Abstract
Glutathione (GSH) is an important bioactive substance applied widely in pharmaceutical and food industries. Due to the strong product inhibition in the GSH biosynthetic pathway, high levels of intracellular content, yield and productivity of GSH are difficult to achieve. Recently, a novel bifunctional GSH synthetase was identified to be less sensitive to GSH. A recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus was constructed for GSH production. In this study, efficient GSH production using this engineered strain was investigated. The cultivation process was optimized by controlling dissolved oxygen (DO), amino acid addition and glucose feeding. 36.8 mM (11.3 g/L) GSH were formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) were added and glucose was supplied as the sole carbon and energy source.
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Acknowledgments
This study was supported by the National Science Foundation for Young Scientist of China (Grant No. 21406065), the Fundamental Research Funds for the Central Universities (Grant No. 222201313007 & 22A201514042), the National Special Fund for State Key Laboratory of Bioreactor Engineering (No. 2060204) and Shanghai Committee of Science and Technology (Grant No. 13DZ1930202).
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Wang, D., Wang, C., Wu, H. et al. Glutathione production by recombinant Escherichia coli expressing bifunctional glutathione synthetase. J Ind Microbiol Biotechnol 43, 45–53 (2016). https://doi.org/10.1007/s10295-015-1707-5
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DOI: https://doi.org/10.1007/s10295-015-1707-5