Fermentative Production of Halogenated Tryptophan Derivatives with Corynebacterium glutamicum Overexpressing Tryptophanase or Decarboxylase Genes.
Chembiochem
; 23(9): e202200007, 2022 05 04.
Article
en En
| MEDLINE
| ID: mdl-35224830
ABSTRACT
The aromatic amino acid l-tryptophan serves as a precursor for many valuable compounds such as neuromodulators, indoleamines and indole alkaloids. In this work, tryptophan biosynthesis was extended by halogenation followed by decarboxylation to the respective tryptamines or cleavage to the respective indoles. Either the tryptophanase genes tnaAs from E. coli and Proteus vulgaris or the aromatic amino acid decarboxylase genes AADCs from Bacillus atrophaeus, Clostridium sporogenes, and Ruminococcus gnavus were expressed in Corynebacterium glutamicum strains producing (halogenated) tryptophan. Regarding indoles, final titers of 16â
mg L-1 7-Cl-indole and 23â
mg L-1 7-Br-indole were attained. Tryptamine production led to a much higher titer of 2.26â
g L-1 upon expression of AADC from B. atrophaeus. AADC enzymes were shown to be active with halogenated tryptophan inâ
vitro and inâ
vivo and supported production of 0.36â
g L-1 7-Br-tryptamine with a volumetric productivity of 8.3â
mg L-1 h-1 in a fed-batch fermentation.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Triptofanasa
/
Corynebacterium glutamicum
Idioma:
En
Revista:
Chembiochem
Asunto de la revista:
BIOQUIMICA
Año:
2022
Tipo del documento:
Article
País de afiliación:
Alemania