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PubMed1991

Biodegradation by an arthrobacter species of hydrocarbons partitioned into an organic solvent.

An Arthrobacter strain mineralized naphthalene and n-hexadecane dissolved in 2,2,4,4,6,8,8-heptamethylnonane. The extent of mineralization increased with greater volumes of solvent. Measurements under aseptic conditions of the partitioning of naphthalene into the aqueous phase from the solid phase or from heptamethylnonane showed that the rates were rapid and did not limit mineralization. The rate of mineralization of hexadecane was rapid, although partitioning of the compound into aqueous solution was not detected. The Arthrobacter sp. grown in media with or without heptamethylnonane did not excrete products that increased the aqueous solubility of naphthalene and hexadecane. Measurements of the number of cells in the aqueous phase showed that the Arthrobacter sp. attached to the heptamethylnonane-water interface, but attachment was evident even without a substrate in the heptamethylnonane. Tests with small inocula of the Arthrobacter sp. demonstrated that at least a portion of naphthalene or hexadecane dissolved in heptamethylnonane was degraded by cells attached to the solvent-water interface. The cells did not adhere in the presence of 0.1% Triton X-100. The surfactant prevented mineralization of the hexadecane initially dissolved in heptamethylnonane, but it increased the rate and extent of mineralization of naphthalene initially dissolved in heptamethylnonane. The data show that organic solvents into which hydrophobic compounds partition affect the biodegradation of those compounds and that attachment of microorganisms to the organic solvent-water interface may be important in the transformation.

Journal Article↗
PubMed1965

Polymer-Producing Species of Arthrobacter.

Gasdorf, Helen J. (Northern Regional Research Laboratory, Peoria, Ill.), R. G. Benedict, M. C. Cadmus, R. F. Anderson, and R. W. Jackson. Polymer-producing species of Arthrobacter. J. Bacteriol. 90:147-150.1965.-Two slime-producing microorganisms, designated as NRRL B-1973 and NRRL B-1797, were isolated from a Guatemalan soil sample. Their morphological and physiological characteristics permit their assignment to the genus Arthrobacter. Both cultures produce a large amount of extracellular polysaccharide, the maximal amount being 1.4 g per 3 g of glucose. The carbohydrate constituents of B-1973 polysaccharide are galactose, glucose, and mannuronic acid; those of B-1797 are galactose, glucose, and glucuronic acid. The organisms are morphologically and physiologically alike. The differences between these two cultures and previously described species of Arthrobacter appear sufficient to designate a new species. The name Arthrobacter viscosus sp. n. is proposed.

Journal Article↗
PubMed1964

SPECIFICITY OF IMPROVED METHODS FOR MYCOBACTIN BIOASSAY BY ARTHROBACTER TERREGENS.

Antoine, Alan D. (Johns Hopkins University-Leonard Wood Memorial Leprosy Research Laboratory, Baltimore, Md.), Norman E. Morrison, and John H. Hanks. Specificity of improved methods for mycobactin bioassay by Arthrobacter terregens. J. Bacteriol. 88:1672-1677. 1964.-Arthrobacter terregens was used to assay mycobactin, a growth factor for Mycobacterium paratuberculosis. Improved techniques permit the assay of mycobactin within 3 to 4 days by agarplate or liquid-medium methods. For the agarplate method, Arthrobacter terregens gave linear increases in zonal growth at mycobactin concentrations of 0.07 to 0.30 mug per spot; for the liquid-medium method, linear increases in turbidimetric growth occurred at 0.05 to 0.27 mug/ml. Specificity studies show that the mycobactin hydrolytic products, cobactin and mycobactic acid, function as growth stimulators, but the high concentrations required would produce only minimal interference in mycobactin assays. Furthermore, the response to mycobactic acid is characterized by a delayed response of 3 days. Various synthetic hydroxylamine-containing compounds and metalchelating agents cannot replace the biological activity of mycobactin. Diacetylmycobactin is 7.4 times more effective than mycobactin as a growth stimulator.

Animals↗
PubMed1977

Enzymes of the yeast lytic system produced by Arthrobacter GJM-1 bacterium and their role in the lysis of yeast cell walls.

Yeast lytic system produced by Arthrobacter GJM-1 bacterium during growth on baker's yeast cell walls contains a complete set of enzymes which can hydrolyze all structural components of cell walls of Saccharomyces cerevisiae. Chromatographic fractionation of the lytic system showed the presence of two types of endo-beta-1,3-glucanase. Rapid lysis of isolated cell walls of yeast was induced only by endo-beta-1,3-glucanase exhibiting high affinity to insoluble beta-1,3-glucans and releasing laminaripentaose as the main product of hydrolysis of beta-1,3-glucans. This enzyme was able to lyse intact cells of S. cerevisiae only in the presence of an additional factor present in the Arthrobacter GJM-1 lytic system, which was identified as an alkaline protease. This enzyme possesses the lowest molecular weight among other identified enzyme components present in the lytic system. Its role in the solubilization of yeast cell walls from the outer surface by endo-beta-1,3-glucanase could be substituted by preincubation of cells with Pronase or by allowing the glucanase to act on cells in the presence of thiol reagents. The mechanism of lysis of intact cells and isolated cell walls by the enzymes of Arthrobacter GJM-1 is discussed in the light of the present conception of yeast cell wall structure.

Arthrobacter↗
PubMed1993

Morphological, physiological and enzymatic characteristics of cephalosporin acylase-producing Arthrobacter strain 45-8A.

A bacterial strain producing cephalosporin acylases was isolated from soil. The morphological and physiological properties of this strain suggest that it belongs to the genus Arthrobacter, and the isolate was therefore designated Arthrobacter strain 45-8A. Substrate specificity of the enzyme was examined. The enzyme can convert both cephalosporin acid to 7-aminocephalosporanic acid. An interesting feature of the acylases is their temperature-dependent regulation. Activity of acylases was detected in strain 45-8A grown at temperature below 30 degrees C, but was not observed at higher temperature. Arthrobacter strain 45-8A did not exhibit beta-lactamase activity, even though its resistance to cephalosporin C was very strong (> 2000 micrograms/ml). This is quite beneficial for its application in the manufacture of 7-aminocephalosporanic acid.

Arthrobacter↗
PubMed1992

Levels of trehalose and glycogen in Arthrobacter globiformis under conditions of nutrient starvation and osmotic stress.

Cells of Arthrobacter globiformis grown in carbohydrate-rich media were found to contain large quantities of low-Mr carbohydrates (800 micrograms/mg protein) and only small amounts of amino acids, in addition to high amounts of glycogen (2 mg/mg protein). At increasing osmotic values of the medium, low-Mr carbohydrate levels increased to 1300 micrograms/mg protein. Low-Mr pools were extracted from the cells with hot 75% ethanol, and subjected to thin layer, gel and gas-liquid chromatography. They turned out to consist mainly of alpha,alpha-trehalose. Levels of trehalose in Arthrobacter cells have the tendency to remain constant, both during nutrient exhaustion (resulting in glycogen consumption), and on addition of excess of carbon source to the medium (resulting in an increased glycogen content of the cells). The stress-tolerant properties of Arthrobacter (resistance to nutrient starvation, desiccation and high salt concentration) are discussed with respect to the high glycogen and trehalose contents of the cells.

Actinomycetales↗
PubMed1976

Growth and pigment production by Arthrobacter pyridinolis n. sp.

A new bacterium capable of growing on 2-hydroxypyridine as sole source of carbon and nitrogen was isolated from soil. During its growth on solid medium, approximately 50% of this substrate was converted to a brilliant blue crystalline pigment which was deposited extracellularly in the colony mass. The pigment was identical to that produced by Arthrobacter crystallopoietes during its growth on 2-hydroxypyridine. The new isolate exhibited the typical cycle of morphogenesis characteristic of the genus Arthrobacter. The organism is different from all other reported species of Arthrobacter. It is proposed that the organism be named Arthorbacter pyridinolis n. sp.

Arthrobacter↗
PubMed1994

Construction of a new host-vector system in Arthrobacter sp. and cloning of the lipase gene.

Arthrobacter sp. strain MIS38 was transformed with a shuttle vector containing the kanamycin resistant gene kan (derived from Tn5) by an electroporation method. This shuttle vector is from Brevibacterium lactofermentum and Escherichia coli, pULRS8. The following optimal condition of electroporation was determined. A square wave pulse of 1 kV/cm electric field strength for 0.5 ms duration yielded 3 x 10(5) transformants/micrograms plasmid DNA. The number of transformants increased with the amount of DNA over the range 0.01-5 micrograms. This host-vector system was then used successfully to clone and express a lipase gene from Arthrobacter sp. strain MIS38 into both Arthrobacter sp. MIS38 and E. coli JM109.

Amino Acid Sequence↗
PubMed2005

Arthrobacter ardleyensis sp. nov., isolated from Antarctic lake sediment and deep-sea sediment.

Three psychrotrophic Arthrobacter strains, isolated from Antarctic lake sediment (An24, An25T) and deep-sea sediment (ZX6) were studied. Their 16S rRNA gene sequences showed highest similarities (97.0-97.9%) with those of A. nicotianae and A. protophormiae. All three strains underwent rod-coccus morphological change, had high mol% G+C content, were aerobic to slightly anaerobic, and grew between 0 degrees C and 30 degrees C, with optimal growth temperature around 25 degrees C. The cell wall peptidoglycan was A4alpha variant. DNA-DNA hybridization, physiological and chemotaxonomic studies indicated that these three strains constituted a new homogeneous genomic species within the genus Arthrobacter, for which the name Arthrobacter ardleyensis, with the type strain An25T (CGMCC 1.3685, JCM 12921) was proposed.

Aerobiosis↗
PubMed2005

Microbial synthesis of chiral amines by (R)-specific transamination with Arthrobacter sp. KNK168.

Arthrobacter sp. KNK168 shows (R)-enantioselective transaminase [(R)-transaminase] activity, which converts prochiral ketones into the corresponding chiral (R)-amines in the presence of an amino donor. The cultural conditions and reaction conditions for asymmetric synthesis of chiral amines with this microorganism were examined. The transaminase was inducible, and its production was enhanced by the addition of sec-butylamine and 3-amino-2,2-dimethylbutane to the culture medium. (R)-1-Phenylethylamine was a good amino donor for amination of 3,4-dimethoxyphenylacetone with Arthrobacter sp. KNK168. Under the optimum conditions, 126 mM (R)-3,4-dimethoxyamphetamine (DMA) [>99% enantiomeric excess (ee)] was synthesized from 154 mM 3,4-dimethoxyphenylacetone and 154 mM (R)-1-phenylethylamine through the whole cell reaction with an 82% conversion yield. (R)-Enantiomers of other amines, such as (R)-4-methoxyamphetamine, (R)-1-(3-hydroxyphenyl)ethylamine and (R)-1-(3-hydroxyphenyl)ethylamine, were also synthesized from the corresponding carbonyl compounds through asymmetric amination with Arthrobacter sp. KNK168.

Acetone↗
PubMed2005

Biodegradation of naphthalene-2-sulfonic acid present in tannery wastewater by bacterial isolates Arthrobacter sp. 2AC and Comamonas sp. 4BC.

Two bacterial strains, 2AC and 4BC, both capable of utilizing naphthalene-2-sulfonic acid (2-NSA) as a sole source of carbon, were isolated from activated sludges previously exposed to tannery wastewater. Enrichments were carried out in mineral salt medium (MSM) with 2-NSA as the sole carbon source. 16S rDNA sequencing analysis indicated that 2AC is an Arthrobacter sp. and 4BC is a Comamonas sp. Within 33 h, both isolates degraded 100% of 2-NSA in MSM and also 2-NSA in non-sterile tannery wastewater. The yield coefficient was 0.33 g biomass dry weight per gram of 2-NSA. A conceptual model, which describes the aerobic transformation of organic matter, was used for interpreting the biodegradation kinetics of 2-NSA. The half-lives for 2-NSA, at initial concentrations of 100 and 500 mg/l in MSM, ranged from 20 h (2AC) to 26 h (4BC) with lag-phases of 8 h (2AC) and 12 h (4BC). The carbon balance indicates that 75-90% of the initial TOC (total organic carbon) was mineralized, 5-20% remained as DOC (dissolved organic carbon) and 3-10% was biomass carbon. The principal metabolite of 2-NSA biodegradation (in both MSM and tannery wastewater) produced by Comamonas sp. 4BC had a MW of 174 and accounted for the residual DOC (7.0-19.0% of the initial TOC and 66% of the remaining TOC). Three to ten percent of the initial TOC (33% of the remaining TOC) was associated with biomass. The metabolite was not detected when Arthrobacter sp. 2AC was used, and a lower residual DOC and biomass carbon were recorded. This suggests that the two strains may use different catabolic pathways for 2-NSA degradation. The rapid biodegradation of 2-NSA (100 mg/l) added to non-sterile tannery wastewater (total 2-NSA, 105 mg/l) when inoculated with either Arthrobacter 2AC or Comamonas 4BC showed that both strains were able to compete with the indigenous microorganisms and degrade 2-NSA even in the presence of alternate carbon sources (DOC in tannery wastewater = 91 mg/l). The results provide information useful for the rational design of bioreactors for tannery wastewater treatment.

Arthrobacter↗
PubMed2006

Phenol degradation by immobilized cells of Arthrobacter citreus.

An aerobic microorganism with an ability to utilize phenol as carbon and energy source was isolated from a hydrocarbon contamination site by employing selective enrichment culture technique. The isolate was identified as Arthrobacter citreus based on morphological, physiological and biochemical tests. This mesophilic organism showed optimal growth at 25 degrees C and at pH of 7.0. The phenol utilization studies with Arthrobacter citreus showed that the complete assimilation occurred in 24 hours. The organism metabolized phenol up to 22 mM concentrations whereas higher levels were inhibitory. Thin layer chromatography, UV spectral and enzyme analysis were suggestive of catechol, as a key intermediate of phenol metabolism. The enzyme activities of phenol hydroxylase and catechol 2,3-dioxygenase in cell free extracts of Arthrobacter citreus were indicative of operation of a meta-cleavage pathway for phenol degradation. The organism had additional ability to degrade catechol, cresols and naphthol. The degradation rates of phenol by alginate and agar immobilized cells in batch fermentations showed continuous phenol metabolism for a period of eight days.

Agar↗
PubMed1993

Characterization of the methylenediphosphonate transport system in Arthrobacter sp. GLP-1 using the novel tritium-labelled derivative.

The novel tritium-labelled derivative of methylenediphosphonate (MDP) was used in uptake studies of Arthrobacter sp. GLP-1 capable of utilizing a wide range of organophosphonates as its sole source of phosphorus. The MDP uptake was greatly stimulated upon phosphate deprivation. The uptake obeys Michaelis-Menten kinetics with respective Km and Vmax values of 33 microM and 0.3 nmol.min-1.mg-1 fr.wt. Glyphosate and pyrophosphate were competitive inhibitors of MDP uptake. The effect of orthophosphate was more complex than a mere inhibition of MDP uptake since activation occurred at low concentrations. The uptake of MDP by Arthrobacter sp. strain GLP-1 appears to be mediated by a transport system different from the glyphosate uptake system operating in the same cells. The driving force for MDP uptake by Arthrobacter sp. GLP-1 may be a proton gradient across the cell membrane.

Arthrobacter↗
PubMed1998

Whipple's syndrome (uveitis, B27-negative spondylarthropathy, meningitis, and lymphadenopathy) associated with Arthrobacter sp. infection.

OBJECTIVE: To report an unusual case of Whipple's disease, including uveitis, seronegative spondylarthropathy, meningitis, and lymphadenopathy, associated with an Arthrobacter sp. infection. DESIGN: Interventional case report. PATIENT AND INTERVENTION: A 60-year-old white man presenting with severe chronic uveitis and systemic inflammatory manifestations was treated efficiently for Whipple's disease after histopathologic analysis of vitreous and inguinal adenopathy biopsy specimens. The authors performed a retrospective, laboratory-based evaluation of stored tissue specimens. MEASUREMENTS: Molecular analysis based on 16S ribosomal RNA gene amplification was applied to pretreatment biopsy specimens of inguinal lymph node to identify a causative bacterial agent. RESULTS: Tropheryma whippelii genome was not detected in these specimens. However, an amplification product was obtained after the first polymerase chain reaction run and subsequently was sequenced. It corresponded to an Arthrobacter sp., a gram-positive agent presenting diagnostic patterns and therapeutic management similar to those of Whipple's disease caused by T. whippelii. CONCLUSION: The absence of T. whippelii identification by molecular amplification during a clinically and histologically oriented Whipple's syndrome should not rule out the diagnosis. Arthrobacter infection may represent a new bacterial etiology of systemic inflammatory disorders involving the eye and associated with periodic acid-Schiff-positive inclusions.

Arthrobacter↗
PubMed1994

Purification and characterization of 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain 4-CB1.

4-Chlorobenzoyl coenzyme A dehalogenase was purified to homogeneity from Arthrobacter sp. strain 4-CB1 (previously known as Acinetobacter sp. strain 4-CB1), a bacterium isolated from PCB-contaminated soil. Purification was accomplished by four chromatographic steps, including a novel affinity chromatography step. 4-Chlorobenzoyl CoA dehalogenase is a homotetramer of 33-kDa subunits with an isoelectric point of 6.1. The enzyme is stable between pH 6.5 and 10. The optimum pH for kcat is pH 8. The enzyme is able to dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position, although the rate of dehalogenation of 4-fluorobenzoyl CoA is quite slow. The enzyme is specific for dehalogenation at the 4-position, as 3-chloro- and 2-chlorobenzoyl CoA are not dehalogenated. The N-terminal sequence of the Arthrobacter sp. strain 4-CB1 dehalogenase is almost identical to that of the 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain SU and shows 30% identity to that from Pseudomonas sp. strain CBS-3.

Amino Acid Sequence↗
PubMed1969

Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase".

1. A species of Arthrobacter (designated Arthrobacter 9759) was isolated from soil by its ability to grow aerobically on l-threonine as sole source of carbon atoms, nitrogen atoms and energy; the organism also grew well on other sources of carbon atoms including glycine, but no growth was obtainable on aminoacetone or dl-1-aminopropan-2-ol. 2. During growth on threonine, (14)C from l-[U-(14)C]threonine was rapidly incorporated into glycine and citrate, and thereafter into serine, alanine, aspartate and glutamate. 3. With extracts of threonine-grown cells supplied with l-[U-(14)C]threonine, evidence was obtained of the NAD and CoA-dependent catabolism of l-threonine to produce acetyl-CoA plus glycine. Short-term incorporation studies in which [2-(14)C]acetate and [2-(14)C]glycine were supplied (a) to cultures growing on threonine, and (b) to extracts of threonine-grown cells, showed that the acetyl-CoA was metabolized via the tricarboxylic acid cycle and glyoxylate cycle whereas the glycine was converted into pyruvate via the folate-dependent ;serine pathway'. 4. The threonine-grown organism contained ;biosynthetic' threonine dehydratase and a potent NAD-linked l-threonine dehydrogenase but possessed no l-threonine aldolase activity. 5. Evidence was obtained that the acetyl-CoA and glycine produced from l-threonine had their immediate origin in the alpha-amino-beta-oxobutyrate formed by the threonine dehydrogenase; the CoA-dependent cleavage of this compound was catalysed by an alpha-amino-beta-oxobutyrate CoA-ligase, which was identified with ;aminoacetone synthase'. A continuous spectrophotometric assay of this enzyme was developed, and it was found to be inducibly synthesized only during growth on threonine and not during growth on acetate plus glycine. 6. By using a reconstituted mixture of separately purified l-threonine dehydrogenase and alpha-amino-beta-oxobutyrate CoA-ligase (i.e. ;aminoacetone synthase'), l-[U-(14)C]threonine was broken down to [(14)C]glycine plus [(14)C]acetyl-CoA (trapped as [(14)C]citrate). 7. There was no evidence of aminoacetone metabolism by Arthrobacter 9759 even though a small amount of this amino ketone appeared in the culture medium during growth on threonine.

Acetates↗
PubMed2003

Identification and differentiation of species and strains of Arthrobacter and Microbacterium barkeri isolated from smear cheeses with Amplified Ribosmal DNA Restriction Analysis (ARDRA) and pulsed field gel electrophoresis (PFGE).

ARDRA (Amplified Ribosomal-DNA Restriction Analysis) was used to differentiate among species and genera of Arthrobacter and Microbacteria. Species-specific restriction patterns of PCR-products were obtained with NciI for Arthrobacter citreus (DSM 20133T), A. sulfureus (DSM 20167T), A. globiformis (DSM 20124T) and A. nicotianae strains (DSM 20123T, MGE 10D, CA13, CA14, isolate 95293, 95294, and 95299), A. rhombi CCUG 38813T, and CCUG 38812, and Microbacterium barkeri strains (DSM 30123T, MGE 10D, CA12 and CA15, isolate 95292, and isolate 95207). All yellow pigmented coryneforme bacteria isolated from the smear of surface ripened cheeses were identified as either A. nicotianae or M. barkeri strains. Using pulsed field gel electrophoresis (PFGE) strain specific restriction pattern for all Arthrobacter species and Microbacteria tested were obtained with restriction enzymes AscI and SpeI.

Actinomycetales↗
PubMed1991

Description of the erythromycin-producing bacterium Arthrobacter sp. strain NRRL B-3381 as Aeromicrobium erythreum gen. nov., sp. nov.

Arthrobacter sp. strain NRRL B-3381T (T = type strain) is a nonmycelial, nonsporulating actinomycete that produces the macrolide antibiotic erythromycin. This bacterium differs in many ways from the type species of the genus Arthrobacter (Arthrobacter globiformis), suggesting that a taxonomic revision is appropriate. The G + C content of strain NRRL B-3381T DNA is 71 to 73 mol%, and the peptidoglycan of this organism contains LL-diaminopimelic acid. Evolutionary distance data obtained from 16S rRNA sequences identified NRRL B-3381T as the deepest branching member of the Nocardioides group of actinomycetes. The principal long-chain fatty acids which we identified that distinguished strain NRRL B-3381T from related G + C-rich bacteria were 10-methyloctadecanoic (tuberculosteric), octadecenoic, and hexadecanoic acids. These characteristics, together with phage typing and biochemical characteristics, form the basis for our recommendation that strain NRRL B-3381 should be the type strain of a new taxon, for which we propose the name Aeromicrobium erythreum.

Amino Acids↗