Expression of Different Levels of Ethanologenic Enzymes from Zymomonas mobilis in Recombinant Strains of Escherichia coli
- 1 February 1988
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 54 (2) , 397-404
- https://doi.org/10.1128/aem.54.2.397-404.1988
Abstract
The expression of Zymomonas mobilis genes encoding pyruvate decarboxylase and alcohol dehydrogenase II in Escherichia coli converted this organism from the production of organic acids to the production of ethanol. Ethanol was produced during both anaerobic and aerobic growth. The extent to which these ethanologenic enzymes were expressed correlated with the extent of ethanol production. The replacement of organic acids with ethanol as a metabolic product during aerobic and anaerobic growth resulted in dramatic increases in final cell density, indicating that these acids (and the associated decline in pH) are more damaging than the production of ethanol. Of the plasmids examined, the best plasmid for growth and ethanol production expressed pyruvate decarboxylase and alcohol dehydrogenase II at levels of 6.5 and 2.5 IU/mg of total cell protein, respectively.This publication has 20 references indexed in Scilit:
- Faculty Opinions recommendation of Mutations of Bacteria from Virus Sensitivity to Virus Resistance.Published by H1 Connect ,2010
- The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterisation and physiological rolesEuropean Journal of Biochemistry, 1986
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- Bioreactors: Design and OperationScience, 1983
- Mutants of Escherichia coli K12 with Defects in Anaerobic Pyruvate MetabolismMicrobiology, 1981
- The respiratory chain NADH dehydrogenase of Escherichia coli. Isolation of an NADH:quinone oxidoreductase from membranes and comparison with the membrane-bound NADH:dichlorophenolindophenol oxidoreductase.Journal of Biological Chemistry, 1981
- Elementary steps in the reaction mechanism of the pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of acetylation and deacetylationBiochemistry, 1980
- Escherichia coli mutants with altered control of alcohol dehydrogenase and nitrate reductaseJournal of Bacteriology, 1980
- Pyruvate Formate‐Lyase of Escherichia coli: the Acetyl‐Enzyme IntermediateEuropean Journal of Biochemistry, 1974
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951