• Korean Journal of Microbiology
• /
• v.49 no.3
• /
• pp.297-300
• /
• 2013

EPS producing bacteria were enumerated in ginseng root system (rhizosphere soil, rhizoplane, inside of root). EPS producing bacterial density of rhizosphere soil, rhizoplane and inside of root were distributed $9.0{\times}10^6$ CFU/g, $7.0{\times}10^6$ CFU/g, and $1.4{\times}10^3$ CFU/g, respectively. Phylogenetic analysis of the 24 EPS producing isolates based on the 16S rRNA gene sequences, EPS producing isolates from rhizosphere soil (RS) belong to genus Arthrobacter (6 strains) and Rhizobium (1 strain). EPS producing bacteria from rhizoplane (RP) were Arthrobacter (6 strains), Rhodococcus (1 strain) and Pseudomonas (1 strain). EPS producing bacteria from inside of root (IR) were categorized into Rhzobium (6 strains), Bacillus (1 strain), Rhodococcus (1 strain), and Pseudomonas (1 strain). Phylogenetic analysis indicated that Arthrobacter may be a member of representative EPS producing bacteria from ginseng rhizosphere soil and rhizoplane, and Rhizobium is typical EPS producing isolates from inside of ginseng root. The yield of EPS was 10.0 and 4.9 g/L by Rhizobium sp. 1NP2 (KACC 17637) and Arthrobacter sp. 5MP1 (KACC 17636). The purified EPS were analyzed by Bio-LC and glucose, galactose, mannose and glucosamine were detected. The major EPS sugar of these strains was glucose (72.7-84.9%).

• Journal of the Korean Society of Tobacco Science
• /
• v.2 no.2
• /
• pp.20-37
• /
• 1980

Among the 34 strains of Nicotinophiles selected in the previous experiments, strain NCT27 identified with Pseudomonas putida and strain NCT30 identified with Arthrobacter oxydans biotype nan thus were Investigated for optimization of growth conditions for nicotine degradation and other cultural characteristics. The compositions of optimized medium were to be following: $KH_2PO_4$ 2.Ogr, KCI 5.Ogr, $MgSO_4$.$7H_2O$ 20mg, $MnSO_4$.$6H_2O$ 0.2mg, $FeSO_4$.$7H_2O$ 1.Omg, Col$^{++}$ (Cobalt Acetate),2.O$\gamma$, N1$^{++}$ (NiSO4,6H2O) 0.5$\gamma$, and yeast extract 80mg per liter. The optimum initial concentrations of nicotine for growth were 0.4% for Pseudomonas and 0.1% for Arthrobacter, respectively. The optimum temperature and pH were 3$0^{\circ}C$ and 7.0 for both of strains. The pH of culture medium of Pseudomonas was changed from acidic condition to basic one in going from the logarithmic growth phase to the stationary growth phase. In contrast with Pseudomonas, it remained constant in case of Arthrobacter. The growth of Arthrobacter was completely inhibited in the nicotine concentration of 0.7&. However, Pseudomonas could grow even in the nicotine concentration of 1.0%. Moreover, it could grow successfully in the tobacco extract media as well as media containing carbon and nitrogen sources other than nicotine. The maximum rates of nicotine degradation were to be 1.22 gr./hr./liter for Pseudomonas and 0.186 gr./hr./liter for Arthrobacter, respectively.

• Journal of Microbiology and Biotechnology
• /
• v.6 no.6
• /
• pp.402-406
• /
• 1996

Inulin fructotransferase (depolymerizing) (EC 2.4.1.93) was purified 34-fold from the culture broth of Arthrobacter sp. A-6 by using a combination of ammonium sulfate fractionation, DEAE-Sepharose CL-6B chromatography and Sephacryl S-200 gel filtration. The purified enzyme converts inulin into di-D-fructofuranose dianhydride III(DFA III) and small quantities of fructo-oligosaccharides. The temperature and pH optima of the enzyme were $70^{\circ}C$ and 6.0, respectively. Molecular weight of the enzyme was determined to be 49 kDa by 12$%$ SDS-polyacrylamide gel electrophoresis, and 145 kDa by Sephacryl S-200gel filtration. This indicates that the functional inulin fructotransferase of Arthrobacter sp. A-6 has a homomeric trimer structure. The enzyme had an isoelectric point of pH 4.6. The N-terminal amino acid sequence of the purified enzyme subunit was Ala-Asp-Asn-Pro-Asp-Gly(\ulcorner)-Ser-Asn-Met(or Glu)-Tyr-Asp-Val.

• Microbiology and Biotechnology Letters
• /
• v.27 no.6
• /
• pp.471-476
• /
• 1999

Inulin fructotransferase(depolymerizing)(EC 2.4.1.93)(inulaseII) which converts inulin into di-D-fructofuranose-1,2':2,3'-dianhydride (DFAIII) was purified from Arthrobacter ureafaciens KCTC 3387 using column chromatography on DEAE-Toyopearl 650M and gel filtration of Sephadex G-200. The enzyme was purified 7-fold with a yield of 11% from a culture supernatant. The purified enzyme gave a single band on polyacrylamide gel electrophoresis, and the molecular weight of the enzyme was estimated to be 45,000 by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the enzyme reaction were pH6.5~7.0 and $55{\circ}C$, respectively. The enzyme was stable within a pH range of 5.0 to 10.6 and up to $60^{\circ}C$. The Km of this enzyme for DFAIII production was 11.9mM. The enzyme was inactivated by $Hg^{2+}$ and after exhaustive digestion of inulin by this enzyme, 1-kestose and nystose were produced in addition of DFAIII.

• Microbiology and Biotechnology Letters
• /
• v.28 no.4
• /
• pp.214-218
• /
• 2000

The inulinase producing microorganism was isolated from soil and tentatively identified as Arthrobacter protophormiae/ramosus. Inulinase was pruified by ethanol precipitation, DEAE-Sephadex ion exchange chromatography and Sephadex gel filtration chromatography. The molecular weight of the purified enzyme was 34 kDa. The specific activity, yield and purity were 31.5 Unit/mg, 19.5% and 18.5 fold, respectively. Optimal pH and temperature for reaction of the purified inulinase were 8.5 and $55^{\circ}C$, respectively. The enzyme was stable at pH 7.5, below$ 55^{\circ}C$, and the activity was stimulated Mg2+.

• Journal of Microbiology and Biotechnology
• /
• v.10 no.2
• /
• pp.275-280
• /
• 2000

The inulin fructotransferse (depolymerizing) (IFTase, EC 2.4.1.93) gene of Arthrobacter sp. A-6 was cloned and expressed in Escherichia coli and Bacillus subtilis. The IFTase gene consisted of an ORF of 1.311 nucleotides encoding a polypeptide of 436 amino acids containing a signal peptide of 31 amino acids in the N-terminus. The molecular mass of the IFTase based on the nucleotide sequence was calculated to be 46.116 Da. The recombinant E. coli $DH5{\alpha}$ cells expressing the Arthrobacter sp. A-6 IFTase gene produced most of the IFTase intracelularly. In contrast, the recombinant B. subtilis DB 104 carrying the IFTas gene on a B. subtilis-E. Coli expression vector secreted the IFTase into the culture fluid efficiently.

• Korean Chemical Engineering Research
• /
• v.54 no.1
• /
• pp.140-144
• /
• 2016

In this study, the physical factors for amylase production by Arthrobacter sp. were optimized using response surface methodology(RSM). Antarctic microorganism Arthrobacter sp. PAMC 27388 was obtained from the Polar and Alpine Microbial Collection(PAMC) at the Korea Polar Research Institute. This microorganism was confirmed for the excretion of amylase with Lugol's solution. The amylase activity was after flask culture was as low as 1.66 mU/L before optimization. The physical factors including the inoculum volume, the initial culture pH, and the medium volume were chosen to be optimized for the enhanced amylase production. The calculated results using RSM indicate that the optimal physical factors were 2.49 mL inoculum volume, 6.85 pH and 42.87 mL medium volume with a predicted amylase production of 2.84 mU/L. The experimentally obtained amylase activity was 2.50 mU/L, which was a 150% increase compared to the level before optimization.

• Korean Chemical Engineering Research
• /
• v.52 no.6
• /
• pp.834-839
• /
• 2014

This study was conducted to optimize the medium composition for carotenoid production in Arthrobacter sp. PAMC 25486 through response surface methodology (RSM). Using a Placket-Burman design, from which yeast extract, $MgSO_4$ and dextrose were identified as the significant factors affecting carotenoids production. RSM studies for carotenoids production by Arthrobacter sp. PAMC 25486 have been carried out for three parameters of yeast extract, $MgSO_4$ and dextrose concentrations. These significant factors were optimized by experiments and RSM, as 1 g/L yeast extract, 0.0879 g/L $MgSO_4$ and 1 g/L dextrose. The experimentally obtained concentration of carotenoid was 288 mg/L, and it became 2-fold increase on concentration before optimization.

• KSBB Journal
• /
• v.31 no.1
• /
• pp.58-65
• /
• 2016

In this study, Arthrobacter scleromae SYE-3, which was isolated from indigenous plant in a subtropical region, Neigeria, with plant growth promoting activity was evaluated to determine the optimal culture condition. A bacterial strain SYE-3 had the IAA productivity ($89.15{\pm}0.36mg/L$) and ACC deaminase activity ($0.20{\pm}0.06$ at 72 hours). Also, optimal culture conditions such as temperature and pH of strain SYE-3 were $20^{\circ}C$ and 10 in LB medium, respectively. Strain SYE-3 had up to 3% salt tolerance in the LB medium. Plant growth promoting ability of strain SYE-3 using yam (Dioscorea japonica Thunb.) was evaluated. As a result, strain SYE-3 had showed very powerful effect on the increase of the shoot length and root biomass of yam (190.0% and 282.41% increase for 112 days, respectively). These results indicated that Arthrobacter scleromae SYE-3 can serve as a promising microbial resource for the biofertilizers of subtropical crops.

• Journal of Soil and Groundwater Environment
• /
• v.19 no.3
• /
• pp.47-55
• /
• 2014

Arthrobacter chlorophenolicus A6 possesses several monooxygenases (CphC-I, CphC-II, and CphB) that can catalyze the transformation of 4-chlorophenol (4-CP) to hydroxylated intermediates in the initial steps of substrate metabolism. The corresponding genes of the monooxygenases were cloned, and the competent cells were transformed with these recombinant plasmids. Although CphC-II and CphB were expressed as insoluble forms, CphC-I was successfully expressed as a soluble form and isolated by purification. The specific activity of the purified CphC-I was analyzed by using 4-CP, 4-chlorocatechol (4-CC), and catechol (CAT) as substrates. The specific activities for 4-CP, 4-CC, and CAT were determined to be 0.312 U/mg, 0.462 U/mg, 0.246 U/mg, respectively. The results of this study indicated that CphC-I is able to catalyze the degradation of 4-CC and CAT in addition to 4-CP, which is a primary substrate. This research is expected to provide the fundamental information for the development of an eco-friendly biochemical degradation of aromatic hydrocarbons.