Use of the tac promoter and lacIq for the controlled expression of Zymomonas mobilis fermentative genes in Escherichia coli and Zymomonas mobilis
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Differential Expression of Zymomonas mobilis Sucrase Genes (sacB and sacC) in Escherichia coli and Sucrase Mutants of Zymomonas mobilis
The sacB and sacC genes encoding levansucrase and extracellular sucrase respectively were independently subcloned in pBluescript (high copy number) and in Z. mobilis-E. coli shuttle vector, pZA22 (low copy number). The expression of these genes were compared under identical background of E. coli and Z. mobilis host. The level of sacB gene expression in E. coli was almost ten fold less than the ...
متن کاملGlycolytic enzymes in Zymomonas mobilis.
Raps, Shirley (University of Illinois, Urbana) and R. D. DeMoss. Glycolytic enzymes in Zymomonas mobilis. J. Bacteriol. 84:115-118. 1962-An enzyme extract of Zymomonas mobilis (Pseudomonas lindneri) was capable of fermenting glucose-6-phosphate to CO(2) and ethanol. The extract was found to contain phosphohexoisomerase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase, but no demonstrable...
متن کاملPyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli.
Pyruvate decarboxylase (EC 4.1.1.1) from Zymomonas mobilis purified to homogeneity by using dye-ligand and ion-exchange chromatography. Antibodies produced against the enzyme and the amino-terminal sequence obtained for the pure enzyme were used to select and confirm the identity of a genomic clone encoding the enzyme selected from a genomic library of Z. mobilis DNA cloned into pUC9. The genom...
متن کاملProduction of Acetaldehyde by Zymomonas mobilis.
Mutants of Zymomonas mobilis were selected for decreased alcohol dehydrogenase activity by using consecutively higher concentrations of allyl alcohol. A mutant selected by using 100 mM allyl alcohol produced acetaldehyde at a level of 4.08 g/liter when the organism was grown in aerated batch cultures on a medium containing 4.0% (wt/wt) glucose. On the basis of the amount of glucose utilized, th...
متن کاملPyruvate decarboxylase from Zymomonas mobilis
To study the mechanism of re-activation of Zymomonas mobilis pyruvate decarboxylase apoenzyme by its cofactors thiamin diphosphate and Mg2", cofactor-free enzyme was prepared by dialysis against I mM-dipicolinic acid at pH 8.2. This apoenzyme was then used in a series of experiments that included determination of: (a) the affinity towards one cofactor when the other was present at saturating co...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1992
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.174.22.7370-7378.1992