Expression of a soluble flavone synthase allows the biosynthesis of phytoestrogen derivatives in Escherichia coli

Autor: Effendi Leonard, Kok Hong Lim, Mattheos A. G. Koffas, Joseph A. Chemler
Rok vydání: 2006
Předmět:
Zdroj: Applied Microbiology and Biotechnology. 70:85-91
ISSN: 1432-0614
0175-7598
Popis: Flavones are plant secondary metabolites with potent pharmacological properties. We report the functional expression of FSI, a flavonoid 2-oxoglutarate-dependent dioxygenase-encoding flavone synthase from parsley in Escherichia coli. This expression allows the biosynthesis of various flavones from phenylpropanoid acids in recombinant E. coli strains simultaneously expressing five plant-specific flavone biosynthetic genes. The gene ensemble consists of 4CL-2 (4-coumarate:CoA ligase) and FSI (flavone synthase I) from parsley, chsA (chalcone synthase) and chiA (chalcone isomerase) from Petunia hybrida, and OMT1A (7-O-methyltransferase) from peppermint. After a 24-h cultivation, the recombinant E. coli produces significant amounts of apigenin (415 microg/l), luteolin (10 microg/l), and genkwanin (208 microg/l). The majority of the flavone products are excreted in the culture media; however, 25% is contained within the cells. The metabolic engineering strategy presented demonstrates that plant-specific flavones are successfully produced in E. coli for the first time by incorporating a soluble flavone synthase confined only in Apiaceae.
Databáze: OpenAIRE