Fed-batch production of l-tryptophan from glycerol using recombinant Escherichia coli

Julia Tröndle, Natalia Trachtmann, Georg A. Sprenger, Dirk Weuster-Botz

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

l-tryptophan is an essential amino acid of high industrial interest that is routinely produced by microbial processes from glucose as carbon source. Glycerol is an alternative substrate providing a variety of economic and metabolic advantages. Process performance of the recombinant l-tryptophan producer Escherichia coli NT367 was studied in controlled fed-batch processes. The chromosome of the recombinant l-tryptophan producer was equipped with additional genes coding for enzymes of the aromatic amino acids biosynthetic pathway and l-serine biosynthesis, including genes for feedback-resistant enzyme variants (trpE fbr, aroFBL, and serA fbr), deletions of enzymatic steps for the degradation of precursors or the product l-tryptophan (sdaB and tnaA), and alterations in the regulation of l-tryptophan metabolism (deletion of trpL and trpR). The impact of glycerol supply rates as well as the application of a multicopy plasmid (pF112- aroFBL -kan) were investigated in fully controlled stirred-tank bioreactors on a 15 L scale. The combination of E. coli NT367 carrying pF112- aroFBL -kan and an appropriate biomass-specific glycerol supply-rate resulted in the highest final product concentration of 12.5 g L −1 l-tryptophan with the lowest concentrations of other aromatic amino acids. Fed-batch production of l-tryptophan from glycerol was shown for the first time with recombinant E. coli.

Original languageEnglish
Pages (from-to)2881-2892
Number of pages12
JournalBiotechnology and Bioengineering
Volume115
Issue number12
DOIs
StatePublished - Dec 2018

Keywords

  • Escherichia coli
  • fed-batch process
  • glycerol
  • l-tryptophan
  • plasmid

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