Bioconversion of n-octane to octanoic acid by a recombinant Escherichia coli cultured in a two-liquid phase bioreactor.
The alk genes from the catabolic OCT plasmid of Pseudomonas oleovorans, which encode the enzymes involved in the oxidation of n-alkanes to carboxylic acids, were introduced into E. coli W3110. The resulting recombinant converts n-octane in a two-liquid phase medium into the corresponding alkanoate and excretes this compound into the aqueous phase. The rate of octanoic acid production by the recombinant E. coli is equal to or better than the alkane oxidation rate of P. oleovorans, suggesting that two-liquid phase fermentations with E. coli might have future industrial applications.
Favre-Bulle
O
O
Groningen Biotechnology Center, University of Groningen, The Netherlands.
Schouten
T
T
Kingma
J
J
Witholt
B
B
D002210:Caprylates / Q000737:chemistry*; D002478:Cells, Cultured; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics* / Q000648:ultrastructure; D005798:Genes, Bacterial; D009795:Octanes / Q000737:chemistry*; D010957:Plasmids / Q000235:genetics; D011549:Pseudomonas / Q000235:genetics
D002210:Caprylates; D009795:Octanes; C031492:octanoic acid; C026728:octane