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Novel Strategy for Malic Acid Production in Recombinant Escherichia coli via Protein Colocalization
Kumaravel ASHOKKUMAR,Jae Hoon JEONG,Soon Ho HONG 한국생물공학회 2021 한국생물공학회 학술대회 Vol.2021 No.10
Protein scaffold complex strategy was introduced between the enzymes phosphoenolpyruvate carboxylase (Ppc) and malate dehydrogenase (MdhA) in non-oxidative malic acid pathway (Fig. 1). The protein scaffold can increase the carbon flux towards the malic acid production by closely co-localization of pathway enzymes. Various culture conditions such as pH, temperature and glucose concentration were optimized for effective malic acid production. Similarly, various competing pathway mutant E. coli strains were also tested for improved malic acid production.
Jae Hoon JEONG,Kumaravel ASHOKKUMAR,Soon Ho HONG 한국생물공학회 2021 한국생물공학회 학술대회 Vol.2021 No.10
In this study, constructed Escherichia coli could efficiently adsorb fenitrothion by displaying a pesticide-binding peptide on it using the anchoring motif OmpC. A codon-optimized, pesticide-binding peptide was attached to the C-terminus of OmpC at loop 7 (993 bp). The efficiency of fenitrothion binding by the monomer peptide was evaluated under different temperatures, pH levels, and fenitrothion concentrations. To enhance fenitrothion adsorption, a dimer of pesticide-binding peptide was also constructed and displayed. Compared with the peptide monomer, the dimer-displaying strain showed superior fenitrothion-binding ability. The performance of the strains was evaluated in artificial polluted soil, and their morphology was analyzed by FE-SEM. The results showed that these two kinds of constructed strains can adsorb fenitrothion in contaminated environments with no cellular activity reduction.