48 results
Search Results
2. [6-desoxy-L-idose, 6-desoxy-L-sorbose, and 6-desoxy-L-psicose].
- Author
-
Kaufmann H and Reichstein T
- Subjects
- Chromatography, Paper, Electrophoresis, Fermentation, Acetobacter metabolism, Hexoses analysis
- Published
- 1967
- Full Text
- View/download PDF
3. Isocitrate dehydrogenase and glutamate synthesis in Acetobacter suboxydans.
- Author
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Greenfield S and Claus GW
- Subjects
- Carbon Isotopes, Cell-Free System, Chromatography, Paper, Citrates metabolism, Citrates pharmacology, Hydro-Lyases metabolism, Ketoglutaric Acids metabolism, Oxidoreductases metabolism, Acetobacter drug effects, Acetobacter enzymology, Acetobacter metabolism, Glutamates biosynthesis, Isocitrate Dehydrogenase metabolism
- Abstract
Acetobacter suboxydans is an obligate aerobe for which an operative tricarboxylic acid cycle has not been demonstrated. Glutamate synthesis has been reported to occur by mechanisms other than those utilizing isocitrate dehydrogenase, a tricarboxylic acid cycle enzyme not previously detected in this organism. We have recovered alpha-ketoglutarate and glutamate from a system containing citrate, nicotinamide adenine dinucleotide (NAD), a divalent cation, pyridoxal phosphate, an amino donor, and dialyzed, cell-free extract. Aconitase activity was readily detected in these extracts, but isocitrate dehydrogenase activity, measured by NAD reduction, was masked by a cyanide-resistant, particulate, reduced NAD oxidase. Isocitrate dehydrogenase activity could be demonstrated after centrifuging the extracts at 150,000 x g for 3 hr and treating the supernatant fluid with 2-heptyl-4-hydroxyquinoline N-oxide. It is concluded that A. suboxydans can utilize the conventional tricarboxylic acid cycle enzymes to convert citrate to alpha-ketoglutarate which can then undergo a transamination to glutamate.
- Published
- 1969
- Full Text
- View/download PDF
4. Long-term storage of acetic acid bacteria by means of lyophilization.
- Author
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Sourek J and Kulhánek M
- Subjects
- Acetobacter metabolism, Agar, Chromatography, Paper, Culture Media, Fermentation, Gelatin, Glutamates, Hot Temperature, Methods, Peptones, Sodium, Sorbitol, Sorbose biosynthesis, Starch, Water, Acetobacter growth & development, Bacteriological Techniques, Freeze Drying
- Published
- 1969
5. Enzymatic studies on the oxidation of sugar and sugar alcohol. 8. Particle-bound L-sorbose dehydrogenase from Gluconobacter suboxydans.
- Author
-
Sato K, Yamada Y, Aida K, and Uemura T
- Subjects
- Alcohol Oxidoreductases antagonists & inhibitors, Carbohydrate Metabolism, Chloromercuribenzoates, Chromatography, Paper, Copper pharmacology, Drug Stability, Fructose, Hydrogen-Ion Concentration, Ions, Mercury pharmacology, Oxidation-Reduction, Silver pharmacology, Sorbose, Sucrose, Temperature, Acetobacter analysis, Alcohol Oxidoreductases metabolism
- Published
- 1969
- Full Text
- View/download PDF
6. Phosphoenolpyruvate carboxylation and aspartate synthesis in Acetobacter suboxydans.
- Author
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Claus GW, Orcutt ML, and Belly RT
- Subjects
- Acetobacter enzymology, Aspartate Aminotransferases, Carbon Isotopes, Cell-Free System, Chromatography, Paper, Oxaloacetates biosynthesis, Phenylhydrazines analysis, Spectrophotometry, Acetobacter metabolism, Aspartic Acid biosynthesis, Carbon Dioxide metabolism, Pyruvates metabolism
- Abstract
Dialyzed extracts of Acetobacter suboxydans ATCC 621 catalyze (14)CO(2) assimilation in the presence of phosphoenolpyruvate and a divalent cation. The formation of (14)C-oxalacetate was demonstrated and found not to be dependent upon the presence of orthophosphate or diphosphonucleotides. Oxalacetate synthesis was stimulated by orthophosphate and inhibited by aspartate. All attempts to demonstrate a reversible carboxylation mechanism have failed. (14)C-aspartate was synthesized when phosphoenolpyruvate, H(14)Co(3) (-), pyridoxal phosphate, and glutamate were added to dialyzed extracts. Chromatographic and spectrophotometric analyses and chemical degradation further demonstrate the presence of a reversible aspartate aminotransferase. The function of oxalacetate synthesis in a bacterium that reportedly lacks an operative tricarboxylic acid cycle is discussed.
- Published
- 1969
- Full Text
- View/download PDF
7. The oxidation of D-quinate and related acids by Acetomonas oxydans.
- Author
-
Whiting GC and Coggins RA
- Subjects
- Alcohol Oxidoreductases metabolism, Chromatography, Paper, Manometry, Oxidoreductases metabolism, Quinic Acid metabolism, Spectrophotometry, Acetobacter metabolism, Cinchona metabolism, Cycloparaffins metabolism, Plants, Medicinal, Shikimic Acid metabolism
- Abstract
1. Growing cells of a small number of strains of Acetomonas oxydans oxidized d-quinate to 5-dehydroquinate. 2. d-Shikimate was oxidized to 4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylate (3-dehydroshikimate, formerly 5-dehydroshikimate). 3. d-Dihydroshikimate was oxidized to the corresponding 5-dehydro compound, but epidihydroshikimate oxidation by growing cells was not observed. 4. Cell-free extracts oxidized d-quinate to 5-dehydroquinate with the consumption of the stoicheiometric amount of oxygen, but oxidation of shikimate and dihydroshikimate did not go to completion. 5. Oxidation of quinate was brought about by a constitutive particulate enzyme probably localized in the cytoplasmic membrane. No evidence was found for the participation of NAD, NADP or free flavine compounds in electron transport, but the system was cytochrome-linked.
- Published
- 1967
- Full Text
- View/download PDF
8. Biphasic growth of Acetobacter suboxydans on a glycerol-limiting medium.
- Author
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Batzing BL and Claus GW
- Subjects
- Acetobacter metabolism, Acetone biosynthesis, Chromatography, Paper, Oxidation-Reduction, Time Factors, Acetobacter growth & development, Culture Media, Glycerol metabolism
- Abstract
Dihydroxyacetone was quantitatively produced from glycerol during the primary exponential growth phase and depleted during the secondary exponential phase. Although no growth was detected on the basal medium, growth occurred upon addition of dihydroxyacetone.
- Published
- 1971
- Full Text
- View/download PDF
9. Nonfunctional tricarboxylic acid cycle and the mechanism of glutamate biosynthesis in Acetobacter suboxydans.
- Author
-
Greenfield S and Claus GW
- Subjects
- Acetates metabolism, Acetobacter enzymology, Acetobacter growth & development, Carbon Isotopes, Cell-Free System, Chromatography, Paper, Citrates metabolism, Coenzyme A metabolism, Culture Media, Decarboxylation, Electrophoresis, Hydro-Lyases metabolism, Isocitrate Dehydrogenase metabolism, Ketone Oxidoreductases metabolism, Malate Dehydrogenase metabolism, Oxaloacetates metabolism, Oxo-Acid-Lyases metabolism, Pyruvates metabolism, Spectrophotometry, Succinate Dehydrogenase metabolism, Acetobacter metabolism, Citric Acid Cycle, Glutamates biosynthesis
- Abstract
Acetobacter suboxydans does not contain an active tricarboxylic acid cycle, yet two pathways have been suggested for glutamate synthesis from acetate catalyzed by cell extracts: a partial tricarboxylic acid cycle following an initial condensation of oxalacetate and acetyl coenzyme A. and the citramalate-mesaconate pathway following an initial condensation of pyruvate and acetyl coenzyme A. To determine which pathway functions in growing cells, acetate-1-(14)C was added to a culture growing in minimal medium. After growth had ceased, cells were recovered and fractionated. Radioactive glutamate was isolated from the cellular protein fraction, and the position of the radioactive label was determined. Decarboxylation of the C5 carbon removed 100% of the radioactivity found in the purified glutamate fraction. These experiments establish that growing cells synthesize glutamate via a partial tricarboxylic acid cycle. Aspartate isolated from these hydrolysates was not radioactive, thus providing further evidence for the lack of a complete tricarboxylic acid cycle. When cell extracts were analyzed, activity of all tricarboxylic acid cycle enzymes, except succinate dehydrogenase, was demonstrated.
- Published
- 1972
- Full Text
- View/download PDF
10. Microbial production of D-mannitol and D-fructose from glycerol.
- Author
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Onishi H and Suzuki T
- Subjects
- Candida metabolism, Chromatography, Paper, Culture Media, Fermentation, Methods, Nitrogen metabolism, Time Factors, Acetobacter metabolism, Fructose biosynthesis, Glycerol metabolism, Mannitol biosynthesis, Mitosporic Fungi metabolism
- Published
- 1970
- Full Text
- View/download PDF
11. Biochemical dehydrogenations of saccharides. V. Isolation of 5-ketosorbose formed during sorbose fermentation.
- Author
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Kulhánek M and Sevcíková Z
- Subjects
- Chromatography, Paper, In Vitro Techniques, Acetobacter metabolism, Carbohydrates biosynthesis, Fermentation, Sorbose metabolism
- Published
- 1965
- Full Text
- View/download PDF
12. Biosynthesis of alpha-isopropylmalic and citric acids in Acetobacter suboxydans.
- Author
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Maragoudakis ME and Strassman M
- Subjects
- Carbon Isotopes, Chromatography, Chromatography, Paper, Citrates analysis, Coenzyme A metabolism, Crystallization, Keto Acids metabolism, Malates analysis, Oxygen Consumption, Radiometry, Spectrophotometry, Valerates metabolism, Acetobacter metabolism, Citrates biosynthesis, Malates biosynthesis
- Abstract
Cell-free extracts of Acetobacter suboxydans were prepared which were capable of condensing alpha-ketoisovalerate with (14)C-labeled acetyl-coenzyme A to yield (14)C-labeled alpha-isopropylmalate. The product of the reaction was isolated by paper and column chromatography and was characterized by recrystallization with synthetic alpha-isopropylmalic acid to constant specific radioactivity. The formation of alpha-isopropylmalate by extracts of A. suboxydans plus the ability of the organism to grow in a simple glucose-glycerol medium containing glutamic acid as the only amino acid indicate that the pathway for leucine biosynthesis shown to exist in yeast and Salmonella typhimurium also occurs in A. suboxydans. As a comparison, the condensation of oxalacetate and ((14)C) acetyl-coenzyme A to yield ((14)C) citric acid was shown, by similar means, to occur in A. suboxydans. This is of interest since the existence of this classical condensing enzyme has hitherto not been demonstrated in this organism. This reaction was further demonstrated in cell-free extracts of A. suboxydans by means of a spectrophotometric assay at 232 mmu which measured the cleavage of the carbon-sulfur bond of acetyl-coenzyme A in the presence of oxalacetate. Comparison of the specific activities of crude cell-free extracts indicated a much more extensive occurrence of this reaction in yeast than in A. suboxydans.
- Published
- 1967
- Full Text
- View/download PDF
13. Some remarks on two papers by Shimwell et al. on acetic acid bacteria
- Author
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J. De Ley
- Subjects
Bacteria ,biology ,General Medicine ,Acetates ,biology.organism_classification ,Microbiology ,Mutation ,Mutation (genetic algorithm) ,Acetobacter ,Acetic acid bacteria ,Molecular Biology ,Acetic Acid - Abstract
Several incorrect statements by Carr and Shimwell (1961) and Hodgkiss, Shimwell and Carr (1962) on the classification of acetic acid bacteria are pointed out and briefly discussed.
- Published
- 1963
14. 6-Desoxy-L-idose, 6-Desoxy-L-sorbose und 6-Desoxy-L-psicose. Desoxyzucker, 41. Mittelung [1]
- Author
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H. Kaufmann and T. Reischstein
- Subjects
biology ,Chemistry ,Organic Chemistry ,Paper electrophoresis ,biology.organism_classification ,Biochemistry ,Catalysis ,Amorphous solid ,Inorganic Chemistry ,Paper chromatography ,Drug Discovery ,Melting point ,Organic chemistry ,Fermentation ,Physical and Theoretical Chemistry ,Acetobacter - Abstract
Although crystalline 6-deoxy-L-idose (2) and crystalline 6-deoxy-L-sorbose (3) have similar melting points and specific rotations, they can be conclusively differentiated from one another through paper chromatography and paper electrophoresis. 6-Deoxy-L-idose cannot be converted into 6-deoxy-L-sorbose on short heating in very dilute aequeous mineral acids. The synthesis of amorphous 6-deoxy-L-psicose (17), through oxidative fermentation of 6-deoxy-L-allitol with Acetobacter suboxydans, has been described.
- Published
- 1967
15. Biosynthesis of α-Isopropylmalic and Citric Acids in Acetobacter suboxydans
- Author
-
Michael E. Maragoudakis and Murray Strassman
- Subjects
Recrystallization (geology) ,Microbial Physiology and Metabolism ,Chromatography, Paper ,Malates ,Microbiology ,chemistry.chemical_compound ,Oxygen Consumption ,Biosynthesis ,Valerates ,Acetobacter ,Coenzyme A ,Citrates ,Radiometry ,Molecular Biology ,chemistry.chemical_classification ,Carbon Isotopes ,Chromatography ,biology ,Glutamic acid ,biology.organism_classification ,Keto Acids ,Yeast ,Amino acid ,Paper chromatography ,chemistry ,Biochemistry ,Spectrophotometry ,Crystallization ,Citric acid - Abstract
Cell-free extracts of Acetobacter suboxydans were prepared which were capable of condensing α-ketoisovalerate with 14 C-labeled acetyl-coenzyme A to yield 14 C-labeled α-isopropylmalate. The product of the reaction was isolated by paper and column chromatography and was characterized by recrystallization with synthetic α-isopropylmalic acid to constant specific radioactivity. The formation of α-isopropylmalate by extracts of A. suboxydans plus the ability of the organism to grow in a simple glucose-glycerol medium containing glutamic acid as the only amino acid indicate that the pathway for leucine biosynthesis shown to exist in yeast and Salmonella typhimurium also occurs in A. suboxydans . As a comparison, the condensation of oxalacetate and ( 14 C) acetyl-coenzyme A to yield ( 14 C) citric acid was shown, by similar means, to occur in A. suboxydans . This is of interest since the existence of this classical condensing enzyme has hitherto not been demonstrated in this organism. This reaction was further demonstrated in cell-free extracts of A. suboxydans by means of a spectrophotometric assay at 232 mμ which measured the cleavage of the carbon-sulfur bond of acetyl-coenzyme A in the presence of oxalacetate. Comparison of the specific activities of crude cell-free extracts indicated a much more extensive occurrence of this reaction in yeast than in A. suboxydans .
- Published
- 1967
16. Identification of altro-heptulose and l-threitol as products of meso-erythritol oxidation by Acetobacter suboxydans
- Author
-
V. V. Rendig, E.A. McComb, and C. L. Hu
- Subjects
Biophysics ,Erythritol ,Ribitol ,Biochemistry ,chemistry.chemical_compound ,Sugar Alcohols ,Ribose ,Acetobacter ,Organic chemistry ,Threitol ,Molecular Biology ,Carbon Isotopes ,Chromatography ,biology ,Research ,Erythrulose ,Heptoses ,biology.organism_classification ,carbohydrates (lipids) ,Paper chromatography ,Metabolism ,chemistry ,Alcohols ,Sorbitol ,Tetroses ,Oxidation-Reduction - Abstract
In addition to the main product l -erythrulose, altro -heptulose and l -threitol were found in medium in which meso -erythritol was undergoing oxidation by Acetobacter suboxydans . These compounds were isolated by paper chromatography and identified by their dibenzylidene derivatives. It was established that threitol had the l -configuration by measuring the optical rotation. Another compound present in the medium appeared to be heptulose phosphate by its chromatographic behavior. The formation of altro -heptulose was not detected when sorbitol ( d -glucitol), ribitol (adonitol), d -mannitol, d -ribose, or l -erythrulose were used as substrates. No heptulose formation was observed when meso -erythritol was oxidized by Acetobacter xylinium . C 14 studies revealed that the three compounds detected in the medium were derived from meso -erythritol. Some possible biochemical pathways by which these compounds might be synthesized are discussed. To the authors' knowledge this is the first report of the synthesis in vivo of this heptulose and of l -threitol by Acetobacter suboxydans .
- Published
- 1965
17. Biphasic Growth of Acetobacter suboxydans on a Glycerol-Limiting Medium
- Author
-
B. L. Batzing and G. W. Claus
- Subjects
Glycerol ,Time Factors ,biology ,Chromatography, Paper ,Physiology and Metabolism ,Dihydroxyacetone ,Limiting ,biology.organism_classification ,Microbiology ,Culture Media ,Acetone ,chemistry.chemical_compound ,Paper chromatography ,chemistry ,Exponential growth ,Biochemistry ,Phase (matter) ,Acetobacter ,Oxidation-Reduction ,Molecular Biology - Abstract
Dihydroxyacetone was quantitatively produced from glycerol during the primary exponential growth phase and depleted during the secondary exponential phase. Although no growth was detected on the basal medium, growth occurred upon addition of dihydroxyacetone.
- Published
- 1971
18. Studies on the Formation of Glucosamine Acid byAcetobacter melanogenumBeijerinck andPseudomonas fluorescens liquefaciens
- Author
-
Hisashi Kayamori and Takeshi Takahashi
- Subjects
biology ,Organic Chemistry ,Pseudomonas ,Gluconobacter ,Pseudomonas fluorescens ,Oxidative phosphorylation ,biology.organism_classification ,Applied Microbiology and Biotechnology ,Biochemistry ,Analytical Chemistry ,chemistry.chemical_compound ,Paper chromatography ,chemistry ,Glucosamine ,Acetobacter ,Molecular Biology ,Bacteria ,Biotechnology - Abstract
d-Glucosaminic acid has recently been found to be an oxidized product of d-glucosamine formed by Ps. fluorescens. It has been revealed that many strains of oxidative bacteria can oxidize glucosamine. The formation of glucosamine acid has been recognized among a large number of strains of Pseudomonas, Acetobacter and Gluconobacter, by means of paper chromatography. Furthermore, one of these strains, A. melanogenum Beijerinck, oxidized glucosamine to glucosaminic acid with the theoretical consumption of oxygen as Ps. fluorescens liquefaciens. Glucosaminic acid was proved by isolation and identification by means of using resting cells.The experiment of growth shows that Ps. fluorescens liq. could not secure any energy by means of the oxidation of glucosamine.
- Published
- 1960
19. Studies on the Formation of Glucosaminic Acid by Acetobacter melanogenum Beigerinck and Pseudomonas fluorescens liquefaciens
- Author
-
Hisashi Kayamori and Takeshi Takahashi
- Subjects
biology ,Organic Chemistry ,Pseudomonas ,Gluconobacter ,Pseudomonas fluorescens ,Oxidative phosphorylation ,biology.organism_classification ,Applied Microbiology and Biotechnology ,Biochemistry ,Analytical Chemistry ,Paper chromatography ,chemistry.chemical_compound ,chemistry ,Glucosamine ,Acetobacter ,Molecular Biology ,Bacteria ,Biotechnology - Abstract
D-Glucosaminic acid has recently been found to be an oxidized product of D-glucosamine formed by Ps. fluorescens. It has been revealed that many strains of oxidative bacteria can oxidize glucosamine. The formation of glucosaminic acid has been recognized among a large number of strains of Pseudomonas, Acetobacter and Gluconobacter, by means of paper chromatography. Furthermore, one of these strains, A. melanogenum Beijerinck, oxidized glucosamine to glucosaminic acid with the theoretical consumption of oxygen as Ps. fluorescens liquefaciens. Glucosaminic acid was proved by isolation and identification by means of using resting cells. The experiment of growth shows that Ps. fluorescens liq. could not secure any energy by means of the oxidation of glucosamine.
- Published
- 1960
20. Prediction of the course of continuous fermentation on the basis of analysis of the batch process
- Author
-
Z. Fencl and M. Novák
- Subjects
Basis (linear algebra) ,biology ,business.industry ,Growth ,General Medicine ,Pulp and paper industry ,Microbiology ,Biotechnology ,Glucose Oxidase ,Aspergillus ,Continuous fermentation ,Fermentation ,biology.protein ,Batch processing ,Acetobacter ,Sorbitol ,Glucose oxidase ,Product formation ,Growth rate ,business ,Mathematics - Abstract
A way of predicting the conditions of product formation in a two-state continuous cultivation on the basis of analyzing the batch process is described. The prediction applies to processes where the product formation is proportional to the growth rate and where the relationship between culture activity and the external conditions is linear. Using the example of glucose oxidase production byAspergillus niger the prediction is borne out. The difference between the predicted and found values does not exceed 15%.
- Published
- 1969
21. THE INVESTMENT VALUE OF CONTINUOUS CULTURE
- Author
-
R. C. Telling, D. N. East, and R. Elsworth
- Subjects
biology ,business.industry ,Pulp and paper industry ,Sorbose ,biology.organism_classification ,Applied Microbiology and Biotechnology ,Microbiology ,Biotechnology ,chemistry.chemical_compound ,chemistry ,Scientific method ,Investment value ,Batch processing ,Production (economics) ,Sorbitol ,Acetobacter ,business ,Mathematics - Abstract
SUMMARY: Comparisons are given of the output of sorbose from 3 litre cultures of Acetobacter suboxydans grown in a sorbitol medium in batch and continuous culture. An estimate is given of the investment value of a continuous process of sorbose production relative to the batch process.
- Published
- 1959
22. SORBOSE FROM SORBITON Semiplant-Scale Production by Acetobacter suboxydans
- Author
-
J. J. Stubbs, E. T. Roe, P. A. Wells, and Lewis B. Lockwood
- Subjects
chemistry.chemical_compound ,biology ,Scale (ratio) ,chemistry ,General Engineering ,Acetobacter ,biology.organism_classification ,Pulp and paper industry ,Sorbose - Published
- 1939
23. The oxidation of <scp>d</scp>-quinate and related acids by Acetomonas oxydans
- Author
-
G. C. Whiting and R. A. Coggins
- Subjects
Chromatography, Paper ,Manometry ,Stereochemistry ,General Mathematics ,Quinic Acid ,chemistry.chemical_element ,Shikimic Acid ,Flavin group ,Oxygen ,Acetomonas oxydans ,Acetobacter ,Organic chemistry ,Cinchona ,chemistry.chemical_classification ,Plants, Medicinal ,Applied Mathematics ,Cycloparaffins ,Articles ,Electron transport chain ,Alcohol Oxidoreductases ,Membrane ,Enzyme ,chemistry ,Spectrophotometry ,Cytoplasm ,NAD+ kinase ,Oxidoreductases - Abstract
1. Growing cells of a small number of strains of Acetomonas oxydans oxidized d-quinate to 5-dehydroquinate. 2. d-Shikimate was oxidized to 4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylate (3-dehydroshikimate, formerly 5-dehydroshikimate). 3. d-Dihydroshikimate was oxidized to the corresponding 5-dehydro compound, but epidihydroshikimate oxidation by growing cells was not observed. 4. Cell-free extracts oxidized d-quinate to 5-dehydroquinate with the consumption of the stoicheiometric amount of oxygen, but oxidation of shikimate and dihydroshikimate did not go to completion. 5. Oxidation of quinate was brought about by a constitutive particulate enzyme probably localized in the cytoplasmic membrane. No evidence was found for the participation of NAD, NADP or free flavine compounds in electron transport, but the system was cytochrome-linked.
- Published
- 1967
24. Nonfunctional Tricarboxylic Acid Cycle and the Mechanism of Glutamate Biosynthesis in Acetobacter suboxydans
- Author
-
G. W. Claus and Seymour Greenfield
- Subjects
Electrophoresis ,Oxaloacetates ,Chromatography, Paper ,Decarboxylation ,Physiology and Metabolism ,Coenzyme A ,Citric Acid Cycle ,Acetates ,Biology ,Microbiology ,Malate dehydrogenase ,chemistry.chemical_compound ,Glutamates ,Malate Dehydrogenase ,Acetobacter ,Citrate synthase ,Citrates ,Pyruvates ,Molecular Biology ,Hydro-Lyases ,chemistry.chemical_classification ,Carbon Isotopes ,Cell-Free System ,Succinate dehydrogenase ,Oxo-Acid-Lyases ,Ketone Oxidoreductases ,biology.organism_classification ,Isocitrate Dehydrogenase ,Culture Media ,Succinate Dehydrogenase ,Citric acid cycle ,Enzyme ,Biochemistry ,chemistry ,Spectrophotometry ,biology.protein - Abstract
Acetobacter suboxydans does not contain an active tricarboxylic acid cycle, yet two pathways have been suggested for glutamate synthesis from acetate catalyzed by cell extracts: a partial tricarboxylic acid cycle following an initial condensation of oxalacetate and acetyl coenzyme A. and the citramalate-mesaconate pathway following an initial condensation of pyruvate and acetyl coenzyme A. To determine which pathway functions in growing cells, acetate- 1 - 14 C was added to a culture growing in minimal medium. After growth had ceased, cells were recovered and fractionated. Radioactive glutamate was isolated from the cellular protein fraction, and the position of the radioactive label was determined. Decarboxylation of the C5 carbon removed 100% of the radioactivity found in the purified glutamate fraction. These experiments establish that growing cells synthesize glutamate via a partial tricarboxylic acid cycle. Aspartate isolated from these hydrolysates was not radioactive, thus providing further evidence for the lack of a complete tricarboxylic acid cycle. When cell extracts were analyzed, activity of all tricarboxylic acid cycle enzymes, except succinate dehydrogenase, was demonstrated.
- Published
- 1972
25. Synthesis and Kinase Phosphorylation of 4-Deoxy-<scp>D</scp>-threohexulose
- Author
-
Keith Norman Slessor and Clifford Raymond Haylock
- Subjects
Chemical Phenomena ,Chromatography, Paper ,Stereochemistry ,Phosphofructokinase-1 ,Acid Phosphatase ,Saccharomyces cerevisiae ,Lithium ,Structure-Activity Relationship ,chemistry.chemical_compound ,Hydrolysis ,Acetals ,Adenosine Triphosphate ,Sugar Alcohols ,Ethers, Cyclic ,Hexokinase ,Acetobacter ,Animals ,Hexosephosphates ,Hexoses ,Binding Sites ,biology ,Kinase ,Muscles ,Substrate (chemistry) ,General Medicine ,Ketones ,Plants ,biology.organism_classification ,Yeast ,Chemistry ,Kinetics ,chemistry ,Yield (chemistry) ,Phosphorylation ,Rabbits ,Hexosediphosphates ,Aluminum - Abstract
Synthesis of the only unknown deoxyfructose, 4-deoxy-D-threohexulose, is reported. Its preparation involved reductive lithium aluminum hydride ring opening of 3,4-anhydro-1,2:5,6-di-O-isopropylidene- D-talitol, followed by hydrolysis of the resulting epimeric deoxy diisopropylidene hexitols and selective Acetobacter suboxydans oxidation of 3-deoxy-D-arabinohexitol. Kinetic studies using 4-deoxy-D-threohexulose as substrate for yeast hexokinase support the premise that the C-4 hydroxyl is a binding group in formation of the enzyme–substrate complex. Enzymatic synthesis of 4-deoxy-D-threohexulose 6-phosphate and 4-deoxy-D-threohexulose 1,6-diphosphate has been achieved in low yield from 4-deoxy-D-threohexulose.
- Published
- 1973
26. The serum polyol pattern and the urinary polyol excretion in diabetic and in uremic patients
- Author
-
E. Pitkänen
- Subjects
medicine.medical_specialty ,Chromatography, Gas ,Chromatography, Paper ,Urinary system ,Clinical Biochemistry ,Borohydrides ,Urine ,Biochemistry ,Excretion ,Sodium borohydride ,chemistry.chemical_compound ,Sugar Alcohols ,Urinary excretion ,Polyol ,Diabetes mellitus ,Internal medicine ,Diabetes Mellitus ,medicine ,Acetobacter ,Humans ,Mannitol ,Uremia ,chemistry.chemical_classification ,Chromatography ,Biochemistry (medical) ,General Medicine ,medicine.disease ,Endocrinology ,chemistry ,Biological Assay ,Oxidation-Reduction ,Inositol ,medicine.drug - Abstract
A gas-liquid chromatographic method, based on acetylation of polyols, was applied to a study of polyols in urine and in serum. The profile of the normal urinary polyol excretion was described and the formation of additional polyols was demonstrated by treating samples with sodium borohydride prior to chromatography. In diabetes mellitus the urinary excretion of mannitol and myo-inositol was elevated. In cases of chronic renal failure the retention of polyols in serum was demonstrated and the level of myo-inositol was shown to be increased both in serum and in urine. The design of the experimental conditions eliminated the errors due to the intake of exogenous polyols. The metabolic significance of the findings is still to be determined.
- Published
- 1972
27. [6-desoxy-L-idose, 6-desoxy-L-sorbose, and 6-desoxy-L-psicose]
- Author
-
H, Kaufmann and T, Reichstein
- Subjects
Electrophoresis ,Chromatography, Paper ,Fermentation ,Acetobacter ,Hexoses - Published
- 1967
28. The pathway of myo-inositol degradation in Aerobacter aerogenes. Identification of the intermediate 2-deoxy-5-keto-D-gluconic acid
- Author
-
W A, Anderson and B, Magasanik
- Subjects
Aldehydes ,Chemical Phenomena ,Chromatography, Paper ,Infrared Rays ,Periodic Acid ,Sodium ,Enterobacter ,Hydrazones ,Gluconates ,Keto Acids ,Malonates ,Mass Spectrometry ,Phenylhydrazines ,Chemistry ,Isomerism ,Spectrophotometry ,Methods ,Acetobacter ,Dicarboxylic Acids ,Oxidation-Reduction ,Inositol ,Hexoses - Published
- 1971
29. Biochemical dehydrogenations of saccharides. V. Isolation of 5-ketosorbose formed during sorbose fermentation
- Author
-
M. Kulhánek and Zdena Ševčíková
- Subjects
chemistry.chemical_compound ,Biochemistry ,Chemistry ,Chromatography, Paper ,Aldonic acid ,Fermentation ,Carbohydrates ,Acetobacter ,Sorbose ,General Medicine ,In Vitro Techniques ,Microbiology - Abstract
Путем продления нормальной ферментации сорбозы была приготовлена смесь, содержащая 5-кето-сорбозу, возникающую путем дальнейшей дегидрогенации сорбозы. Из этой смеси с помощью разделения на колонке катекса в форме Ba2+ была выделена кристаллическая 5-кето-сорбоза. Так были подтверждены выводы предыдущего сообщения относительно этого побочного метаболита ферментации сорбозы.
- Published
- 1965
30. Isocitrate dehydrogenase and glutamate synthesis in Acetobacter suboxydans
- Author
-
G. W. Claus and Seymour Greenfield
- Subjects
IDH1 ,Microbial Physiology and Metabolism ,Chromatography, Paper ,Biology ,Nicotinamide adenine dinucleotide ,Microbiology ,Aconitase ,chemistry.chemical_compound ,Glutamates ,Acetobacter ,Citrates ,Pyridoxal phosphate ,Molecular Biology ,Hydro-Lyases ,Carbon Isotopes ,Cell-Free System ,biology.organism_classification ,Isocitrate Dehydrogenase ,Citric acid cycle ,Isocitrate dehydrogenase ,Biochemistry ,chemistry ,Ketoglutaric Acids ,NAD+ kinase ,Oxidoreductases - Abstract
Acetobacter suboxydans is an obligate aerobe for which an operative tricarboxylic acid cycle has not been demonstrated. Glutamate synthesis has been reported to occur by mechanisms other than those utilizing isocitrate dehydrogenase, a tricarboxylic acid cycle enzyme not previously detected in this organism. We have recovered α-ketoglutarate and glutamate from a system containing citrate, nicotinamide adenine dinucleotide (NAD), a divalent cation, pyridoxal phosphate, an amino donor, and dialyzed, cell-free extract. Aconitase activity was readily detected in these extracts, but isocitrate dehydrogenase activity, measured by NAD reduction, was masked by a cyanide-resistant, particulate, reduced NAD oxidase. Isocitrate dehydrogenase activity could be demonstrated after centrifuging the extracts at 150,000 × g for 3 hr and treating the supernatant fluid with 2-heptyl-4-hydroxyquinoline N -oxide. It is concluded that A. suboxydans can utilize the conventional tricarboxylic acid cycle enzymes to convert citrate to α-ketoglutarate which can then undergo a transamination to glutamate.
- Published
- 1969
31. Long-term storage of acetic acid bacteria by means of lyophilization
- Author
-
J, Sourek and M, Kulhánek
- Subjects
Bacteriological Techniques ,Hot Temperature ,Chromatography, Paper ,Sodium ,Water ,Starch ,Culture Media ,Agar ,Freeze Drying ,Glutamates ,Peptones ,Fermentation ,Methods ,Acetobacter ,Gelatin ,Sorbitol ,Sorbose - Published
- 1969
32. Phosphoenolpyruvate carboxylation and aspartate synthesis in Acetobacter suboxydans
- Author
-
M. L. Orcutt, R. T. Belly, and G. W. Claus
- Subjects
Oxaloacetates ,Microbial Physiology and Metabolism ,Chromatography, Paper ,Microbiology ,Divalent ,chemistry.chemical_compound ,Acetobacter ,Aspartate Aminotransferases ,Pyridoxal phosphate ,Pyruvates ,Molecular Biology ,Chemical decomposition ,chemistry.chemical_classification ,Aspartic Acid ,Carbon Isotopes ,biology ,Cell-Free System ,Carbon Dioxide ,biology.organism_classification ,Phenylhydrazines ,Citric acid cycle ,chemistry ,Biochemistry ,Carboxylation ,Spectrophotometry ,Phosphoenolpyruvate carboxykinase ,Bacteria - Abstract
Dialyzed extracts of Acetobacter suboxydans ATCC 621 catalyze 14 CO 2 assimilation in the presence of phosphoenolpyruvate and a divalent cation. The formation of 14 C-oxalacetate was demonstrated and found not to be dependent upon the presence of orthophosphate or diphosphonucleotides. Oxalacetate synthesis was stimulated by orthophosphate and inhibited by aspartate. All attempts to demonstrate a reversible carboxylation mechanism have failed. 14 C-aspartate was synthesized when phosphoenolpyruvate, H 14 Co 3 − , pyridoxal phosphate, and glutamate were added to dialyzed extracts. Chromatographic and spectrophotometric analyses and chemical degradation further demonstrate the presence of a reversible aspartate aminotransferase. The function of oxalacetate synthesis in a bacterium that reportedly lacks an operative tricarboxylic acid cycle is discussed.
- Published
- 1969
33. VALINE-ISOLEUCINE METABOLISM IN ACETOBACTER SUBOXYDANS AND THE INHIBITION OF GROWTH BY VALINE.
- Author
-
KERWAR SS, CHELDELIN VH, and PARKS LW
- Subjects
- Oregon, Acetobacter, Amino Acids, Culture Media, Escherichia coli, Isoleucine, Leucine, Metabolism, Pharmacology, Research, Threonine Dehydratase, Valine
- Abstract
Kerwar, Suresh S. (Oregon State University, Corvallis), Vernon, H. Cheldelin, and L. W. Parks. Valine-isoleucine metabolism in Acetobacter suboxydans and the inhibition of growth by valine. J. Bacteriol. 88:179-186. 1964.-Extracts of Acetobacter suboxydans can synthesize valine and isoleucine via acetolactate and acetohydroxybutyrate, respectively. The amounts of these amino acids synthesized from different intermediates were determined. The pathways appear to be identical to those described for yeast, Neurospora, and Escherichia coli. When exogenous valine was added to a synthetic growth medium inoculated with A. suboxydans, no growth of the culture was observed. The inhibitory effect of valine was reversed by the addition of isoleucine. The site and mechanism of valine inhibition were investigated. Threonine deaminase was inhibited by valine and isoleucine but not by leucine. Repression of the deaminase by isoleucine but not by valine was indicated. The data reported in this paper suggest that valine prevented growth of the organism through false feedback inhibition of threonine deaminase, thereby limiting isoleucine biosynthesis.
- Published
- 1964
- Full Text
- View/download PDF
34. Isolation of 5,6-dimethylbenzimidazolyl cobamine coenzyme as a cofactor for glutamate formation from Acetobacter suboxydans
- Author
-
Koso Kato, Tadashi Kamikubo, and Mitsunori Hayashi
- Subjects
Electrophoresis ,Chromatography ,biology ,Chemistry ,Stereochemistry ,Cyanide ,Coenzymes ,Biophysics ,Glutamic acid ,biology.organism_classification ,Biochemistry ,Cofactor ,Vitamin B 12 ,chemistry.chemical_compound ,Corrinoid ,Glutamates ,Spectrophotometry ,biology.protein ,Acetobacter ,Fermentation ,Corrinoids ,Molecular Biology ,Bacteria - Abstract
In order to know the kinds and forms of vitamin B 12 coenzymes which participate in the formation of glutamic acid through the pathway via citramalate, mesaconate and β-methyla spartate by Acetobacter suboxydans , isolation and identification of the compounds from the bacteria were attempted. From 500 l fermentation of A. suboxydans , 1.7 kg of the freeze-dried cells were obtained. Corrinoids were extracted from the cells with 80% ethanol with or without cyanide, purified with p -chlorophenol-chloroform, fractionated by aluminacolumn chromatography and crystallized in acetone. The paper-ionophoretic, paper-chromatographic, spectrophotometric and microbiological investigations of the cyanocorrinoid showed that the compound obtained might be 5,6-dimethylbenzimidazolyl cobamide. The investigation on the nucleoside, a Ce(III)-decomposition product of the corrinoid proved to be α-ribazole and therefore gave an additional evidence for 5,6-dimethylbenzimidazolyl cobamide. For coenzyme forms, cautions were taken to operate in every process without cyanide and in the dark. Similar physicochemical tests indicated that the coenzyme form of the compound is cobalamin coenzyme.
- Published
- 1968
35. A MICROBIOLOGICAL ASSAY METHOD FOR p-AMINOBENZOIC ACID
- Author
-
Edith R. Isbell, Roy C. Thompson, and Herschel K. Mitchell
- Subjects
Clostridium acetobutylicum ,Sucrose ,Cell Biology ,Biology ,biology.organism_classification ,Biochemistry ,Neurospora crassa ,B vitamins ,chemistry.chemical_compound ,Hydrolysis ,Biotin ,chemistry ,Acetobacter ,Molecular Biology ,Caltech Library Services ,Organism - Abstract
Since the establishment of p-aminobenzoic acid as a member of the B vitamin group, a considerable interest has been shown in methods of determination in natural materials. Since known chemical methods are not sufficiently sensitive, it became evident that microbiological tests should be the most practicable. The organism Clostridium acetobutylicum has been used (1) but no general assay procedure has been presented. Several bacterial strains which respond to p-aminobenzoic acid have been investigated in this laboratory, but satisfactory assay procedures with these organisms have not yet been devised. For the discovery of the test organism used in the procedure described in this paper, we are indebted to Dr. Beadle and Dr. Tatum who kindly furnished us with a culture of their p-aminobenzoic acid requiring a mutant strain of Neurospora crassa, designated by them as Neurospora crassa p-aminobenzoicless No. 1633 (2). This mold will grow optimally on a medium consisting of inorganic salts, ammonium tartrate, sucrose, biotin, and p-aminobenzoic acid. For purposes of assay, however, it has proved advantageous to supplement this basal medium with natural extracts which are either naturally low in p-aminobenzoic acid or have been treated to remove it. With such a complex medium, the possibility of interference by toxic substances or stimulatory substances other than p-aminobenzoic acid which might be present in samples to be assayed is reduced to a minimum. Since the completion of a considerable part of the experimental work described in this paper, microbiological assay methods for p-aminobenzoic acid have been published by Landy and Dicken (3) utilizing the organism Acetobacter suboxydans and by Lewis (4) using Lactobacillus arabinosus 17-5.
- Published
- 1943
36. Rapid screening assays for soluble and particulate bacterial dehydrogenases
- Author
-
K. Kersters
- Subjects
Dehydrogenase ,Microbiology ,Fluorescence ,Cofactor ,Pseudomonas ,Escherichia coli ,Acetobacter ,Molecular Biology ,chemistry.chemical_classification ,Bacteriological Techniques ,biology ,Histocytochemistry ,Bacterial taxonomy ,Screening assay ,General Medicine ,NAD ,biology.organism_classification ,Culture Media ,Indophenol ,Enzyme ,chemistry ,Biochemistry ,Spectrophotometry ,biology.protein ,NAD+ kinase ,Oxidoreductases ,NADP ,Bacteria - Abstract
Two easy and quick assays are described for the semiquantitative determination of soluble and particulate dehydrogenases in bacteria. Soluble NAD- and NADP-linked dehydrogenases are determined by a spot test on paper. The presence of a dehydrogenase is recognized by the fluorescence of the reduced cofactor on the paper. Particle-linked dehydrogenases are detected by the bleaching of 2,6-dichlorophenol-indophenol. The advantages of these assays are that they are reliable, inexpensive to perform and require a minimum of time, labour and enzyme material. This may be useful as a comparative biochemical tool for bacterial taxonomy.
- Published
- 1967
37. TRICARBOXYLIC ACID CYCLE ACTIVITY IN ACETOBACTER PASTEURIANUM
- Author
-
Elwell H. Kawasaki, Tsoo E. King, and Vernon H. Cheldelin
- Subjects
biology ,Citric Acid Cycle ,food and beverages ,Articles ,Oxidative phosphorylation ,Metabolism ,biology.organism_classification ,Microbiology ,Genus Acetobacter ,Citric acid cycle ,Biochemistry ,Acetobacter ,Molecular Biology ,The Krebs Cycle - Abstract
Previous papers from this laboratory (King and Cheldelin, 1952, 1952a, 1954; Hauge et al., 1955, 1955a) have reported on the oxidation of carbohydrates in Acetobacter suboxydans. Neither resting nor disintegrated cells can oxidize acetate or other intermediates of the tricarboxylic acid cycle. These findings have recently been confirmed in another laboratory (Rao and Gunsalus, 1955). From the comparative biochemical viewpoint, it is of interest to study the oxidative behavior of other species of the genus Acetobacter. Results reported in this paper demonstrate that Acetobacter pasteurianum, in contrast to A. suboxydans, can oxidize all the intermediates of the Krebs cycle. Other evidence also indicates the functioning of this cycle in A. pasteurianum.
- Published
- 1956
38. Syntheses of glucose, cellobiose and other saccharides by Acetobacter acetigenum in a lactate-buffered glycerol medium
- Author
-
C. P. Jackson and K. Ramamurti
- Subjects
Glycerol ,Multidisciplinary ,Aqueous solution ,Chromatography ,Cellobiose ,biology ,Ethyl acetate ,Buffers ,biology.organism_classification ,chemistry.chemical_compound ,Acetic acid ,Acetic anhydride ,Glucose ,chemistry ,Activated charcoal ,Biochemistry ,Distilled water ,Lactates ,Acetobacter ,Carbohydrate Metabolism ,Lactic Acid - Abstract
WE have cultivated Acetobacter acetigenum N.C.I.B. 8132, a cellulose-forming micro-organism, in 10 litres of medium in 40 ‘Glaxo’ flasks, which were shaken during incubation at 30° for twenty-one days. The medium contained (gm./l.): potassium dihydrogen phosphate, 2.0; crystalline magnesium sulphate, 1.0; crystalline ferrous sulphate, 0.01; ammonium hydrogen phosphate, 2.5; calcium D-pantothenate, 0.002 ; riboflavin, 0.002; biotin, 0.0001; glycerol, 30; lactic acid, 10.2; the pH value was adjusted with potassium hydroxide to 4.6. The metabolism solution was Seitz-filtered to remove cells and cellulose and concentrated to 500 ml. over barium carbonate, in vacuo at 35°. Activated charcoal, ‘Ultrasorb S.C. 120/240’ (British Carbo Norit Union) as used by Hughes and Whelan1, was sieved through a British Standards 170 mesh and the material retained on the sieve was used to pack two ‘Pyrex’ glass columns (138 × 7.8 cm.) to a depth of 105 cm. In each column 1.9 kgm. of this charcoal rested on a pad of glass-wool overlayed with 100 gm. of ‘Celite’ added as a slurry in water. The columns were washed each with 5 litres of 50 per cent (v/v) aqueous ethanol and then each with 20 litres of distilled water. After removal of insoluble barium salts the metabolism concentrate was rediluted to 10 litres with distilled water and passed through the columns during 14 hr. Each column was eluted with 80 litres of distilled water followed by aqueous ethanol solutions (each of 50 litres) in which the respective ethanol percentages (v/v) were 0.5, 5, 10, 20, 35, and 50. Six aqueous ethanolic fractions, A 1–A 6, were collected and concentrated at 35°. Portions of each were de-ionized with ‘Zeo-Karb 225’ and ‘Deacidite E’ and chromatographed on paper against authentic sugars using (a) n-propanol/water/ethylacetate, 7:2:1 by volume; (b) pyridine/water/ethylacetate, 1:2:2 by volume; (c) ethyl acetate/acetic acid/water, 3:1:3 by volume. The chromatograms gave evidence of the presence of the following sugars: A 2, glucose, fructose, xylose, and ribulose; A 3 similar to A 2 together with a trace of cellobiose; A 4, mainly cellobiose ; A 5, cellotriose and cellotetraose. Fraction A 3 was then de-ionized and submitted to column partition chromatography according to the procedure of Lemieux, Bishop and Pelletier2, which involves the use of ‘Celite No. 535’ to hold the stationary phase. After irrigation with water-saturated n-butanol, the column was extruded and cut into zones as determined by an alkaline permanganate spray. A fraction was separated which, after several further passages through the ‘Celite’ and a final purification by band paper chromatography, yielded 45 mgm. of a substance which had the mobility of glucose when chromatographed in two different solvent systems. An acetate was prepared by heating with anhydrous sodium acetate and acetic anhydride, and after purification this had m.p. 131°, alone or mixed with authentic β-penta-acetyl glucose of m.p. 131°. The infra-red spectra of both acetates were compared and no significant differences could be observed. (Found: C, 49.3; H, 5.8 per cent. Calc. for C16H22O11: C, 49.2; H, 5.7 per cent.)
- Published
- 1960
39. VALINE-ISOLEUCINE METABOLISM IN ACETOBACTER SUBOXYDANS AND THE INHIBITION OF GROWTH BY VALINE
- Author
-
Suresh S. Kerwar, Vernon H. Cheldelin, and L. W. Parks
- Subjects
Microbiology ,Neurospora ,Oregon ,chemistry.chemical_compound ,Threonine Dehydratase ,Leucine ,Valine ,Escherichia coli ,Acetobacter ,Amino Acids ,Isoleucine ,Threonine ,Molecular Biology ,Pharmacology ,chemistry.chemical_classification ,Growth medium ,biology ,Research ,Articles ,biology.organism_classification ,Culture Media ,Amino acid ,Metabolism ,Biochemistry ,chemistry - Abstract
Kerwar, Suresh S. (Oregon State University, Corvallis), Vernon, H. Cheldelin, and L. W. Parks . Valine-isoleucine metabolism in Acetobacter suboxydans and the inhibition of growth by valine. J. Bacteriol. 88: 179–186. 1964.—Extracts of Acetobacter suboxydans can synthesize valine and isoleucine via acetolactate and acetohydroxybutyrate, respectively. The amounts of these amino acids synthesized from different intermediates were determined. The pathways appear to be identical to those described for yeast, Neurospora , and Escherichia coli . When exogenous valine was added to a synthetic growth medium inoculated with A. suboxydans , no growth of the culture was observed. The inhibitory effect of valine was reversed by the addition of isoleucine. The site and mechanism of valine inhibition were investigated. Threonine deaminase was inhibited by valine and isoleucine but not by leucine. Repression of the deaminase by isoleucine but not by valine was indicated. The data reported in this paper suggest that valine prevented growth of the organism through false feedback inhibition of threonine deaminase, thereby limiting isoleucine biosynthesis.
- Published
- 1964
40. A PRESUMABLE PATHWAY OF KOJIC ACID FORMATION FROM FRUCTOSE BY GLUCONOEACTER
- Author
-
Yonosuke Ikeda
- Subjects
biology ,Chemistry ,Ketose ,Dihydroxyacetone ,Dehydrogenase ,Fructose ,biology.organism_classification ,Applied Microbiology and Biotechnology ,Microbiology ,chemistry.chemical_compound ,Biochemistry ,Mannitol dehydrogenase ,Gluconic acid ,Acetobacter ,Kojic acid - Abstract
1. The unknown substance reported in the previous paper was identified as glucosone. The formation of glucosone from fructose by Gluconoacetobacter roseus is a similar reaction with the formation of reductone (enol form of glycerosone) from dihydroxyacetone by the same bacterium. A presumable pathway of ketose oxidation would be shown as follows:2. The fructose dehydrogenase of G. roseus was investigated by Thunberg method. The activity of this dehydrogenase was the same order as that of gluconic acid dehydrogenase and was inhibited by the addition of 1:5.000mol. of 2, 4-dinitrophenol, when other dehydrogenases such as glucose, gluconic acid, and mannitol dehydrogenase were not affected. The fructose dehydrogenase of this bacterium seemed to be of the same type as the dihydroxyacetone dehydrogenase of Acetobacter suboxydans.3. The author isolated a new substance from the fermented broth of fructose. The chemical structure of this compound is now under further investigation. This compound developes purple color with ferric chloride solution and gives different m.p. and Rf value from those of kojic acid, comenic acid, and rubiginol.4. Although the biological induction of kojic acid from glucosone is not yet attained, the author assumes that glucosone would be the most possible intermediate of kojic acid formation, because Bond, Knight and Walker proved in 1937 the existance of the same substance in the brothh fermented by Aspergillus cryzae.
- Published
- 1955
41. Studies on Kojic Acid Fermentation
- Author
-
Yonosuke Ikeda
- Subjects
biology ,Chemistry ,Stereochemistry ,Ketose ,Medicine (miscellaneous) ,Dihydroxyacetone ,Fructose ,Dehydrogenase ,biology.organism_classification ,chemistry.chemical_compound ,Mannitol dehydrogenase ,Chemistry (miscellaneous) ,Gluconic acid ,Acetobacter ,Kojic acid ,Food Science ,Biotechnology - Abstract
1. The unknown substance reported in the previous paper was identified ad glucosone. The formation of glucosone from fructose by Gluoonoacetobacter roseus is a similar reaction with the formation of reductone (enol form of glycerosone) from dihydroxyacetone by the same bacteria. A presumable pathway of ketose oxidation would be shown as follows: CH2OH CO CHOH R_??_CHOH COH CHOH R -2H→CHO CO CHOH R_??_CHO COH COH R This hypothesis extremely agreed with the experimental data of MAGSANIK and CHARGAFF who had reported the formation of α, β-diketo-inositol from inosose by Acetobacter suboxydans. 2. The fructose dehydrogenase of G. roseus was investigated by ZUNEERG method. The activity of this dehydrogenase was the same order as that of gluconic acid dehydrogenase and was inhibited by the addition of 1:5000 mol. of 2, 4-dinitrophenol, when the other dehydroge-nases such as glucose, gluconic acid, mannitol dehydrogenase did not be affected. The fruc-tose dehydrogenase of this bacteria seemed to be the same type as the dihydroxyacetone dehy-drogenase of Acetobacter suboxydans. 3. The author isolated a new substance from the fermented broth of fructose. The chemi-cal structure of this compound is now under the further investigation. This compound deve-loped purple colour with, ferric chloride solution and gives different m. p. and RF value from those of kojic acid, comenic acid and rubiginol. 4. Although the biological induction of kojic acid from glucosone is not yet attained, the author thinks glucosone would be the most possible intermediate of kojic acid formation, be-cause, in 1937, BOND, KNIGHT and WALKER have proved the existance of same substance in the broth fermented by Aspergillus oryzae.
- Published
- 1954
42. Formation of d-Glucose, Cellobiose, and Other Saccharides during Synthesis of Cellulose by Acetobacter acetigenum in a Lactate-buffered Glycerol Medium
- Author
-
Jackson Cp and Ramamurti K
- Subjects
biology ,Chemistry ,Cell Biology ,Cellobiose ,Carbohydrate metabolism ,biology.organism_classification ,Biochemistry ,chemistry.chemical_compound ,D-Glucose ,Glycerol ,Inositol ,Cellulose ,Acetobacter ,Molecular Biology ,Ethylene glycol - Abstract
In extension of the studies on the formation of cellulose by Acetobacter acetigenum (Z-4), the action of this organism on glycerol has now been investigated; this paper records the examination of the products formed in a defined glycerol medium buffered with lactate. Preliminary observations on the action of this organism on ethylene glycol and on inositol are also reported.
- Published
- 1962
43. PURIFICATION AND PROPERTIES OF 2,5-DIKETOGLUCONIC ACID DECARBOXYLASE
- Author
-
A. G. Datta, R. M. Hochster, and H. Katznelson
- Subjects
Desmolases ,chemistry.chemical_classification ,Chromatography ,biology ,Chemistry ,Decarboxylation ,General Medicine ,biology.organism_classification ,Reaction product ,chemistry.chemical_compound ,Enzyme ,Organic chemistry ,Acetobacter ,Derivative (chemistry) - Abstract
2,5-Diketogluconic acid decarboxylase has been purified from extracts of Acetobacter melanogenum. This paper reports the method of purification, the properties of the purified enzyme, and some properties of the reaction product. A crystalline o-nitrophenylhydrazone derivative of the decarboxylation product has been obtained.
- Published
- 1958
44. Formation of gentiobiose, sophorose and other oligosaccharides by Acetobacter species growing in glucose media
- Author
-
T.K. Walker, D. N. Pellegrino, and A. W. Khan
- Subjects
chemistry.chemical_classification ,biology ,Sophorose ,Stereochemistry ,Acetobacter species ,Biophysics ,Oligosaccharides ,Oligosaccharide ,Disaccharides ,biology.organism_classification ,Biochemistry ,Acetobacter rancens ,chemistry.chemical_compound ,Chemically defined medium ,Glucose ,chemistry ,Acetobacter ,Carbohydrate Metabolism ,Gentiobiose ,Glucans ,Molecular Biology ,Acetobacter aceti - Abstract
When Acetobacter aceti, Acetobacter rancens, Acetobacter acidum-mucosum and Acetobacter acetosum var. nairobiense were grown in defined media containing glucose as sole source of carbon, gentiobiose (O-β- d -glucopyranosyl-(1 → 6)- d -glucopyranose) and sophorose (O-β- d -glucopyranosyl-(1 → 2)- d -glucopyranose) were the principal oligosaccharide products in all cases. These were accompanied by other disaccharides and by higher saccharides. Paper chromatograms showed that each Acetobacter species synthesized the same series of sugars.
- Published
- 1959
45. The Suitability of Some Media and Peptones for Sulfonamide Testing
- Author
-
Roar Gudding
- Subjects
Immunodiffusion ,Article ,Photometry ,Folic Acid ,Sulfanilamides ,medicine ,Methods ,Aminobenzoates ,Bacillus megaterium ,Sulfonamides ,Chromatography ,General Veterinary ,biology ,Chemistry ,Sulfonamide (medicine) ,General Medicine ,biology.organism_classification ,Free medium ,Culture Media ,Agar ,Folic acid ,Depression, Chemical ,Peptones ,Chromatography, Gel ,Folic Acid Antagonists ,Biological Assay ,Acetobacter ,Bacteria ,medicine.drug - Abstract
GUDDING, ROAR: The suitability of some media and peptones for sulfonamide testing. Acta vet. scand. 1974, 15, 366–380. — The content of p-aminobenzoic acid and folic acid has been determined in some media and peptones, and the sensitivity of Bacillus megaterium, cultivated on these substrates, towards sulfonamides has been examined. The concentrations of p-aminobenzoic acid and folic acid should be as low as possible in suitable substrates, but other factors are also of importance. The presence of antagonists towards folic acid has been demonstrated in some media, and the consequences of these inhibitors are discussed. Three of the media (Paper Disc Method-Antibiotic Sensitivity Medium, AB Biodisk; Sulphonamide Antagonist Free Medium, Mast Laboratories; and Mueller Hinton, Difco Laboratories) seem to be satisfactory for the determination of the resistance of bacteria towards sulfonamides. The application of Acetobacter medium is suggested for the detection of rest concentrations of sulfonamides in foodstuffs. detection of sulfonamide residues; p-aminobenzoic acid; folic acid.
- Published
- 1974
46. Induction of orientation of bacterial cellulose microfibrils by a novel terpenoid from Acetobacter xylinum
- Author
-
W. Geoffrey Haigh, Klaus Biemann, J. Ross Colvin, Neil H. Tattrie, and Hans J. Förster
- Subjects
Spectrophotometry, Infrared ,Gluconacetobacter xylinus ,Molecular Conformation ,Biochemistry ,Chromatography, DEAE-Cellulose ,chemistry.chemical_compound ,Extracellular ,Cellulose ,Molecular Biology ,Birefringence ,biology ,Terpenes ,Cell Biology ,biology.organism_classification ,Lipids ,Terpenoid ,chemistry ,Bacterial cellulose ,Alcohols ,Microscopy, Electron, Scanning ,Microfibril ,Acetobacter ,Bacteria - Abstract
1. The bacterium Acetobacter xylinum produces extracellular cellulose microfibrils that form a pellicle in the medium enmeshing the bacterial cells. These microfibrils may show some localized alignment, which can be seen as birefringence when the culture is viewed between crossed Polaroid sheets. 2. An increase in birefringence can be induced by the addition of small amounts of certain classes of lipids, particularly sterols, to the cultures. 3. A crude lipid extract from Acetobacter cells induced greatly increased birefringence when added to fresh cultures of this organism. 4. When the bacterial lipids were fractionated, most of the activity was recovered in a complex, polar lipid. The lipid is secreted into the medium during growth and is unstable. The non-saponifiable portion of this lipid is shown to be a 1:1 mixture of a saturated and a monounsaturated C35 tetrahydroxy terpene with a hopane ring system in the accompanying paper by Förster et al. (1973). The saturated molecule is referred to as tetrahydroxybacteriohopane. 5. Tetrahydroxybacteriohopane is itself capable of inducing birefringence in cultures as is 22-hydroxyhopane, which was also isolated from the non-saponifiable fraction of the total lipids. 6. The mechanism of induction of birefringence (orientation of microfibrils) is not known. This is unlikely to be a specific effect, since all the above compounds are active (intact lipid, tetrahydroxybacteriohopane, 22-hydroxyhopane), as are other classes of lipid. It is suggested, however, that a common mechanism may be involved and that similar compounds may be concerned with control of microfibril alignment in the cells of higher plants.
- Published
- 1973
47. A new type of Acetobacter: Acetobacter acidophilum prov. sp
- Author
-
J. M. Wiame, R. G. Dothey, and R. Harpigny
- Subjects
Ethanol ,Strain (chemistry) ,Bacteria Present ,Biology ,biology.organism_classification ,Microbiology ,chemistry.chemical_compound ,Acetic acid ,chemistry ,Biochemistry ,Oxidizing agent ,Pure culture ,Acetobacter ,Bacteria - Abstract
SUMMARY: A new type of Aeetobacter, provisionally named Acetobacter acidophilum, has been isolated in pure culture from an experimental vinegar generator originally inoculated with active industrial beechwood shavings. In contrast to other bacteria, this organism needs an acidic medium for growth and has a very specific oxidizing capacity. It does not grow above pH 4·3 and oxidizes only primary alcohols. Other substrates, including glucose and acetic acid, are not oxidized at a rate higher than 1 % of the oxidation rate for ethanol. The new isolation procedure, which has been applied for the strain described in this paper, allows the isolation of the bacteria present on active shavings, suggesting that this type of bacteria belongs probably to the group of organisms responsible for the acetification in the ‘quick vinegar process’.
- Published
- 1959
48. ACETIC ACID.
- Author
-
MCDONALD, JAMES C.
- Subjects
ACETOBACTER ,NONFICTION - Abstract
The article reviews the book "Acetic Acid Bacteria," by T. Asai.
- Published
- 1969
- Full Text
- View/download PDF
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