Purification and some properties of glycerol dehydrogenase from Erwinia aroideae.

Sugiura, Masahiro; Oikawa, Tsutomu; Hirano, Kazuyuki; Shimizu, Hiroshi; Hirata, Fumio

doi:10.1248/cpb.26.716

Cited by 8 publications

(7 citation statements)

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“…Similar pH profiles are reported for glycerol dehydrogenases from E. coli,3) E. aroideae 7 ) and Mucor javanicus.…”

Section: Discussionsupporting

confidence: 80%

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Purification and Characterization of Glycerol Dehydrogenase Isoenzymes fromGeotrichum candidum

Itoh

1982

Agricultural and Biological Chemistry

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“…Similar pH profiles are reported for glycerol dehydrogenases from E. coli,3) E. aroideae 7 ) and Mucor javanicus.…”

Section: Discussionsupporting

confidence: 80%

“…7 ) On the other hand, NADP+ -linked glycerol dehydrogenase . (EC 1.1.1.72) was found in several fungi S I' V11) and animal tissues.…”

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confidence: 99%

Purification and Characterization of Glycerol Dehydrogenase Isoenzymes fromGeotrichum candidum

Itoh

1982

Agricultural and Biological Chemistry

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“…These substrates were chosen because several different nicotinamide-dependent dehydrogenases, such as propanol dehydrogenases, propionaldehyde dehydrogenases, 1,2-propanediol dehydrogenases, 1,3-propanediol oxidoreductases, and glycerol dehydrogenases, are known to be involved in the degradation of these substrates (15,34,38,42,45). In addition, the latter three types of enzymes exhibit a rather broad substrate specificity and are most active with short-chain polyols and the correlating carbonyl compounds (13,14,28,29,42,43,45). After inoculation of the enrichment cultures and growth for 1 day at 30°C, microorganisms and environmental matrix substances were pelleted, used to inoculate fresh medium, and incubated for another day.…”

Section: Resultsmentioning

confidence: 99%

Construction and Screening of Metagenomic Libraries Derived from Enrichment Cultures: Generation of a Gene Bank for Genes Conferring Alcohol Oxidoreductase Activity on Escherichia coli

Knietsch

Waschkowitz²,

Bowien³

et al. 2003

Appl Environ Microbiol

162

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Enrichment of microorganisms with special traits and the construction of metagenomic libraries by direct cloning of environmental DNA have great potential for identifying genes and gene products for biotechnological purposes. We have combined these techniques to isolate novel genes conferring oxidation of short-chain (C 2 to C 4 ) polyols or reduction of the corresponding carbonyls. In order to favor the growth of microorganisms containing the targeted genes, samples collected from four different environments were incubated in the presence of glycerol and 1,2-propanediol. Subsequently, the DNA was extracted from the four samples and used to construct complex plasmid libraries. Approximately 100,000 Escherichia coli strains of each library per test substrate were screened for the production of carbonyls from polyols on indicator agar. Twenty-four positive E. coli clones were obtained during the initial screen. Sixteen of them contained a plasmid (pAK101 to pAK116) which conferred a stable carbonyl-forming phenotype. Eight of the positive clones exhibited NAD(H)-dependent alcohol oxidoreductase activity with polyols or carbonyls as the substrates in crude extracts. Sequencing revealed that the inserts of pAK101 to pAK116 encoded 36 complete and 17 incomplete presumptive proteinencoding genes. Fifty of these genes showed similarity to sequenced genes from a broad collection of different microorganisms. The genes responsible for the carbonyl formation of E. coli were identified for nine of the plasmids (pAK101, pAK102, pAK105, pAK107 to pAK110, pAK115, and pAK116). Analyses of the amino acid sequences deduced from these genes revealed that three (orf12, orf14, and orf22) encoded novel alcohol dehydrogenases of different types, four (orf5, sucB, fdhD, and yabF) encoded novel putative oxidoreductases belonging to groups distinct from alcohol dehydrogenases, one (glpK) encoded a putative glycerol kinase, and one (orf1) encoded a protein which showed no similarity to any other known gene product.

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“…This enzyme was partially purified from Aerobacter aerogenes by Kaplan et al in 1953. 1 ) Afterwards, a number of bacteria including Aerobacter aerogenes,2.3) Escherichia COli,4) Bacillus subtilis,5) Streptococcus/aecalis, 6) and Erwinia aroideae 7 ) have been found to have the potential to produce this enzyme.…”

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confidence: 99%

“…The enzyme production by G. candidum, grown under favorable conditions, reached more than 100 units/dl, and this enzyme level is higher than those of various bacteria, e.g., 22 units/dl by A. aerogenes,3) 0.1 units/dl by E. coli K12 4 ) and 78 units/dl by E. aroideae. 7 ) Thus, G. candidum seems to be an excellent species for large scale production of this enzyme.…”

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confidence: 99%

Glycerol Dehydrogenase Production byGeotrichum candidum

Umeda¹

1982

Agricultural and Biological Chemistry

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Purification and some properties of glycerol dehydrogenase from Erwinia aroideae.

Cited by 8 publications

References 0 publications

Purification and Characterization of Glycerol Dehydrogenase Isoenzymes fromGeotrichum candidum

Purification and Characterization of Glycerol Dehydrogenase Isoenzymes fromGeotrichum candidum

Construction and Screening of Metagenomic Libraries Derived from Enrichment Cultures: Generation of a Gene Bank for Genes Conferring Alcohol Oxidoreductase Activity on Escherichia coli

Glycerol Dehydrogenase Production byGeotrichum candidum

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