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PubMed1997

The phylogeny of acetic acid bacteria based on the partial sequences of 16S ribosomal RNA: the elevation of the subgenus Gluconoacetobacter to the generic level.

Thirty-six strains of acetic acid bacteria classified in the genera Acetobacter, Gluconobacter, and Acidomonas were examined for their partial base sequences in positions 1220 through 1375, 156 bases, of 16S rRNA. The strains of the Q10-equipped Gluconobacter species examined were divided into two subgroups, which included the type strains of Gluconobacter oxydans, the type species of the genus Gluconobacter, and of a second species, Gluconobacter cerinus, respectively. The base differences numbered four between the two type strains. The strains of the Q9-equipped species examined classified in the type subgenus Acetobacter of the genus Acetobacter were not very distant phylogenetically from those of the genus Gluconobacter. The calculated number of base differences was 9-6 between the type strains of G. oxydans and G. cerinus and the type strains of Acetobacter aceti and Acetobacter pasteurianus. In contrast, the strains of the Q10-equipped species examined classified in the subgenus Gluconoacetobacter of the genus Acetobacter were very distant phylogenetically from those of the Acetobacter and Gluconobacter species mentioned above. The number of base differences was calculated to be 14-8. Furthermore, the strains of the methanol-assimilating, Q10-equipped species of the genus Acidomonas examined were located in phylogenetically isolated positions. The type strain of Acidomonas methanolica (identical to Acetobacter methanolicus), the type species of the genus Acidomonas, had 16-9 base differences. The data obtained here indicated that the members of the subgenus Gluconoacetobacter of the genus Acetobacter can be distinguished at the generic level. The new genus Gluconoacetobacter was proposed with the type species, Gluconoacetobacter liquefaciens, in recognition of the genus Acidomonas along with the genera Acetobacter and Gluconobacter in the classification of the acetic acid bacteria.

Acetic Acid↗
PubMed1989

Detoxification of formaldehyde by acetic acid bacteria.

Formaldehyde resistance of methylotrophic and non-methylotrophic Acetobacter strains was investigated. A facultatively methylotrophic Acetobacter methanolicus (MB58) gets rid of free formaldehyde by assimilating it. Heterotrophically growing cells tolerate 12 mM free formaldehyde. Non-methylotrophic but methanol oxidizing Acetobacter pasteurianus strains possess the same level of formaldehyde resistance. Formaldehyde resistance can be drastically lowered down to 4 mM by blocking the formate dehydrogenase by means of hypophosphite. Acetobacter spp. Martin 1 and LMG 76.10 are not able to oxidize methanol or formaldehyde via formate to CO2 and possess a significantly lower formaldehyde resistance (4 mM). Hence high formaldehyde resistance of the Acetobacter spp. investigated is based above all on a properly operating linear dissimilatory sequence. The dissimilatory RuMP cycle can hardly help detoxify formaldehyde.

Acetobacter↗
PubMed1983

Sulfur metabolism in the biosynthesis of monobactams.

We studied the biosynthesis of monobactams with respect to sulfur metabolism in Chromobacterium violaceum, Acetobacter sp., and Agrobacterium radiobacter. All three organisms used inorganic sulfur for monobactam production. When sulfur-containing amino acids were assayed as a source of sulfur for monobactam production, C. violaceum used cystine but not cysteine or methionine, Acetobacter sp. used all three compounds, and A. radiobacter used none. 35S from cysteine, methionine, and sodium sulfate was incorporated into monobactam by Acetobacter sp. Cell-free extracts of all three organisms were shown to possess cysteine desulfhydrase activity. In Acetobacter sp., this activity was constitutive, required pyridoxal phosphate, and had a pH optimum of 9.5. Extensive loss of 3H from L-[3-3H]cysteine was seen upon desulfhydration; no evidence of serine formation was found. Active sulfate was formed in cell-free extracts of A. radiobacter, and, since inorganic sulfur was used by all three organisms, it is likely that the sulfamate group of monobactams is produced via active sulfate.

Acetobacter↗
PubMed1982

Biosynthesis of monobactam compounds: origin of the carbon atoms in the beta-lactam ring.

The biosynthesis of monobactams by strains of Chromobacterium violaceum, Acetobacter sp., and Agrobacterium radiobacter was studied. Monobactams were produced during logarithmic growth by C. violaceum and Acetobacter sp. and during late log growth on glycerol and in stationary phase by A. radiobacter. The addition of various amino acids failed to significantly stimulate monobactam production in any of the producing organisms. Several 14C-amino acids and pyruvate were incorporated in vivo into monobactams. Serine, glycine, and cysteine were better incorporated than alanine or aspartate, whereas an excess of nonradioactive serine depressed the incorporation of labelled cysteine, glycine, and pyruvate. A comparison of [1-14C] glycine and [2-14C] glycine incorporation data suggests that glycine was first converted to serine. With a mixture of [U-14C[serine and [3-3H]serine, C. violaceum synthesized a monobactam with a complete retention of tritium, whereas with a [U-14C] cystine and [3-3H] cystine mixture, there was an extensive loss of C-3 tritium. Acetobacter sp. and A. radiobacter also utilized the double-labeled serine without the loss of tritium in their respective monobactams. It appears, therefore that in the three organisms, the carbon atoms of the beta-lactam ring of the monobactam are derived directly from serine without the loss of the C-3 hydrogen atoms, probably by an SN2 ring closure mechanism. With [methyl-14C] methionine, most of the radioactivity in the monobactam from Acetobacter sp. was in the methyl moiety of the beta-lactam ring methoxyl group.

Aztreonam↗
PubMed1965

ACETOLACTATE METABOLISM AND THE PRESENCE OF A DIHYDROXY ACID DEHYDRATASE IN MICRO-ORGANISMS.

1. The growth characteristics of nine micro-organisms on complex broth and defined media, usually with a single nitrogen source (other than vitamins), were examined as a necessary step before growth of cells for enzyme assays. Six of these bacteria gave a positive colour test with a creatine-potassium hydroxide reagent, indicating the presence of acetoin, which other investigators have shown is formed via the intermediate, alpha-acetolactate. 2. Cell-free extracts of exponential-phase cells of Bacillus subtilis, Staphylococcus aureus, Proteus morganii, Acetobacter rancens (two strains), A. kuetzingianus, A. acetosus, Acetomonas (Acetobacter) melanogenus and Acetomonas (Acetobacter) suboxydans (A.T.C.C. no. 621) were found to contain the enzyme, dihydroxy acid dehydratase (2,3-dihydroxy acid hydro-lyase). 3. The specific activity of the dehydratase from organisms grown on valine- and isoleucine-deficient media was greater than those grown on a complex broth or media containing complete amino acid mixtures. The omission of valine plus isoleucine from a medium containing 19 amino acids caused an increase in the dehydratase specific activity of Staphylococcus aureus and Proteus morganii. 4. The rate of keto acid formation from alphabeta-dihydroxyisovalerate by extracts of six of the above-named organisms was faster than, but somewhat proportional to, the similar rate from alphabeta-dihydroxy-beta-methyl-n-valerate as substrate. 5. These findings may be related to acetolactate synthesis, acetoin formation and valine-isoleucine biosynthesis in the above-mentioned micro-organisms.

Acetobacter↗
PubMed1980

Calcofluor white ST Alters the in vivo assembly of cellulose microfibrils.

The fluorescent brightener, Calcofluor White ST, prevents the in vivo assembly of crystalline cellulose microfibrils and ribbons by Acetobacter xylinum. In the presence of more than 0.01 percent Calcofluor, Acetobacter continues to synthesize high-molecular-weight beta-1,4 glucans. X-ray crystallography shows that the altered product exhibits no detectable crystallinity in the wet state, but upon drying it changes into crystalline cellulose I. Calcofluor alters cellulose crystallization by hydrogen bonding with glucan chains. Synthesis of this altered product is reversible and can be monitored with fluorescence and electron microscopy. Use of Calcofluor has made it possible to separate the processes of polymerization and crystallization leading to the biogenesis of cellulose microfibrils, and has suggested that crystallization occurs by a cell-directed. self-assembly process in Acetobacter xylinum.

Acetobacter↗
PubMed2005

Culture medium optimization for acetic acid production by a persimmon vinegar-derived bacterium.

A new acetic acid-producing microorganism, Acetobacter sp. RKY4, was isolated from Korean traditional persimmon vinegar, and we optimized the culture medium for acetic acid production from ethanol using the newly isolated Acetobacter sp. RKY4. The optimized culture medium for acetic acid production using this microorganism was found to be 40 g/L ethanol, 10 g/L glycerol, 10 g/L corn steep liquor, 0.5 g/L MgSO4.7H2O, and 1.0 g/L (NH4)H2PO4. Acetobacter sp. RKY4 produced 47.1 g/L of acetic acid after 48 h of fermentation in a 250 mL Erlenmeyer flask containing 50 mL of the optimized medium.

Acetic Acid↗