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>The specific activities of SDH and SNDH in the CutA-based engineered strain and the control strain at different temperatures. A, C, and E are SDH and SNDH specific activities of G. oxydans/pGUC-tufB-sdh-GGGGS-sndh at 30°C, 35°C, and 37°C, respectively. B, D, and F are SDH and SNDH specific activities of G. oxydans/pGUC-tufB-SH3-sdh-GGGGS-sndh-tufB-SH3lig-(GGGGS)2-cutA at 30°C, 35°C, and 37°C, respectively. Error bars represent the standard deviation of three biological replicates.</div>

Journal of Chemistry

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Figure 6

Figure 6: 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 6 | 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 