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PubMed2001

Reaction kinetics and modeling of the enzyme-catalyzed production of lactosucrose using beta-fructofuranosidase from Arthrobacter sp. K-1.

Lactosucrose synthesis from sucrose and lactose was carried out by using beta-fructofuranosidase from Arthrobacter sp. K-1. The transfructosylation mechanism was found to be of an ordered bi-bi type in which sucrose was bound first to the enzyme and lactosucrose was released last. Hydrolysis side-reaction experiments indicated that the reactions were uncompetitively inhibited by glucose and lactose, while no inhibition by fructose was apparent. The overall reaction rates were formulated. The reaction rate constants, equilibrium constant, and dissociation and Michaelis constants were determined at 35 degrees C and 50 degrees C by fitting the experimental concentration changes with the calculated values by a nonlinear least-square method. The average relative derivation for the concentrations was 9.67%. The kinetic parameters were also calculated for 43 degrees C and 60 degrees C by assuming the Arrhenius law, and the course of reaction was predicted. The obtained reaction rate equations well represented the concentration changes during the experiment at all temperatures.

Algorithms↗
PubMed2005

Optimum culture conditions for the production of N-substituted formamide deformylase by Arthrobacter pascens F164.

We investigated the optimum culture conditions for the production of a novel enzyme, N-substituted formamide deformylase, which acts mainly on N-benzylformamide, in Arthrobacter pascens F164. The highest enzyme activity was obtained when this strain F164 was cultivated in a synthetic medium with N-benzylformamide as sole nitrogen source. This deformylase was found to be an inducible enzyme depending on N-benzylformamide.

Amidohydrolases↗
PubMed2004

Hexavalent chromium reduction by an actinomycete, arthrobacter crystallopoietes ES 32.

Environmental contamination by hexavalent chromium, Cr(VI), presents a serious public health problem. This study assessed the reduction of Cr(VI) by intact cells and a cell-free extract (CFE) of an actinomycete, Arthrobacter crystallopoietes (strain ES 32), isolated from soil contaminated with dichromate. Both intact cells and CFE of A. crystallopoietes, displayed substantial reduction of Cr(VI). Intact cells reduced about 90% of the Cr(VI) added within 12 h and Cr(VI) was almost completely reduced after 24 h. The KM and Vmax of Cr(VI) bioreduction by intact cells were 2.61 microM and 0.0142 micromol/min/mg protein, respectively. Cell-free chromate reductase of the A. crystallopoietes (ES 32) reduced hexavalent chromium at a KM of 1.78 microM and a Vmax of 0.096 micromol/min/mg protein. The rate constant (k) of chromate reduction was inversely related to Cr(VI) concentration and the half-life (t1/2) of Cr(VI) reduction increased with increasing concentration. A. crystallopoietes produced a periplasmic chromate reductase that was stimulated by NADH. Results indicate that A. crystallopoietes ES 32 can be used to detoxify Cr(VI) in polluted sites, particularly in stressed environments.

Actinobacteria↗
PubMed1988

Enzymatic dehalogenation of 4-chlorobenzoate by extracts from Arthrobacter sp. SU DSM 20407.

In extracts from Arthrobacter sp. SU DSM 20407 an enzyme was detectable, that converted 4-chlorobenzoate into 4-hydroxybenzoate. This conversion was also observed when no oxygen was present in the reaction mixture. Boiling for 5 min destroyed the enzyme activity. 4-Bromo- and 4-iodobenzoate were substrates for the enzyme too, but not 4-fluorobenzoate, 4-chlorophenylacetate and 4-chlorocinnamic acid. The enzyme showed optimum activity at 16 degrees C and at pH 7-7.5. The specific activity in the extracts varied between 0.5 and 5 mU/mg of protein. Zn2+ and Cu2+ inhibited the enzyme, while H2O2 slightly activated. In contrast to all other 4-chlorobenzoate dehalogenases described before the enzyme was not inhibited by EDTA, nor was it activated by Mn2+. Other divalent ions also had no effect. The molecular mass of the enzyme was 45,000 +/- 5,000 Da as judged by gel-filtration.

Arthrobacter↗
PubMed1990

Microbial metabolism of quinoline and related compounds. VI. Degradation of quinaldine by Arthrobacter sp.

Quinaldine catabolism was investigated with the bacterial strain Arthrobacter sp., which is able to grow aerobically in a mineral salt medium with quinaldine as sole source of carbon, nitrogen and energy. The following degradation products of quinaldine were isolated from the culture fluid and identified: 1H-4-oxoquinaldine, N-acetylisatic acid, N-acetylanthranilic acid, anthranilic acid, 3-hydroxy-N-acetylanthranilic acid and catechol. 3-Hydroxy-N-acetylanthranilic acid was not further metabolized by this organism. A degradation pathway is proposed.

Arthrobacter↗
PubMed1993

Microbial metabolism of quinoline and related compounds. XVI. Quinaldine oxidoreductase from Arthrobacter spec. Rü 61a: a molybdenum-containing enzyme catalysing the hydroxylation at C-4 of the heterocycle.

Quinaldine oxidoreductase from Arthrobacter spec. Rü 61a converts quinaldine to 1H-4-oxoquinaldine. The enzyme was purified 70-fold to apparent homogeneity in a 5-step procedure with a recovery of 4%. The molecular mass of the native enzyme was calculated to be 340,000 Da by gel filtration. SDS-polyacrylamide gel electrophoresis of the enzyme revealed 3 protein bands corresponding to 82,000 Da, 35,000 Da and 22,000 Da. The enzyme contained 1.6 atoms of molybdenum, 8 atoms of iron, 8 atoms of acid labile sulfur, 2 molecules of FAD and as part of the molybdenum cofactor, molybdopterin cytosine dinucleotide. Due to the composition of the cofactors the quinaldine oxidoreductase belongs to the class of molybdo-iron/sulfur-flavoproteins. Cyanide, arsenite and 4-hydroxymercuribenzoate were effective inhibitors whereas the enzyme was not affected by methanol.

Amino Acid Sequence↗
PubMedDate not supplied

Marine biosurfactants, II. Production and characterization of an anionic trehalose tetraester from the marine bacterium Arthrobacter sp. EK 1.

Within a screening for biosurfactants we could isolate various n-alkanes utilizing marine bacteria which were capable of synthesizing glycolipids. One strain was identified as Arthrobacter sp. EK 1 which produced trehalose lipids. After purification by column and thick layer chromatography the main fraction, an anionic 2,3,4,2'-trehalose tetraester, was obtained. The chain lengths of fatty acids ranged from 8 up to 14, furthermore succinate could be detected. Since the place of substitution of succinate has so far not been cited in literature, a definitive structural elucidation was carried out chemically by hydroboration and by 1H, 2D1H, 13C and 13C-1H correlation NMR measurements. All investigations confirmed the exact position of succinate at C 2 atom of trehalose. After improvement of growth conditions the production of the trehalose tetraester increased up to 4.8 milligrams during a fermentation in 20 l bioreactor under nitrogen limitation.

Animals↗
PubMed2001

Flow-through chemiluminescence sensor using immobilized histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007 and peroxidase for selective determination of histamine.

A flow sensor with immobilized oxidases is proposed for the determination of histamine in fish meat. Chemiluminometric measurement of histamine was based on the luminol reaction with hydrogen peroxide produced by immobilized histamine oxidase (EC 1.4.3.-.) and peroxidase (EC 1.11.1.7.) within a flow cell. Histamine oxidase was found in cells of Arthrobacter crystallopoietes KAIT-B-007 isolated from soil. The oxidase and peroxidase were coimmobilized covalently on tresylated hydrophilic vinyl polymer beads and packed into transparent PTFE; the tubing was used as the flow cell. One assay for histamine was done at intervals of 2 min without carryover. The calibration curve for histamine was linear from 0.1 microM to 50 microM. The response was reproducible within 1.25% of the relative standard deviation for 115-replicate injections of 50 microM histamine. The sensor system was applied to the determination of histamine in fish meat extracts.

Amine Oxidase (Copper-Containing)↗
PubMed1975

Bacterial carotenoids, XLVI. C50-Carotenoids, 14. C50-Carotenoids from Arthrobacter glacialis.

From the psychrophilic bacterium Arthrobacter glacialis have been isolated three C50-carotenoids with molecular formulae C50H72O2: the bicyclic decaprenoxanthin (1a, 7% of total carotenoids), the aliphatic bisanhydrobacterioruberin (2a, 10%) and the monocyclic A.g. 470 (3a, 83%). Decaprenoxanthin (1) and bisanhydrobacterioruberin (2) were in all respects, including chiroptical properties, identical with known carotenoids. The constitution of the previously undescribed A.g. 470 (3a) followed from its spectral properties (electronic, 1H NMR including Eu-shift experiments and mass spectra) and derivatization to 3b and 3c. 3a suffered remarkable elimination to the tridecaene 4a (C47H64O) upon DMSO/KOMe/MeOH treatment. Judged by CD data A.g. 470 (3a) also in stereochemical respect 3a appears to be half decaprenoxanthin (1a)+half bisanhydrobacterioruberin (2a). The intensity ratios of the M-92/M-106 ions on electron impact of 3a,b,c and 4a,b are consistent with the general theory.

Arthrobacter↗
PubMedDate not supplied

[Effect of various carbon sources on cholinesterase formation by Arthrobacter simplex var. cholinesterasus].

The effect of carbohydrates, aromatic alcohols, choline and acetylcholine on the biomass production and biosynthesis of choline esterase was studied with Arthrobacter simplex var. cholinesterasus. Fructose was found to be the best carbon source for the biomass accumulation and synthesis of choline esterase. Almost the same amount of the enzyme was produced on media with glucose and maltose as on the medium with fructose though the biomass yield was much lower. On the contrary, the biomass production was higher on media with acetylcholine and ethanol, but synthesis of the enzyme was inhibited. Choline was not assimilated by the culture. Differences in assimilation of glucose and fructose by the culture were found to depend on their concentration and the presence, or absence, of the inductor (acetylcholine) in the medium. Fructose was assimilated by the culture almost completely irrespective of its concentration and the presence of the inductor in the medium. Glucose was assimilated partly, best of all at a concentration of 0.5%. An increase of the concentration to 1% inhibited assimilation of glucose by the organism though had no effect on the biomass production and synthesis of the enzyme. The inductor stimulated assimilation of glucose by a factor of 1.5. Synthesis of choline esterase on the medium with acetylcholine at a concentration of 1% was increased more than twofold upon addition of glucose at a concentration of 0.1%. Biosynthesis of the enzyme rised with glucose concentration though accumulation of the biomass was inhibited. Inhibition of choline esterase synthesis on the medium with acetylcholine as a sole carbon source is due to a lack of energy and the absence of synthesis of carbon compounds which are acceptors of acetyl and methyl groups.

Acetylcholine↗
PubMed1998

Transformation of cortisone acetate using immobilized Arthrobacter simplex cells.

A new cell immobilization method was developed in which cells of Arthrobacter simplex BY-2-3-51 were immobilized by entrapment with a polyvinyl alcohol-alginate complex carrier. The immobilized cells preparation contains spherical beads with high mechanical strength and delta 1-dehydrogenase activity. The activation conditions and enzymatic properties of the immobilized cells were studied. When the initial substrate concentration was 20 mg/mL, the conversion of cortisone acetate to prednisone acetate by immobilized cells in the shaken culture was 98% at 18 hours. The stability of immobilized cells was maintained by activation at proper times.

Arthrobacter↗
PubMed1998

Cloning, sequencing and characterisation of a downstream region of ksdDI operon of Arthrobacter simplex.

An 8-kb region downstream of the ketosteroid dehydrogenase (ksdD)-ketosteroid isomerase (ksdI) genes of Arthrobacter simplex was cloned. The nucleotide sequence of the first 3-kb segment downstream of ksdD-ksdI operon was determined. Three open reading frames (ORFs) preceded by Shine-Dalgarno (SD) sequences have been found. Homology search revealed that the putative product encoded by ORF3 has high level of similarity with the 3-oxosteroid dehydrogenases from A. simplex and P. testosteroni (90% identity in their putative active sites). The role of ORF3 product as a FAD-containing dehydrogenase in steroid degradation pathway is discussed.

Amino Acid Sequence↗
PubMedDate not supplied

[Reproductive resting forms of Arthrobacter globiformis].

Submerged cultures of Arthrobacter globiformis grown in media unbalanced with respect to carbon and nitrogen sources were found to contain cells exhibiting features typical of resting forms: long-term viability, specific ultrastructure, dormant metabolism, and thermoresistance. Such cells were produced not only in the collection strain VKM B-1112, but also in the A. globiformis strains isolated from 2- to 3-million-year-old permafrost sediments.

Adaptation, Physiological↗
PubMedDate not supplied

[Formation of resting forms of Arthrobacter globiformis in autolysing cell suspensions].

Under conditions of spontaneous or induced autolysis of thick cell suspensions, Arthrobacter globiformis strains produced cells exhibiting features typical of resting microbial forms. The number of viable resting cells was greater under conditions of induced rather than spontaneous autolysis. The thermoresistance of the resting cells of A. globiformis strains isolated from 2- to 3 million-year-old permafrost was higher than that of the collection A. globiformis strain.

Adaptation, Biological↗
PubMed2001

[Studies on bioconversion conditions and stereoselectivity of Arthrobacter K1108 hydantoinase].

The bioconversion conditions of hydantoinase of Arthrobacter K1108 were studied. It was shown that the optimum temperature of the enzyme is 55 degrees C, and the optimum pH is 7.0. The enzyme can be activated by Co2+ and Fe2+, while inhibited by Ca2+. The optimal substrate of the hydantoinase is 5-benzylhydantoin, while 5-phenylhydantoin and 5-indolylmethylhydantoin cannot effectively digested, showing a high specificity on the substrates. An investigation on the hydantoinase stereoselectivity mechanism showed that the N-carbamoylamino acid hydrolase is stereoselective but the hydantoin hydrolase is not.

Amidohydrolases↗
PubMedDate not supplied

[The role of low-molecular-weight nitrogen compounds in the osmotolerance of Rhodococcus erythropolis and Arthrobacter globiformis].

Investigations showed that Rhodococcus erythropolis E-15 and Arthrobacter globiformis 2F cells respond to osmotic shock by increasing the synthesis of free amino acids, primarily glutamic acid (80% of the intracellular free amino acid pool). The osmoprotective role of glutamic acid follows from its beneficial effect on the growth of bacteria in high-salinity media. It was found that the addition of this amino acid to the growth medium at a concentration of 2 mM shortened the lag phase and increased the growth rate and biomass yield of either of the two bacteria. The addition of another osmoprotectant, trehalose, to the high-salinity growth medium of R. erythropolis E-15 at the same concentration (2 mM), restored the growth parameters of this bacterium to the control values.

Amino Acids↗
PubMedDate not supplied

[Facultative methylotroph belonging to the genus Arthrobacter].

A bacterial strain has been isolated and identified, on the basis of its morphological and physiologo-biochemical properties, as Arthrobacter globiformis. The bacterium is a facultative methylotroph and grows not only on media with various organic compounds but also in the presence of methylated amines as a sole source of carbon, nitrogen, and energy. Other C1-substrates were not utilized.

Amines↗
PubMed2002

[Studies on hydantoinase producing conditions of Arthrobacter K1108].

The hydantoinase-producing conditions from strain Arthrobacter K1108 were investigated. It is shown that the hydantoinase in the strain is intracellular and inducible. Its optimal inducer is 5-benzylhydantoin, while 5-indolylmethylhydantoin and 5-phenylhydantoin cannot induce the production of hydantoinase in K1108. A gratuitous inducer was designed, with which the hydantoinase production is 343% as much as that with 5-benzylhydantoin. The media for culturing the bacteria were screened and optimized. Under optimal conditions, the specific activity of K1108 cells reached 10.8 U/mL.

Amidohydrolases↗