Genetic characteristics of cellulose-forming acetic acid bacteria identified phenotypically as Gluconacetobacter xylinus.

Gluconacetobacter xylinus (=Acetobacter xylinum) shows variety in acid formation from sugars and sugar-alcohols. Toyosaki et al. proposed new subspecies of G.

Cloning of a gene encoding hydroxyquinol 1,2-dioxygenase that catalyzes both intradiol and extradiol ring cleavage of catechol.

Two Escherichia coli transformants with catechol 1,2-dioxygenase activity were selected from a gene library of the benzamide-assimilating bacterium Arthrobacter species strain BA-5-17, which produces four catechol 1,2-dioxygenase isozymes. A DNA fragment isolated from one transformant contained a complete open reading frame (ORF). The deduced amino acid sequence of the ORF shared high identity with hydroxyquinol 1,2-dioxygenase.

Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose.

The crystals of beta-amylase from Bacillus cereus belong to space group P21 with the following cell dimensions: a = 57.70 A, b = 92.87 A, c = 65.

Cloning and sequence analysis of two catechol-degrading gene clusters from the aniline-assimilating bacterium Frateuria species ANA-18.

The aniline-assimilating bacterium Frateuria species ANA-18 produced two catechol 1,2-dioxygenases, CD I and CD II, and two muconate cycloisomerases, MC I and MC II. The catA genes catA1 and catA2 encoding CD I and CD II, respectively, were cloned from a gene library of this bacterium. The catA1 gene was clustered with catB1 encoding MC I, catC1 encoding muconolactone isomerase (MI), catD encoding beta-ketoadipate enol-lactone hydrolase (ELH), and ORFR1 encoding a putative LysR-type regulator.

Reclassification of the Strains with Low G+C Contents of DNA belonging to the Genus Gluconobacter ASAI 1935 (Acetobacteraceae).

Three species, Gluconobacter cerinus, G. asaii, and G. frateurii are reported to show lower G+C contents than G.

Purification and characterization of four catechol 1,2-dioxygenase isozymes from the benzamide-assimilating bacterium Arthrobacter species BA-5-17.

When Arthrobacter sp. BA-5-17 was grown on benzamide, the bacterium synthesized four different catechol 1,2-dioxygenase (CD, EC 1.13.

Purification and characterization of two muconate cycloisomerase isozymes from aniline-assimilating Frateuria species ANA-18.

Two muconate cycloisomerases (MC I and MC II, EC 5.5.1.

Metabolism of 2-aminophenol by Pseudomonas sp. AP-3: modified meta-cleavage pathway.

A novel pathway for 2-aminophenol metabolism by Pseudomonas sp. AP-3 is proposed. The proposed pathway is similar to that known for meta-cleavage of catechol except that one of the hydroxyl groups on the metabolites is replaced by an amino group.

Purification, characterization, and gene analysis of catechol 2,3-dioxygenase from the aniline-assimilating bacterium Pseudomonas species AW-2.

Catechol 2,3-dioxygenase (C23D; EC 1.13.1.

A high level of accumulation of 2-hydroxymuconic 6-semialdehyde from aniline by the transpositional mutant Y-2 of Pseudomonas species AW-2.

Four transpositional mutants of aniline-assimilating Pseudomonas sp. AW-2 produced 2-hydroxymuconic 6-semialdehyde (HMS) from aniline and accumulated it in a cultural medium. Among the four mutants, strain Y-2 produced the greatest amount of HMS (0.

Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme.

2-Aminophenol 1,6-dioxygenase was purified from the cell extracts of Pseudomonas sp. AP-3 grown on 2-aminophenol. The product from 2-aminophenol by catalysis of the purified enzyme was identified as 2-aminomuconic 6-semialdehyde by gas chromatographic and mass spectrometric analyses.

Classification of catechol 1,2-dioxygenase family: sequence analysis of a gene for the catechol 1,2-dioxygenase showing high specificity for methylcatechols from Gram+ aniline-assimilating Rhodococcus erythropolis AN-13.

Gram+ aniline-assimilating Rhodococcus erythropolis AN-13 (AN-13) produces catechol 1,2-dioxygenase (C12O) showing high enzymatic activities for 3- and 4-methylcatechols [Aoki et al. (1984) Agric. Biol.

The role of SH and S-S groups in Bacillus cereus beta-amylase.

The properties of sulfhydryl (SH) and disulfide (S-S) groups in Bacillus cereus BQ10-S1 Spo III beta-amylase have been investigated to clarify their roles in the enzyme action. Two out of three cysteine residues in B. cereus beta-amylase were found to form an S-S bond, which was found to be located between Cys91 and Cys99 by the analysis of an S-S containing peptide.

Identification and characterization of clustered genes for thermostable xylan-degrading enzymes, beta-xylosidase and xylanase, of Bacillus stearothermophilus 21.

Bacillus stearothermophilus 21 is a gram-positive, facultative thermophilic aerobe that can utilize xylan as a sole source of carbon. We isolated this strain from soil, purified its extracellular xylanase and beta-xylosidase, and analyzed the two-step degradation of xylan by these enzymes (T. Nanmori, T.

Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme.

The gene encoding the beta-amylase of Bacillus cereus BQ10-S1 (SpoII) was cloned into Escherichia coli JM 109. A sequenced DNA fragment of 2,001 bp contains the beta-amylase gene. The N-terminal sequences (AVNGKG MNPDYKAYLMAPLKKI), the C-terminal sequences (SHTSSW), and the amino acid sequences of the five regions in the beta-amylase molecules were determined.

Production of Phenolic Compounds by Aspergillus S-4 in Sake Cake Medium and Identification of Terrein.

High performance liquid chromatography (HPLC) analysis of the culture filtrate of an isolated mold, Aspergillus terreus S-4, showed a larger peak of a terrein-like substance than those of gallic acid and protocatechuic acid. The chemical structure of this substance was investigated and identified as terrein, 4,5-dihydroxy-3-propenyl- 2-cyclopenten-1-one. We also examined some culture conditions for the production of terrein using a sake cake medium for strain S-4.

Nitrate Reduction in Bacillus licheniformis in the Presence of Ammonium Salt by Shaking Culture.

A nitrate-reducing bacterium was isolated from a hot spring and identified as Bacillus licheniformis. This strain was found to accumulate NO2(-) in the medium even in the presence of NH4(+) by shaking culture when FeSO4 was added to the medium. The NO2(-) accumulation was due to nitrate reductase activity, and the same accumulation was also recognized in some other bacteria.

Purification and properties of thermostable xylanase and beta-xylosidase produced by a newly isolated Bacillus stearothermophilus strain.

We isolated a thermophilic bacterium that produces both xylanase and beta-xylosidase. Based on taxonomical research, this bacterium was identified as Bacillus stearothermophilus. Each extracellular enzyme was separated by hydrophobic chromatography by using a Toyopearl HW-65 column, followed by gel filtration with a Sephacryl S-200 column.

Features of the beta-amylase isoform system in dry and germinating seeds of alfalfa (Medicago sativa L.).

Five isoforms of beta-amylase were purified to homogeneity from alfalfa seeds (Medicago sativa L.) by chromatofocusing and cation-exchange chromatography. These isoforms were identified as beta-amylase based on their catalytic mode to the substrates.

Capillary isotachophoretic determinations of metal ions by use of complexation equilibria in acetone-water medium.

The determination of metal ions by capillary isotachophoresis and the complexation equilibria between metal ions and polyaminopolycarboxylic acids has been investigated. A seven-component mixture of metal ions can be separated in 45% v/v acetone-water medium when EDTA or DCTA is used as the terminating ion. Linear calibration graphs are obtained for a standard mixture of Mn(+), Cu(2+), Zn(2+), Cd(2+), Pb(2+) and Fe(3+) in the range 0.

Thermostable, Raw-Starch-Digesting Amylase from Bacillus stearothermophilus.

An endospore-forming thermophilic bacterium, which produced amylase and was identified as Bacillus stearothermophilus, was isolated from soil. The amylase had an optimum temperature of 70 degrees C and strongly degraded wheat starch granules (93%) and potato starch granules (80%) at 60 degrees C.

Purification of beta-amylase from alfalfa (Medicago sativa L.) seeds.

An amylase from alfalfa (Medicago sativa L. c.v.

Isolation and Characterization of a Bacillus cereus Mutant Strain Hyperproductive of Exo-beta-Amylase.

Starting with a strain of Bacillus cereus excreting about 40-fold more beta-amylase than does the original wild-type strain, we isolated, after mutagenesis with N-methyl-N'-nitro-N-nitrosoguanidine, a strain designated BQ10-S1 SpoIII which showed under optimal conditions a further 5.5-fold increase in beta-amylase activity. The amylase production of this strain was observed to increase in the presence of 0.