Article Abstract:
Cloning of cellobiose phosphoenolpyruvate-dependent phosphotransferase genes functionally expressed in Escherichia coli, reveal a 50-amino acid conserved region, possibly involved in disaccharide binding. The translated sequence for the genes shows a highly conserved region within the EIIC domain which may be the site for binding and phosphorylation. Phosphotransferase system genes on plasmids of Klebsiella oxytoca encode enzymes with a broad range of substrates and support the most rapid growth of recombinant Escherichia coli on cellobiose-minimal medium.
User Contributions:
Comment about this article or add new information about this topic:
Article Abstract:
A genetically engineered Escherichia coli strain was used to produce 1,2-dihydroxy-4'-chlorobiphenyl (DHCB) from 4-chlorobiphenyl (4-CBP). This mutant strain contains a plasmid coding for biphenyl dioxygenase and dihydrodiol dehydrogenase and lacks the ability to produce 3-phenylcathechol dioxygenase. Conditions affecting the conversion of DHCB from 4-CBP were identified and analyzed. Results show that biologic synthesis of DHCB using mutated E. coli strains can be an alternative to the expensive chemical methods commonly used to synthesize this compound.
User Contributions:
Comment about this article or add new information about this topic:
Article Abstract:
A genetically engineered strain of Escherichia coli efficiently ferments acid hydrolysates of pine cellulose and hemicellulose into ethanol. The strain was genetically mutated to eliminate succinate production and contains Zymomonas mobilis genes for ethanol production. Use of this E. coli strain yields more ethanol than conventional yeast fermentation processes. This high yield is due to more efficient sugar conversion utilizing all component hexoses and pentoses.
User Contributions:
Comment about this article or add new information about this topic: