for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
development of an efficient bacterial strain of Gluconobacter oxydans_tufB_ga2dh for the production of 2-dehydro-D-gluconate by overexpressing the ga2dh gene in Gluconobacter oxydans. Supply of sufficient oxygen enhances the positive effect of gene overexpression on 2-dehydro-D-gluconate production. Gluconobacter oxydans_tufB_ga2dh is a competitive species for use in 2-dehydro-D-gluconate production. Transgenic strains, evaluation and optimization, detailed overview
development of an efficient bacterial strain of Gluconobacter oxydans_tufB_ga2dh for the production of 2-dehydro-D-gluconate by overexpressing the ga2dh gene in Gluconobacter oxydans. Supply of sufficient oxygen enhances the positive effect of gene overexpression on 2-dehydro-D-gluconate production. Gluconobacter oxydans_tufB_ga2dh is a competitive species for use in 2-dehydro-D-gluconate production. Transgenic strains, evaluation and optimization, detailed overview
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, overexpression of wild-type and expression of start codon mutated enzyme in Escherichia coli strain DH5alpha
gene ga2dh, recombinant overexpression of the enzyme in Gluconobacter oxydans strain DSM2003 under the control of three promoters, PtufB, Pga2dh or Pghp0169, respectively. Recombinant strain Gluconobacter oxydans_tufB_ga2dh shows a similar growth rate to that of the control strain and displays the highest specific productivity of 2-dehydro-D-gluconate from D-gluconate, which is increased nearly twofold compared with that of the control strain during batch biotransformation, method optimization
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
about 2fold upregulation in presence of 7.85 mM H2O2, and upregulation in presence of some lignocellulosic degradation compounds of corn stover hydrolysate