• Title/Summary/Keyword: Ochrobactrum sp.

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Isolation of an Indigenous Imidacloprid-Degrading Bacterium and Imidacloprid Bioremediation Under Simulated In Situ and Ex Situ Conditions

  • Hu, Guiping;Zhao, Yan;Liu, Bo;Song, Fengqing;You, Minsheng
    • Journal of Microbiology and Biotechnology
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    • v.23 no.11
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    • pp.1617-1626
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    • 2013
  • The Bacterial community structure and its complexity of the enrichment culture during the isolation and screening of imidacloprid-degrading strain were studied using denaturating gradient gel electrophoresis analysis. The dominant bacteria in the original tea rhizosphere soil were uncultured bacteria, Rhizobium sp., Sinorhizobium, Ochrobactrum sp., Alcaligenes, Bacillus sp., Bacterium, Klebsiella sp., and Ensifer adhaerens. The bacterial community structure was altered extensively and its complexity reduced during the enrichment process, and four culturable bacteria, Ochrobactrum sp., Rhizobium sp., Geobacillus stearothermophilus, and Alcaligenes faecalis, remained in the final enrichment. Only one indigenous strain, BCL-1, with imidacloprid-degrading potential, was isolated from the sixth enrichment culture. This isolate was a gram-negative rod-shaped bacterium and identified as the genus Ochrobactrum based on its morphological, physiological, and biochemical properties and its 16S rRNA gene sequence. The degradation test showed that approximately 67.67% of the imidacloprid (50 mg/l) was degraded within 48 h by strain BCL-1. The optimum conditions for degradation were a pH of 8 and $30^{\circ}C$. The simulation of imidacloprid bioremediation by strain BCL-1 in soil demonstrated that the best performance in situ (tea soil) resulted in the degradation of 92.44% of the imidacloprid (100 mg/g) within 20 days, which was better than those observed in the ex situ simulations that were 64.66% (cabbage soil), 41.15% (potato soil), and 54.15% (tomato soil).

Isolation and Characterization of Chlorothalonil-dissipating Bacteria from Soil. (토양으로부터 Chlorothalonil 전환 미생물의 분리 및 특성)

  • 이수현;신재호;최준호;박종우;김장억;이인구
    • Microbiology and Biotechnology Letters
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    • v.32 no.1
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    • pp.96-100
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    • 2004
  • Chlorothalonil is a wide-spectrum fungicide that is widely used in the world. Chlorothalonil is known as a potential toxic pollutant due to its high application rate, persistence, and toxicity to humans and other species. With the Increase of necessity of bioremediation, this study was conducted to isolate the chlorothalonil dissipation bacteria from soil. Soil samples were collected from 184 sites of farmland and wastewater disposal soil.661 strains resistant to chlorothalonil were isolated by dilution method from chlorothalonil-containing enrichment culture. After incubating at $30^{\circ}C$ in 1/10 LB media containing 10 ppm of chlorothalonil for a week, dissipation ability of chlorothalonil was investigated by HPLC. Finally, a strain SH35B, capable of dissipating chlorothalonil efficiently, was selected. The strain SH35B was identified as Ochrobactrum sp. Ten ppm of chlorothalonil In 1/10 LB media were completely dissipated by the growth of Ochrobactrum sp. SH35B for 30 h at $30^{\circ}C$. In the isolated strain, the content of glutathione and the activity of glutathione S-transferase were supposed to be ones of the Important factors for chlorothalonil dissipation and were higher than those of control strains, Escherichia coli and Bacillus subtilis.

Electrochemical Activation of Nitrate Reduction to Nitrogen by Ochrobactrum sp. G3-1 Using a Noncompartmented Electrochemical Bioreactor

  • Lee, Woo-Jin;Park, Doo-Hyun
    • Journal of Microbiology and Biotechnology
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    • v.19 no.8
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    • pp.836-844
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    • 2009
  • A denitrification bacterium was isolated from riverbed soil and identified as Ochrobactrum sp., whose specific enzymes for denitrification metabolism were biochemically assayed or confirmed with specific coding genes. The denitrification activity of strain G3-1 was proportional to glucose/nitrate balance, which was consistent with the theoretical balance (0.5). The modified graphite felt cathode with neutral red, which functions as a solid electron mediator, enhanced the electron transfer from electrode to bacterial cell. The porous carbon anode was coated with a ceramic membrane and cellulose acetate film in order to permit the penetration of water molecules from the catholyte to the outside through anode, which functions as an air anode. A non-compartmented electrochemical bioreactor (NCEB) comprised of a solid electron mediator and an air anode was employed for cultivation of G3-1 cells. The intact G3-1 cells were immobilized in the solid electron mediator, by which denitrification activity was greatly increased at the lower glucose/nitrate balance than the theoretical balance (0.5). Metabolic stability of the intact G3-1 cells immobilized in the solid electron mediator was extended to 20 days, even at a glucose/nitrate balance of 0.1.

A Case of Ochrobactrum anthropi Infection after Using Medicinal Plants (약초 복용 후 Ochrobactrum anthropi에 감염 1예)

  • Cho, Seang-Sig;Cheun, Jai-Woo;Jeun, Chun-Bae;Park, Sang-Muk;Jang, Sook-Jin;Moon, Dae-Soo;Park, Young-Jin
    • Korean Journal of Clinical Laboratory Science
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    • v.38 no.1
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    • pp.22-25
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    • 2006
  • Ochrobactrum anthropi, previously known as Achromobacter species biotypes 1 and 2 (CDC groups Vd-1, Vd-2), belong to the groups of non-Enterobacteriaceae- nonfermentative Gram negative bacilli. Achromobacter is not presently a recognized genus. Achromobacter xylosoxidans has been transferred to genus Alcaligenes as A. xylosoxidans subsp. xylosoxidans, and "Achromobacter" sp. group Vd has been named Ochrobactrum anthropi. O. anthropi was isolated from a blood culture. Organisms were identified as O. anthropi by use of the biochemical test and the VITEK 2(bioMerieux, USA). The Organism was susceptible only to colistin, imipenem, meropenem, and tetracycline, but were resistant to amikacin, aztreonam, cefepime, ceftazidime, cefpirome, ciprofloxacin, gentamicin, isepamcin, netilmicin, pefloxacin, piperacillin, piperacillin/tazobactam, ticarcillin, ticarcillin/clavulanic acid, tobramycin, and trimethoprim/sulfamethoxazole. We report the clinical and microbiologic characteristics of O. anthropi infection in the patient. This is the first case of O. anthropi infection after using a plant as medicine at Chosun University Hospital.

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Soil Microorganism Degrading Polycaprolactone (Polycaprolactone을 분해하는 토양미생물)

  • Kim Mal-Nam
    • Korean Journal of Environmental Biology
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    • v.22 no.3
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    • pp.400-404
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    • 2004
  • Polycaprolactone (PCL), a synthetic aliphatic polyester, was buried in activated sludge soil for 66 days at $27^\circ{C}$ and $37^\circ{C}$. The morphology of the surface of PCL film degraded by soil microorganisms was observed. Soil microorganisms degrading PCL were isolated and identified. Soil fungi and soil bacteria utilizing PCL as carbon or energy source were identified as Paecilomyces fumosoroseus KH27, Penicillium digitatum KH28, Fusarium solani KH29, Aspergillus sp. KH30 and Ochrobactrum anthropi KH31, respectively. Biodegradation test of PCL by the isolated strains showed that, P. digitatum KH28 exhibited the most PCL degrading activity at $27^\circ{C}$. However, at $37^\circ{C}$ O. anthropi KH31 showed higher degrading activity than the other soil microorganisms tested.

Characterization of Ribose-5-Phosphate Isomerase B from Newly Isolated Strain Ochrobactrum sp. CSL1 Producing ʟ-Rhamnulose from ʟ-Rhamnose

  • Shen, Min;Ju, Xin;Xu, Xinqi;Yao, Xuemei;Li, Liangzhi;Chen, Jiajia;Hu, Cuiying;Fu, Jiaolong;Yan, Lishi
    • Journal of Microbiology and Biotechnology
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    • v.28 no.7
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    • pp.1122-1132
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    • 2018
  • In this study, we attempted to find new and efficient microbial enzymes for producing rare sugars. A ribose-5-phosphate isomerase B (OsRpiB) was cloned, overexpressed, and preliminarily purified successfully from a newly screened Ochrobactrum sp. CSL1, which could catalyze the isomerization reaction of rare sugars. A study of its substrate specificity showed that the cloned isomerase (OsRpiB) could effectively catalyze the conversion of $\text\tiny{L}$-rhamnose to $\text\tiny{L}$-rhamnulose, which was unconventional for RpiB. The optimal reaction conditions ($50^{\circ}C$, pH 8.0, and 1 mM $Ca^{2+}$) were obtained to maximize the potential of OsRpiB in preparing $\text\tiny{L}$-rhamnulose. The catalytic properties of OsRpiB, including $K_m$, $k_{cat}$, and catalytic efficiency ($k_{cat}/K_m$), were determined as 43.47 mM, $129.4sec^{-1}$, and 2.98 mM/sec. The highest conversion rate of $\text\tiny{L}$-rhamnose under the optimized conditions by OsRpiB could reach 26% after 4.5 h. To the best of our knowledge, this is the first successful attempt of the novel biotransformation of $\text\tiny{L}$-rhamnose to $\text\tiny{L}$-rhamnulose by OsRpiB biocatalysis.

Identification of a Second Type of AHL-Lactonase from Rhodococcus sp. BH4, belonging to the α/β Hydrolase Superfamily

  • Ryu, Du-Hwan;Lee, Sang-Won;Mikolaityte, Viktorija;Kim, Yea-Won;Jeong, Haeyoung;Lee, Sang Jun;Lee, Chung-Hak;Lee, Jung-Kee
    • Journal of Microbiology and Biotechnology
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    • v.30 no.6
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    • pp.937-945
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    • 2020
  • N-acyl-homoserine lactone (AHL)-mediated quorum sensing (QS) plays a major role in development of biofilms, which contribute to rise in infections and biofouling in water-related industries. Interference in QS, called quorum quenching (QQ), has recieved a lot of attention in recent years. Rhodococcus spp. are known to have prominent quorum quenching activity and in previous reports it was suggested that this genus possesses multiple QQ enzymes, but only one gene, qsdA, which encodes an AHL-lactonase belonging to phosphotriesterase family, has been identified. Therefore, we conducted a whole genome sequencing and analysis of Rhodococcus sp. BH4 isolated from a wastewater treatment plant. The sequencing revealed another gene encoding a QQ enzyme (named jydB) that exhibited a high AHL degrading activity. This QQ enzyme had a 46% amino acid sequence similarity with the AHL-lactonase (AidH) of Ochrobactrum sp. T63. HPLC analysis and AHL restoration experiments by acidification revealed that the jydB gene encodes an AHL-lactonase which shares the known characteristics of the α/β hydrolase family. Purified recombinant JydB demonstrated a high hydrolytic activity against various AHLs. Kinetic analysis of JydB revealed a high catalytic efficiency (kcat/KM) against C4-HSL and 3-oxo-C6 HSL, ranging from 1.88 x 106 to 1.45 x 106 M-1 s-1, with distinctly low KM values (0.16-0.24 mM). This study affirms that the AHL degrading activity and biofilm inhibition ability of Rhodococcus sp. BH4 may be due to the presence of multiple quorum quenching enzymes, including two types of AHL-lactonases, in addition to AHL-acylase and oxidoreductase, for which the genes have yet to be described.