[Potential growth of Achromobacter cobalamini on the wastes from hydrolysis production].
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Alcaligenes↗
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[A hospital epidemic due to Achromobacter calcoaceticus].
35 patients were secondarily infected in our hospital with a strain of A. calcoaceticus resistant to the usual antibiotics and sulfonamides, but sensitive to colimycin. The epidemic lasted 118 days and is not yet finished. Each of the infected patients had a severe surgical or medical illness, underwent operations, trachetomy, etc. and was treated with antibiotics. A. calcoaceticus persisted alone or was associated with other bacteria from 1 to 46 days, in specimens (sputum, etc. or in blood) sometimes until death. It is not pathogenic for rabbits and mice; its pathogenicity in man is discussed in the text. The epidemic strain was not harboured by 15 doctors, students or nurses, nor present on 147 objects in the vicinity of the patients, but was found in a bottle of aqueous 1% eosin solution in the room of an infected child. Experiments show that A. calcoaceticus is not killed by a 1% eosin solution, and freely multiplies in broth containing 0,5% eosin. It is easy to identify the first case and chronology of the epidemic, but it is less easy to identify each time the means of propagation. Usually, infected patients seem to be the source of further infection. Does eosin paly more than an occasional role? Were the germs transported by dust? This not very disturbing epidemic suggests that less pathogenic germs may still cause unsuspected hospital epidemics.
Acinetobacter↗
[Effect of humic acid on formation and several properties of the extracellular polysaccharide of Achromobacter delicatulus].
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Alcaligenes↗
[Bacteremia caused by Achromobacter xylosidans].
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Aged↗
Some newly characterized collagenases from procaryotes and lower eucaryotes.
Chemical and enzymatic properties of four collagenases newly isolated from anaerobic Clostridium histolyticum, aerobic Achromobacter iophagus, and from two lower eucaryotes, the fungus Entomophthora coronata and the insect Hypoderma lineatum are reviewed. The problems of their biosynthesis and precursors, namely the effect of induction of collagenase and neutral proteinase in Achromobacter by their macromolecular substrates are discussed. The two bacterial collagenases are Zn-metallo-enzymes; the highly purified Clostridium collagenase contains cyst(e)ine, serine phosphate and tryptophan additionally to amino acids reported previously. Achromobacter collagenase has the highest specific activity of all collagenases; it yields by autolysis enzymatically active degraded forms. The active dimer is composed of two identical subunits of molecular weight 35,000. Similarities between Achromobacter collagenase, thermolysin and Bacillus subtilis neutral proteinase in molecular weight, amino acid composition, and amino acids important for the active sites are discussed. The two collagenases from low eucaryotes are serine proteinases; Hypoderma collagenase is homologous to the trypsin family in the amino terminal sequence. The initial cleavage of native collagen by highly purified bacterial collagenases occurs in the central helical part of the alpha chains and not progressively from the amino terminal end. One of the two initial cleavages produced by Achromobacter collagenase is situated in the region cleaved specifically by vertebrate collagenases, but with different bond specificity. The same is true for the insect collagenase. Entomophthora collagenase is a proteinase of broad specificity which also cleaves collagen in its helical parts. All four collagenases also degrade other proteins according to their bond specificity.
Alcaligenes↗
Lysobacter strain with high lysyl endopeptidase production.
A new lysyl endopeptidase producing strain, Lysobacter sp. IB-9374, was isolated from soil. This strain secreted the endopeptidase to culture medium at 6-12-fold higher levels relative to Achromobacter lyticus and Lysobacter enzymogenes. The mature Lysobacter sp. enzyme was enzymatically identical to Achromobacter lysyl endopeptidase bearing lysyl bond specificity, a high peptidase activity, a wide pH optimum, and stability against denaturants. Nucleotide sequence analysis of the Lysobacter sp. lysyl endopeptidase gene revealed that the enzyme is synthesized as a precursor protein consisting of signal peptide (20 amino acids (aa)), pro-peptide (185 aa), mature enzyme (268 aa), and C-terminal extension peptide (198 aa). The deduced amino acid sequence of the mature enzyme was totally identical to that of the Achromobacter enzyme. The Lysobacter sp. precursor protein has an 18-aa longer peptide chain following nine consecutive amino acid residues distinct from the Achromobacter counterpart at the C-terminus. Total precursor protein is 671 aa of which only 268 aa are in the finally processed exoenzyme.
Amino Acid Sequence↗
Changes in the microflora of irradiated petrale sole (Eopsetta jordani) fillets stored aerobically at 0.5 C.
The microfloral changes on irradiated petrale sole fillets during aerobic (packaged with oxygen-permeable film), refrigerated storage were determined by the identification of bacterial and yeast isolates to the generic level. The samples were irradiated at 0.0, 0.1, 0.15, 0.2, 0.3, and 0.4 Mrad by use of a cobalt-60 gamma source, were stored at 0.5 C, and were examined periodically for spoilage, total microbial population, and composition. The preirradiation flora of the fresh fillets consisted of coryneforms, Achromobacter, Micrococcus, Flavobacterium, Pseudomonas, and Lactobacillus. Immediately after irradiation, Micrococcus, Achromobacter, coryneforms, and Bacillus were predominant. The flora of the nonirradiated fillets at the time of spoilage consisted of Pseudomonas and Achromobacter. The flora of the irradiated fillets at the time of spoilage consisted of Achromobacter and Trichosporon.
Alcaligenes↗
Effect of gamma irradiation on the microflora of freshwater fish. 3. Spoilage patterns and extension of refrigerated storage life of yellow perch fillets irradiated to 0.1 and 0.2 megarad.
Maximal shelf life was determined and microbial flora were compared for irradiated (0.1 and 0.2 Mrad) and nonirradiated yellow perch fillets stored at 1 C. Shelf life was estimated by organoleptic determinations. Microbiological studies included determination of the effects of irradiation on the total aerobic microbial population, lag phase, and rate of growth. Genera of organisms isolated from fillets through the course of microbial spoilage were identified, and the proteolytic activity of the organisms was determined. Plate counts for fish prior to irradiation showed the presence of approximately 10(6) organisms per g of sample. Irradiation to 0.1 and 0.2 Mrad produced 1.4 and 3 logarithm reductions of the initial count, respectively. Irradiation to 0.1 and 0.2 Mrad approximately doubled the product's shelf life. Organisms initially isolated from the nonirradiated fillets, in order of decreasing number, consisted of Flavobacterium, Micrococcus-Sarcina, Achromobacter-Alcaligenes-Mima, Pseudomonas, Microbacterium, Vibrio, Bacillus, Corynebacterium, Lactobacillus, Brevibacterium, and Aeromonas. By the 6th and 9th days of fillet storage, Pseudomonas and the Achromobacter group were the predominant organisms. All members of the genus Flavobacterium, but not all members of the genus Pseudomonas, were proteolytically active on raw fish juice-agar and skim milk-agar media. The Achromobacter group was found to be nonproteolytic on both media. Residual flora of fillets irradiated to 0.1 and 0.2 Mrad consisted of the Achromobacter group, Lactobacillus, Micrococcus-Sarcina, and Bacillus. Their sequence in predominance, however, varied with dose level. Not all proteolytic bacteria in the fillets were eliminated by 0.1 and 0.2 Mrad; proteolytic Micrococcus-Sarcina survived these treatments.
Bacteria↗
Evaluation of pyrrolidonyl arylamidase for the identification of nonfermenting Gram-negative rods.
To evaluate the activity of pyrrolidonyl arylamidase (PYR) for the differentiation and identification of nonfermenting gram negative rods (NFGNR), 293 isolates were tested. A 24 h culture of each test organism was prepared. From this a 108-109 cfu/mL suspension was added to 0.25 mL of sterile physiologic solution. A PYR disk was then added and the test was incubated for 30 minutes at 35-37 degrees C, at environmental atmosphere. Reading was done by adding 1 drop of cinnamaldehyde reagent. Strains of Acinetobacter baumannii, Acinetobacter haemolyticus, Alcaligenes faecalis, Bergeyella zoohelcum, Bordetella bronchiseptica, Bordetella hinzii, Brevundimonas diminuta, Brevundimonas vesicularis, Brucella ovis, Brucella spp., Brucella suis, Burkholderia cepacia complex, Moraxella catarrhalis, Moraxella lacunata, Moraxella nonliquefaciens, Moraxella osloensis, Oligella ureolytica, Pseudomonas alcaligenes, Pseudomonas mendocina, Pseudomonas pseudoalcaligenes, Pseudomonas putida, Pseudomonas stutzeri, Pseudomonas Vb3, Psychrobacter phenylpyruvicus, and Stenotrophomonas maltophilia were PYR negative. On the other hand Achromobacter piechaudii, Achromobacter denitrificans, Achromobacter xylosoxidans, Burkholderia gladioli, Chryseobacterium gleum-indologenes, Comamonas testosroni, Cupriavidus pauculus, Delftia acidovorans, Elizabethkingia meningoseptica, Myroides spp., Ochrobactrum anthropi, Pseudomonas oryzihabitans, Ralstonia pickettii, Rhizobium radiobacter, Shewanella spp., Sphingobacterium multivorum, Sphingobacterium spiritivorum, and Weeksella virosa were PYR positive. Finally, Acinetobacter lwoffii, Pseudomonas aeruginosa, Pseudomonas fluorescens, Roseomonas spp., and Sphingomonas paucimobilis-parapaucimobilis were PYR variable. PYR testing should be considered as a useful tool to facilitate the identification of NFGNR.
Aminopeptidases↗
Purification, bacteriolytic activity, and specificity of beta-lytic protease from Lysobacter sp. IB-9374.
Lysobacter sp. IB-9374, which was isolated from soil as a high lysyl endopeptidase-producing strain (Chohnanet al., FEMS Microbiol. Lett., 213, 13-20, 2002), was found to produce a beta-lytic protease capable of lysing gram-positive bacteria such as Staphylococcus aureus, Microccocuseus, and Bacillus subtilis. The Lysobacter strain secreted the beta-lytic protease into the culture medium at a 2.4-fold higher level than Achromobacter lyticus. The enzyme was highly purified through a series of six steps with a high yield. The enzyme was strongly inhibited by tetraethylene-pentamine and 1,10-phenanthroline. The purified enzyme lysed more efficiently almost all the gram-positive bacteria tested than lysozyme, lysostaphin, and mutanolysin. The enzyme was very similar to Achromobacter beta-lytic protease containing one zinc atom in terms of amino acid composition and N-terminal sequence. The nucleotide sequence revealed that the mature enzyme was composed of 179 amino acid residues with additional 198 amino acids at the amino-terminal end of the enzyme. The deduced amino acid sequence of the mature enzyme coincided with that of the Achromobacter enzyme, although the prepro-region showed a 41% sequence identity with the counterpart. These results indicate that Lysobacter sp. is a useful strain for an efficient large-scale preparation of beta-lytic protease capable of lysing bacteria.
Journal Article↗
Pigmentiphaga kullae gen. nov., sp. nov., a novel member of the family Alcaligenaceae with the ability to decolorize azo dyes aerobically.
The taxonomic position of Pseudomonas strain K24, which was isolated previously after an aerobic enrichment with the azo compound 1-(4'-carboxyphenylazo)-4-naphthol as the sole source of carbon and energy, was investigated. The detection of a quinone system with ubiquinone Q-8 as the predominant compound and a polyamine pattern with putrescine and 2-hydroxyputrescine as the major polyamines present suggested that strain K24T belongs to the beta-subclass of the Proteobacteria. This was supported by sequencing the 16S rRNA gene, which demonstrated about 95-96% sequence similarity to different species of the genera Achromobacter, Alcaligenes and Bordetella. This suggested that strain K24T is a member of the family Alcaligenaceae. The G+C content of the DNA was 68.5 mol %. Different methods for the construction of phylogenetic dendrograms placed strain K24T separate from the genera Alcaligenes, Achromobacter and Bordetella. Analysis of the fatty acids demonstrated the presence of 10:0 3-OH and high concentrations of summed feature 7 (18:1omega7c, 18:1omega9t and/or 18:1omega12t) and 19:0 cycloomega8c, which is unique among previously described species of the genera Alcaligenes, Achromobacter and Bordetella. On the basis of the low 16S rRNA sequence similarities, the composition of the fatty acid profile and unique phenotypic properties, a new genus and species is proposed for strain K24T with the name Pigmentiphaga kullae gen. nov., sp. nov.
Aerobiosis↗
Metabolism of quaternary carbon compounds: 2,2-dimethylheptane and tertbutylbenzene.
Two Achromobacter strains capable of utilizing 2,2-dimethylheptane or tertbutylbenzene as the sole carbon and energy source were isolated from waste-water. Pivalic acid was found in the cultures of Achromobacter A1 containing 2,2-dimethylheptane. From cultures of Achromobacter A2 in the presence of tertbutylbenzene, a diol was isolated and identified as 2,3-dihydro-2,3-dihydroxytertbutylbenzene. Evidence for meta cleavage of the aromatic ring and for accumulation of pivalic acid in the cultures was also obtained. A metabolic pathway for tertbutylbenzene is suggested.
Alcaligenes↗
Impact of a genetically engineered bacterium with enhanced alkaline phosphatase activity on marine phytoplankton communities.
An indigenous marine Achromobacter sp. was isolated from coastal Georgia seawater and modified in the laboratory by introduction of a plasmid with a phoA hybrid gene that directed constitutive overproduction of alkaline phosphatase. The effects of this "indigenous" genetically engineered microorganism (GEM) on phosphorus cycling were determined in seawater microcosms following the addition of a model dissolved organic phosphorus compound, glycerol 3-phosphate, at a concentration of 1 or 10 (mu)M. Within 48 h, a 2- to 10-fold increase in the concentration of inorganic phosphate occurred in microcosms containing the GEM (added at an initial density equivalent to 8% of the total bacterial population) relative to controls containing only natural microbial populations, natural populations with the unmodified Achromobacter sp., or natural populations with the Achromobacter sp. containing the plasmid but not the phoA gene. Secondary effects of the GEM on the phytoplankton community were observed after several days, evident as sustained increases in phytoplankton biomass (up to 14-fold) over that in controls. Even in the absence of added glycerol 3-phosphate, a numerically stable GEM population (averaging 3 to 5% of culturable bacteria) was established within 2 to 3 weeks of introduction into seawater. Moreover, alkaline phosphatase activity in microcosms with the GEM was substantially higher than that in controls for up to 25 days, and microcosms containing the GEM maintained the potential for net phosphate accumulation above control levels for longer than 1 month.
Journal Article↗
Nucleic acid homologies among oxidase-negative Moraxella species.
The deoxyribonucleic acid (DNA) base composition and DNA homologies of more than 40 strains of oxidase-negative Moraxella species were determined. These bacteria have also been identified as belonging to the Mima-Herellea-Acinetobacter group and the Bacterium anitratum group, as well as to several other genera including Achromobacter and Alcaligenes. The DNA base content of these strains ranged from 40 to 46% guanine plus cytosine. DNA-DNA competition experiments distinguished five groups whose members were determined by showing 50% or more homology to one of the reference strains: B. anitratum type B5W, Achromobacter haemolyticus var. haemolyticus, Alcaligenes haemolysans, Achromobacter metalcaligenes, and Moraxella lwoffi. A sixth group comprised those strains showing less than 50% homology to any of the reference strains. Negligible homology was found between strains of oxidase-negative and oxidase-positive Moraxella species in DNA-DNA competition experiments. However, evidence of a distant relationship between the two groups was obtained in competition experiments by using ribosomal ribonucleic acid.
Bacteria↗
New experiments of biotin enzymes.
The objects of structural studies on biotin-enzymes were acetyl CoA-carboxylase and pyruvate carboxylase of Saccharomyces cerevisiae and beta-methylcrotonyl CoA-carboxylase and acetyl CoA-carboxylase of Achromobacter IV S. It was found that these enzymes can be arranged in three groups. In the first group, as represented by acetyl CoA-carboxylase of Achromobacter, the active enzyme could be resolved in three types of functional components: (1) the biotin-carboxyl carrier protein, (2) the biotin carboxylase, and (3) the carboxyl transferase. In the second group, as represented by beta-methylcrotonyl CoA-carboxylase from Achromobacter only two types of polypeptides are present. The one carries the biotin carboxylase activity together with the biotin-carboxyl-carrier protein, the other one carries the carboxyl transferase activity. In this third group, as represented by the two enzymes of yeast, all three catalytic functions are incorporated in one multifunctional polypeptide chain. The evolution of the different enzymes is discussed. The animal tissues acetyl CoA-carboxylase is under metabolic control, as known from previous studies. It thus has to be expected that the levels of malonyl CoA in livers of rats in all states of depressed fatty acid synthesis are much lower than under normal conditions because the carboxylation of acetyl CoA is strongly reduced and cannot keep pace with the consumption of malonyl CoA by fatty acid synthetase. A new highly sensitive assay method for malonyl CoA was developed which uses tritiated NADPH and measures the incorporation of radioactivity into the fatty acids formed from malonyl CoA in the presence of purified fatty acid synthetase. The application of this method to liver extracts showed that the level of malonyl CoA which amounts to about 7 nmoles per gram of wet liver drops to less than 10% within a starvation period of 24 hr and even further if the starvation period is extended to 48 hr. A low malonyl CoA concentration is also found in the alloxan diabetic animals and in animals being fed a fatty diet after starvation. On the other hand, feeding a carbohydrate rich diet leads to malonyl CoA levels surpassing the levels found after feeding a balanced diet. These observations reconfirm the concept that fatty acid synthesis is principally regulated by the carboxylation of acetyl CoA.
Acetyl-CoA Carboxylase↗
Emerging microorganisms in cystic fibrosis.
Pseudomonas aeruginosa is the most common bacterial isolate obtained from patients with cystic fibrosis of the lungs. Recently, however, new multiresistant organisms have emerged, whose identification may be difficult and whose pathogenic role proves hard to define. Of the 71 strains isolated from 24 patients with cystic fibrosis during acute flareups of pulmonary symptoms, 48 turned out to be Pseudomonas aeruginosa (67.6%); 11 were Pseudomonas non-aeruginosa (15.5%); and 12 were Achromobacter xylosoxidans (16.9%). Each bacterial isolate was tested for sensitivity to nine antibiotics (ceftazidime, azlocillin, piperacillin, aztreonam, cefsulodin, cefoperazone, amikacin, tobramycin, and sisomycin) in terms of minimum inhibitory concentration and minimum bactericidal concentration values. In this series, Achromobacter xylosoxidans proved the species least responsive to treatment, and ceftazidime the most active antibiotic both against Achromobacter and against strains of the genus Pseudomonas. Twenty-three different associations of ceftazidime with aminoglycosides, tested for activity on the multiresistant strains, failed to show synergism of action.
Alcaligenes↗
Enzymatic semisynthesis of [LeuB30] insulin.
Experimental conditions for the preparation of [LeuB30] insulin by coupling of des-AlaB30 insulin with Leu-OBu(t) were determined using Achromobacter protease I and trypsin as catalysts. Successful coupling required a large excess of the amine component (0.8 M), a high concentration of organic cosolvent (35-50%) and neutral pH of the reaction mixture. The coupling yield of Achromobacter protease I after 24 h at 37 degrees C was almost the same or a little higher than that at 25 degrees C. With trypsin, the coupling yield at 37 degrees C after 24 h was considerably lower than at 25 degrees C. This was partly ascribed to the difference in concentration of organic cosolvent at 37 degrees C and 25 degrees C; 35% and 50%, respectively, or possibly of enzyme stability at these temperatures. The maximum product yield was about 90% with both enzymes under optimal conditions. A preparative scale experiment was performed with Achromobacter protease I; the yield of [LeuB30] insulin was 51% using porcine insulin as the starting material. This semisynthetic insulin was identified by HPLC and amino acid analysis. No difference was observed in CD spectra between [LeuB30] insulin and human insulin.
Alcaligenes↗
MICROBIAL DEGRADATION OF ISOPROPYL-N-3 -CHLOROPHENYLCARBAMATE AND 2-CHLOROETHYL-N-3-CHLOROPHENYLCARBAMATE.
Microbial degradation of isopropyl-N-3-chlorophenylcarbamate (CIPC) and 2-chloroethyl-N-3-chlorophenylcarbamate (CEPC) was observed in a soil perfusion system. Degradation in perfused soils, and by pure cultures of effective bacterial isolates, was demonstrated by the production of 3-chloroaniline and the subsequent liberation of free chloride ion. Identified isolates effective in degrading and utilizing CIPC as a sole source of carbon included Pseudomonas striata Chester, a Flavobacterium sp., an Agrobacterium sp., and an Achromobacter sp. Identified isolates, effective in degrading and utilizing CEPC as a sole source of carbon, included an Achromobacter sp. and an Arthrobacter sp. CIPC-effective isolates degraded CEPC more slowly than CIPC, whereas CEPC-effective isolates degraded CIPC more rapidly than CEPC. Both CIPC- and CEPC-effective isolates degraded isopropyl N-phenylcarbamate (IPC) more rapidly than either CIPC or CEPC.
Achromobacter↗