Biochemistry of Vitamin B6 pp 457-460 | Cite as
Industrial Production of L-Tryptophan from Indole and DL-Serine with Two PLP-Dependent Enzymes
Summary
A new enzymatic process of L-tryptophan production has been developed using indole and DL-serine. Two PLP-dependent enzymes simultaneously participate in this process. Tryptophan synthase of Escherichia coli catalyzes ß-substitution reaction of L-serine into L-tryptophan, while serine racemase of Pseudomonas putida converts unreacted D-serine into L-serine. Whole cells of each microorganism were used as the enzyme source. A large scale production was successfully carried out in a 200 liter reactor. After 24hr incubation, 110g/l of L-tryptophan was produced and conversion rates of indole and DL-serine were 100% and 91%, respectively.
Keywords
Enzymatic Process Pseudomonas Putida Enzyme Source 24hr Incubation Serine RacemasePreview
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