Ho Springer-Verlag 2016 Applied biochemistry and biotechnology Vol.178 No.7
<P>In general, gamma-aminobutyric acid (GABA) pathway involves the decarboxylation of glutamate, which is produced from sugar by Corynebacterium fermentation. GABA can be used for the production of pharmaceuticals and functional foods. Due to the increasing demand of GABA, it is essential to create an effective alternative pathway for the GABA production. In this study, Escherichia coli were engineered to produce GABA from glucose via GABA shunt, which consists of succinate dehydrogenase, succinate-semialdehyde dehydrogenase, and GABA aminotransferase. The three enzymes were physically attached to each other through a synthetic scaffold, and the Krebs cycle flux was redirected to the GABA pathway. By introduction of synthetic scaffold, 0.75 g/l of GABA was produced from 10 g/l of glucose at 30 A degrees C and pH 6.5. The inactivation of competing metabolic pathways provided 15.4 % increase in the final GABA concentration.</P>
Van Dung Pham,Sivachandiran Somasundaram,이승환,박시재,홍순호 한국생물공학회 2016 Biotechnology and Bioprocess Engineering Vol.21 No.2
Nylon 4 is a biodegradable polymer which can be produced from the monomer of pyrrolidone. Gammaaminobutyric acid (GABA) is a precursor of pyrrolidone used for the production of bioplastics. In this study, Escherichia coli were engineered to produce gammaaminobutyric acid from glucose via an alternative novel pathway by the introduction of synthetic scaffolds. The GABA pathway constructed contained succinate dehydrogenase, succinate-semialdehyde dehydrogenase and GABA aminotransferase to redirect the Krebs cycle flux to GABA production. By introduction of a synthetic scaffold, production of 0.64 g/L GABA was achieved at 30oC and pH 6.5. Final GABA concentration was increased by 11.3% via the inactivation of competing pathways, and higher initial glucose concentration led to the enhanced final GABA concentration of 1.01 g/L.
Maruthamuthu, Murali kannan,Hong, Jiyeon,Arulsamy, Kulandaisamy,Somasundaram, Sivachandiran,Hong, SoonHo,Choe, Woo-Seok,Yoo, Ik-Keun Springer-Verlag 2018 Bioprocess and biosystems engineering Vol.41 No.4
<P>Peptide-displaying Escherichia coli cells were investigated for use in adsorptive removal of bisphenol A (BPA) both in Luria-Bertani medium including BPA or ATM thermal paper eluted wastewater. Two recombinant strains were constructed with monomeric and dimeric repeats of the 7-mer BPA-binding peptide (KSLENSY), respectively. Greater than threefold increased adsorption of BPA [230.4 A mu mol BPA per g dry cell weight (DCW)] was found in dimeric peptide-displaying cells compared to monomeric strains (63.4 A mu mol per g DCW) in 15 ppm BPA solution. The selective removal of BPA from a mixture of BPA analogs (bisphenol F and bisphenol S) was verified in both monomeric and dimeric peptide-displaying cells. The binding chemistry of BPA with the peptide was assumed, based on molecular docking analysis, to be the interaction of BPA with serine and asparagine residues within the 7-mer peptide sequence. The peptide-displaying cells also functioned efficiently in thermal paper eluted wastewater containing 14.5 ppm BPA.</P>