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 oxidative fermentation of D-sorbitol by the PQQ biosynthesis enhanced engineered strains. The symbols ▼, ●, ▲, and ■ represent the concentration of D-sorbitol, L-sorbose, L-sorbosone, and 2-KLG produced by G. oxydans/pGUC-tufB-SH3-sdh-GGGGS-sndh-tufB-SH3lig-(GGGGS)2-cutA-tufB-pqqABCDE, respectively. The symbol ○ represents OD600 of G. oxydans/pGUC-tufB-SH3-sdh-GGGGS-sndh-tufB-SH3lig-(GGGGS)2-cutA-tufB-pqqABCDE, respectively. Error bars represent the standard deviation of three biological replicates.</div>

Journal of Chemistry

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Figure 7

Figure 7: 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 7 | 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 