Efficient Optimization of Gluconobacter oxydans Based on Protein Scaffold-Trimeric CutA to Enhance the Chemical Structure Stability of Enzymes for the Direct Production of 2-Keto-L-gulonic Acid

<div>Time course of fermentation by CutA-based engineered strain. The symbols ▲ and △ represent the concentration of 2-KLG produced by G. oxydans/pGUC-tufB-SH3-sdh-GGGGS-sndh-tufB-SH3lig-(GGGGS)2-cutA and G. oxydans/pGUC-tufB-sdh-GGGGS-sndh, respectively. The symbols ● and ○ represent OD600 of G. oxydans/pGUC-tufB-SH3-sdh-GGGGS-sndh-tufB-SH3lig-(GGGGS)2-cutA and G. oxydans/pGUC-tufB-sdh-GGGGS-sndh, respectively. Error bars represent the standard deviation of three biological replicates.</div>

Journal of Chemistry

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Figure 4

Figure 4: Efficient Optimization of Gluconobacter oxydans Based on Protein Scaffold-Trimeric CutA to Enhance the Chemical Structure Stability of Enzymes for the Direct Production of 2-Keto-L-gulonic Acid

Figure 4 | Efficient Optimization of Gluconobacter oxydans Based on Protein Scaffold-Trimeric CutA to Enhance the Chemical Structure Stability of Enzymes for the Direct Production of 2-Keto-L-gulonic Acid 