Abstract
Objective
To develop a method combining enzymatic catalysis and resting-cell biotransformation to produce allitol from low cost substrate d-glucose.
Results
The recombinant E. coli expressing d-psicose-3-epimerase (DPE), ribitol dehydrogenase (RDH) and formate dehydrogenase (FDH) for allitol production from d-fructose was constructed. The optimizations of the cell catalytic conditions and the cell cultivation conditions were made. Then, 63.4 g allitol L−1 was obtained from 100 g d-fructose L−1 in 4 h catalyzed by the recombinant E. coli cells. In order to decrease the substrate cost, d-glucose was used as the substrate instead of d-fructose and immobilized glucose isomerase was used to convert d-glucose into d-fructose. In order to simplify allitol production process from d-glucose, one-pot reaction using the mixed catalysts was used and the reaction conditions were optimized. Finally, 12.7 g allitol L−1 was obtained from 50 g d-glucose L−1 catalyzed by the mixed catalysts of immobilized glucose isomerase and the recombinant E. coli cells.
Conclusions
Allitol can be efficiently produced from low cost substrate d-glucose by using the method combining enzymatic catalysis and resting-cell biotransformation, which is the first report.
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Acknowledgements
This research was funded by the Key R & D Plan of Shandong Province in 2019 (2019GSF107015), China. The authors would like to thank Chengjia Zhang, Caiyun Sun from the Core Facilities for Life and Environmental Sciences, State Key Lab of Microbial Technology for help and guidance in the experiments.
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Wen, X., Lin, H., Ren, Y. et al. Optimization for allitol production from d-glucose by using immobilized glucose isomerase and recombinant E. coli expressing d-psicose-3-epimerase, ribitol dehydrogenase and formate dehydrogenase. Biotechnol Lett 42, 2135–2145 (2020). https://doi.org/10.1007/s10529-020-02917-x
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DOI: https://doi.org/10.1007/s10529-020-02917-x