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Glutathione production by recombinant Escherichia coli expressing bifunctional glutathione synthetase
Ist Teil von
Journal of industrial microbiology & biotechnology, 2016, Vol.43 (1), p.45-53
Ort / Verlag
Berlin/Heidelberg: Springer Berlin Heidelberg
Erscheinungsjahr
2016
Link zum Volltext
Quelle
SpringerLink (Online service)
Beschreibungen/Notizen
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.