• Title/Summary/Keyword: Citrobacter sp. Y19

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Degradation oof Triphenylmrthane Dyes by Citobacter sp. (Citrobacter sp.에 의한 Triphenylmethane계 색소의 분해)

  • 민상기;조영배;전홍기
    • Journal of Life Science
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    • v.5 no.1
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    • pp.8-19
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    • 1995
  • The Optimal condition for degradation of crystal violet and other triphenylmethane dyes by Citrobacter sp. SK-3 isolated from the activated sludge of dye manufacturing factory was investigated. The optimal culture medium for the degradation of triphenylmethane dye was composed of minimum inorganic salt medium supplemented with 0.5% galactose, 0.1% beef extract, with the initial pH of 8.0 to 9.0. Under this condition, Citrobacter sp. SK-3 degraded 200 ppm of crystal violet completely within 24 hours. Citrobactre sp. SK-3 also degraded efficiently malachite green, pararosaniline, brilliant green, methyl violet, basic fuchsin and methyl red. Analysis of the degradation products of crystal violet through this layer chromatography and high performance liquid chromatography indicated that the methyl groups bound to crystal violet backborn were gradually demethylated to pentamethyl-, tetramethyl- and trimethylpararosaniline.

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Characteristics of fermentative hydrogen production by the chemoheterotrophic bacterium, Citrobacter sp. Y19

  • Seol, Eun-Hee;Oh, You-Kwan;Lee, Sang-Kil;Park, Sung-Hoon
    • 한국생물공학회:학술대회논문집
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    • 2002.04a
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    • pp.419-422
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    • 2002
  • Fermentative hydrogen production by Citrobacter sp. Y 19 was investigated in batch culture. Optimal hydrogen production activity was observed at pH 6 - 7 and temperature of $36^{\circ}C$, and hydrogen yield and maximal hydrogen production rate were 1.12 mmol/mmol glucose and 32.3 mmol/g cell${\cdot}$h, respectively. With glucose as a substrate, the bacterium produced ethanol, acetate, and carbon dioxide as major glucose fermentation by-products. Y19 could utilize various sugars such as galactose, fructose, lactose, sucrose, and starch for cell growth and hydrogen production.

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Effect of environmental and nutritional conditions on $H_2$ production from glucose by the chemoheterotropic facultative bacterium, Citrobacter sp. Y19

  • Oh, You-Kwan;Seol, Eun-Hee;Lee, Young-Kyun;Park, Sung-Hoon
    • 한국생물공학회:학술대회논문집
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    • 2001.11a
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    • pp.598-601
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    • 2001
  • Citrobacter sp. Y19 was studied for $H_2$ production from glucose in batch culture. Important conditions studied include phosphate concentration, temperature, glucose concentration, and gas-phase replacement. Optimal $H_2$ production was observed at 140 - 180 mM of phosphate and $36^{\circ}C$. When glucose concentration increased from 0.1 to 5% (w/v), $H_2$ production increased up to 2% and remained constant thereafter. Intermittent purging of the reaction bottle with Ar gas stimulated the $H_2$ production by alleviating the inhibition by $H_2$. The maximum productivity was observed to be 113.2 ml $H_2$/h-1.

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Oxygen Sensitivity of Carbon Monoxide-Dependent Hydrogen Production Activity in Citrobacter sp.

  • Kim, Jung-Rae;Oh, You-Kwan;Yoon, Yeo-Joon;Lee, Eun-Yeol;Park, Sung-Hoon
    • Journal of Microbiology and Biotechnology
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    • v.13 no.5
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    • pp.717-724
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    • 2003
  • A newly isolated Citrobacter sp. Y19 catalyzes the CO-dependent $H_2$ production (biological water-gas shift reaction) by the actions of CO dehydrogenase (CODH) and hydrogenase. Y 19 requires $O_2$ for fast growth, but its $H_2$ production activity is significantly inhibited by $O_2$. In the present study, the effect of $O_2$ on the activities of CODH ard hydrogenase was investigated quantitatively in both whole cells and broken cells, based on CO-dependent or methyl viologen (MV)-dependent $H_2$ production in addition to CO-dependent MV reduction. In crude cell extracts, CODH activity was mostly found in the soluble fraction. Inactivation of CODH and hydrogenase activities by $O_2$ followed the first-order decay kinetics, and the dependence of the rate constants on $O_2$ partial pressure could be expressed by the Michaelis-Menten equation. In whole cells, the maximum deactivation rate constants ($k_{d,max}$ of hydrogenase and CODH were quite similar: $0.07{\pm}0.03 min^{-1}\;and\;0.10{\pm}0.04 min^{-1}$, respectively. However, the first-order rate constant ($k_{d,max}/K_s$) of CODH ($0.25\;min^{-1}\;atm^{-1}$) at low $O_2$ partial pressures was about 3-fold higher than that of the hydrogenase, since the half-saturation constant ($K_s$) of CODH was about half of that of hydrogenase. In broken cells, both enzymes became significantly more sensitive to $O_2$ compared to the unbroken cells, while $k_{d,max}/K_s$ increased 37-fold for hydrogenase and 6.7-fold for CODH. When whole cells were incubated under anaerobic conditions after being exposed to air for 1 h, hydrogenase activity was recovered more than 90% in 2 h suggesting that the deactivation of hydrogenase by $O_2$ was reversible. On the contrary, CODH activity was not recovered once deactivated by $O_2$ and the only way to recover the activity was to synthesize new CODH. This study indicates that $O_2$ sensitivity of $H_2$ production activity of Citrobacter sp. Y19 is an important drawback as in other $H_2-producing$ bactria.

Isolation of Citrobacter sp. Mutants Defective in Decolorization of Brilliant Green by Transposon Mutagenesis

  • Jang, Moon-Sun;Lee, Young-Mi;Park, Yong-Lark;Cho, Young-Su;Lee, Young-Choon
    • Journal of Microbiology
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    • v.42 no.2
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    • pp.139-142
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    • 2004
  • To identify genes involved in the decolorization of brilliant green, we isolated random mutants generated by transposon insertion in brilliant green-decolorizing bacterium, Citrobacter sp. The resulting mutant bank yielded 19 mutants with a complete defect in terms of the brilliant green color removing ability. Southern hybridization with a Tn5 fragment as a probe showed a single hybridized band in 7 mutants and these mutants appeared to have insertions at different sites of the chromosome. Tn5-inserted genes were isolated and the DNA sequence flanking Tn5 was determined. By comparing these with a sequence database, putative protein products encoded by bg genes were identified as follows: bg 3 as a LysR-type regulatory protein; bg 11 as a MalG protein in the maltose transport system; bg 14 as an oxidoreductase; and bg 17 as an ABC transporter. The sequences deduced from the three bg genes, bg 2, bg 7 and bg 16, showed no significant similarity to any protein with a known function, suggesting that these three bg genes may encode unidentified proteins responsible for the decolorization of brilliant green.