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consequence of an additional NADH dehydrogenase paralog on the growth of Gluconobacter oxydans DSM3504
by
Luchterhand, B
, Junker, A
, Daniel, R
, Liebl, W
, Kostner, D
, Ehrenreich, A
, Volland, S
, Büchs, J
in
absorbance
/ Acetic acid
/ Acetic acid bacteria
/ Alcohols
/ Applied Microbial and Cell Physiology
/ Bacteria
/ Biocatalysts
/ Biomass
/ Biomedical and Life Sciences
/ Biotechnology
/ Carbohydrates
/ Carbon dioxide
/ Carbon Dioxide - metabolism
/ Cell cycle
/ Dehydrogenase
/ Dehydrogenases
/ DNA sequencing
/ DNA, Bacterial - chemistry
/ DNA, Bacterial - genetics
/ Electron transport
/ Electron transport chain
/ Electrons
/ Enzymes
/ Gene Deletion
/ Gene Dosage
/ Gene sequencing
/ Genes
/ Genetic aspects
/ Genomes
/ Genomics
/ Gluconobacter
/ Gluconobacter oxydans
/ Gluconobacter oxydans - enzymology
/ Gluconobacter oxydans - genetics
/ Gluconobacter oxydans - growth & development
/ Industrial strains
/ L-iditol dehydrogenase
/ Life Sciences
/ Mannitol
/ Mannitol - metabolism
/ Membranes
/ Metabolic Networks and Pathways - genetics
/ Microbial Genetics and Genomics
/ Microbiology
/ Molecular Sequence Data
/ NADH
/ NADH dehydrogenase
/ NADH Dehydrogenase - genetics
/ NADH Dehydrogenase - metabolism
/ Nicotinamide adenine dinucleotide
/ Nucleotide sequence
/ nucleotide sequences
/ Nucleotide sequencing
/ Optical density
/ Oxidation
/ Oxidation-Reduction
/ Oxygen - metabolism
/ Physiological aspects
/ Physiology
/ Plasmids
/ Polyol dehydrogenase
/ Proteobacteria
/ Sequence Analysis, DNA
/ Studies
/ Triose-phosphate isomerase
/ Triose-Phosphate Isomerase - genetics
/ Triose-Phosphate Isomerase - metabolism
2015
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consequence of an additional NADH dehydrogenase paralog on the growth of Gluconobacter oxydans DSM3504
by
Luchterhand, B
, Junker, A
, Daniel, R
, Liebl, W
, Kostner, D
, Ehrenreich, A
, Volland, S
, Büchs, J
in
absorbance
/ Acetic acid
/ Acetic acid bacteria
/ Alcohols
/ Applied Microbial and Cell Physiology
/ Bacteria
/ Biocatalysts
/ Biomass
/ Biomedical and Life Sciences
/ Biotechnology
/ Carbohydrates
/ Carbon dioxide
/ Carbon Dioxide - metabolism
/ Cell cycle
/ Dehydrogenase
/ Dehydrogenases
/ DNA sequencing
/ DNA, Bacterial - chemistry
/ DNA, Bacterial - genetics
/ Electron transport
/ Electron transport chain
/ Electrons
/ Enzymes
/ Gene Deletion
/ Gene Dosage
/ Gene sequencing
/ Genes
/ Genetic aspects
/ Genomes
/ Genomics
/ Gluconobacter
/ Gluconobacter oxydans
/ Gluconobacter oxydans - enzymology
/ Gluconobacter oxydans - genetics
/ Gluconobacter oxydans - growth & development
/ Industrial strains
/ L-iditol dehydrogenase
/ Life Sciences
/ Mannitol
/ Mannitol - metabolism
/ Membranes
/ Metabolic Networks and Pathways - genetics
/ Microbial Genetics and Genomics
/ Microbiology
/ Molecular Sequence Data
/ NADH
/ NADH dehydrogenase
/ NADH Dehydrogenase - genetics
/ NADH Dehydrogenase - metabolism
/ Nicotinamide adenine dinucleotide
/ Nucleotide sequence
/ nucleotide sequences
/ Nucleotide sequencing
/ Optical density
/ Oxidation
/ Oxidation-Reduction
/ Oxygen - metabolism
/ Physiological aspects
/ Physiology
/ Plasmids
/ Polyol dehydrogenase
/ Proteobacteria
/ Sequence Analysis, DNA
/ Studies
/ Triose-phosphate isomerase
/ Triose-Phosphate Isomerase - genetics
/ Triose-Phosphate Isomerase - metabolism
2015
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consequence of an additional NADH dehydrogenase paralog on the growth of Gluconobacter oxydans DSM3504
by
Luchterhand, B
, Junker, A
, Daniel, R
, Liebl, W
, Kostner, D
, Ehrenreich, A
, Volland, S
, Büchs, J
in
absorbance
/ Acetic acid
/ Acetic acid bacteria
/ Alcohols
/ Applied Microbial and Cell Physiology
/ Bacteria
/ Biocatalysts
/ Biomass
/ Biomedical and Life Sciences
/ Biotechnology
/ Carbohydrates
/ Carbon dioxide
/ Carbon Dioxide - metabolism
/ Cell cycle
/ Dehydrogenase
/ Dehydrogenases
/ DNA sequencing
/ DNA, Bacterial - chemistry
/ DNA, Bacterial - genetics
/ Electron transport
/ Electron transport chain
/ Electrons
/ Enzymes
/ Gene Deletion
/ Gene Dosage
/ Gene sequencing
/ Genes
/ Genetic aspects
/ Genomes
/ Genomics
/ Gluconobacter
/ Gluconobacter oxydans
/ Gluconobacter oxydans - enzymology
/ Gluconobacter oxydans - genetics
/ Gluconobacter oxydans - growth & development
/ Industrial strains
/ L-iditol dehydrogenase
/ Life Sciences
/ Mannitol
/ Mannitol - metabolism
/ Membranes
/ Metabolic Networks and Pathways - genetics
/ Microbial Genetics and Genomics
/ Microbiology
/ Molecular Sequence Data
/ NADH
/ NADH dehydrogenase
/ NADH Dehydrogenase - genetics
/ NADH Dehydrogenase - metabolism
/ Nicotinamide adenine dinucleotide
/ Nucleotide sequence
/ nucleotide sequences
/ Nucleotide sequencing
/ Optical density
/ Oxidation
/ Oxidation-Reduction
/ Oxygen - metabolism
/ Physiological aspects
/ Physiology
/ Plasmids
/ Polyol dehydrogenase
/ Proteobacteria
/ Sequence Analysis, DNA
/ Studies
/ Triose-phosphate isomerase
/ Triose-Phosphate Isomerase - genetics
/ Triose-Phosphate Isomerase - metabolism
2015
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consequence of an additional NADH dehydrogenase paralog on the growth of Gluconobacter oxydans DSM3504
Journal Article
consequence of an additional NADH dehydrogenase paralog on the growth of Gluconobacter oxydans DSM3504
2015
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Overview
Acetic acid bacteria such as Gluconobacter oxydans are used in several biotechnological processes due to their ability to perform rapid incomplete regio- and stereo-selective oxidations of a great variety of carbohydrates, alcohols, and related compounds by their membrane-bound dehydrogenases. In order to understand the growth physiology of industrial strains such as G. oxydans ATCC 621H that has high substrate oxidation rates but poor growth yields, we compared its genome sequence to the genome sequence of strain DSM 3504 that reaches an almost three times higher optical density. Although the genome sequences are very similar, DSM 3504 has additional copies of genes that are absent from ATCC 621H. Most importantly, strain DSM 3504 contains an additional type II NADH dehydrogenase (ndh) gene and an additional triosephosphate isomerase (tpi) gene. We deleted these additional paralogs from DSM 3504, overexpressed NADH dehydrogenase in ATCC 621H, and monitored biomass and the concentration of the representative cell components as well as O₂and CO₂transfer rates in growth experiments on mannitol. The data revealed a clear competition of membrane-bound dehydrogenases and NADH dehydrogenase for channeling electrons in the electron transport chain of Gluconobacter and an important role of the additional NADH dehydrogenase for increased growth yields. The less active the NADH dehydrogenase is, the more active is the membrane-bound polyol dehydrogenase. These results were confirmed by introducing additional ndh genes via plasmid pAJ78 in strain ATCC 621H, which leads to a marked increase of the growth rate.
Publisher
Springer-Verlag,Springer Berlin Heidelberg,Springer,Springer Nature B.V
Subject
/ Alcohols
/ Applied Microbial and Cell Physiology
/ Bacteria
/ Biomass
/ Biomedical and Life Sciences
/ Enzymes
/ Genes
/ Genomes
/ Genomics
/ Gluconobacter oxydans - enzymology
/ Gluconobacter oxydans - genetics
/ Gluconobacter oxydans - growth & development
/ Mannitol
/ Metabolic Networks and Pathways - genetics
/ Microbial Genetics and Genomics
/ NADH
/ NADH Dehydrogenase - genetics
/ NADH Dehydrogenase - metabolism
/ Nicotinamide adenine dinucleotide
/ Plasmids
/ Studies
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