Journal
JOURNAL OF BIOTECHNOLOGY
Volume 214, Issue -, Pages 63-68Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jbiotec.2015.09.004
Keywords
Antioxidant; Glutathione; Escherichia coil; Bifunctional glutathione synthetase; Fed-batch fermentation
Categories
Funding
- National Science Foundation for Young Scientist of China [21406065]
- Fundamental Research Funds for the Central Universities [222201313007, 22A201514042]
- Shanghai Committee of Science and Technology [13DZ1930202]
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Glutathione (GSH), an important bioactive product, is widely used in production of pharmaceuticals and foods. In this study, four different vector systems, pET28a, pUC18, pUC19-P32, and pUC19-Pabb, were applied for expression of gshF, encoding the bifunctional glutathione synthetase of Streptococcus thermophiles. These four constructs were named as pET28a-gshF, pUC18-gshF, pUC19-P32-gshF and pUC19-Pabb-gshF, respectively, and then introduced into Escherichia coli strain BL21(DE3) for further investigation of protein expression and GSH production. The expression levels of the GshF in BL21(pUC19-P32-gshF) and BL21(pUC19-Pabb-gshF) were much lower than those of BL21(pET28a-gshF) and BL21(pUC18-gshF). In the fed-batch fermentation, the GSH accumulated by BL21(pUC18-gshF) reached 15.21 g/L, which was the highest level of GSH biosynthesis ever reported. Although BL21(pUC19-Pabb-gshF) produced less GSH compared to BL21(pUC18-gshF), the final GSH concentration produced by BL21 (pUC19-Pabb-gshF) still accumulated to 5.09 g/L, which indicated the potential application of the constitutive promoter in GSH production. (C) 2015 Elsevier B.V. All rights reserved.
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