• Journal of Microbiology and Biotechnology
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• v.8 no.6
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• pp.581-587
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• 1998

Essential amino acids involved in the catalytic role of the extracellular cytosine deaminase from Chromobacterium violaceum YK 391 were determined by chemical modification studies. The enzyme activity required the reduced form of Fe (II) ion, since the enzyme was inhibited by ο-phenanthroline. The enzyme activity was completely inhibited by the chemical modifiers, such as p-chloromercuribenzoate (p-CMB), p-hydroxymercuribenzoate, and chloramine-T at 1 mM each. The enzyme activity was also markedly inhibited by pyridoxal-5'-phosphate, diethyl pyrocarbonate, and phenylmethylsulfonyl fluroride at 1 mM each. The inactivation of the enzyme activity with p-CMB was reversed by a high concentration of cytosine. Furthermore, the inactivation of the enzyme activity with p-CMB was also reactivated by 1 mM dithiothreitol, 1 mM 2-mercaptoethanol, 1 mM cysteine-HCI, 10% ethyl alcohol, and 10% methyl alcohol. These results suggested that cysteine and methionine residues might be located in or near the active site of the enzyme, while lysine, histidine, and serine residues might be indirectly involved in the enzyme activity.

• Mycobiology
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• v.45 no.4
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• pp.370-378
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• 2017

Cylindrocarpon destructans is an ascomycete soil-borne pathogen that causes ginseng root rot. To identify effective biocontrol agents, we isolated several bacteria from ginseng cultivation soil and evaluated their antifungal activity. Among the isolated bacteria, one isolate (named JH7) was selected for its high antibiotic activity and was further examined for antagonism against fungal pathogens. Strain JH7 was identified as a Chromobacterium sp. using phylogenetic analysis based on 16S rRNA gene sequences. This strain was shown to produce antimicrobial molecules, including chitinases and proteases, but not cellulases. Additionally, the ability of JH7 to produce siderophore and solubilize insoluble phosphate supports its antagonistic and beneficial traits for plant growth. The JH7 strain suppressed the conidiation, conidial germination, and chlamydospore formation of C. destructans. Furthermore, the JH7 strain inhibited other plant pathogenic fungi. Thus, it provides a basis for developing a biocontrol agent for ginseng cultivation.

• Journal of Life Science
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• v.15 no.4 s.71
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• pp.584-589
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• 2005

To investigate factors affecting the removal of phosphorus from the practical wastewater in the F-STEP PROCESS using a loess ball and Chromobacterium WS 2-14, first, the loess ball size and calcining temperature, initial pH, initial phosphorus concentration, working temperature, and aeration were studied. A $2\~4mm$ of loess ball made at $960^{\circ}C$ of calcining temperature was the most suitable one for the removal of phosphorus. When the initial pH was increased from 3.0 to 6.0, the removal efficiency of phosphorus was increased. Especially, at 6.0 of initial pH, the maximum removal efficiency of phosphorus was $88.7\%$. The maximum removal efficiency of phosphorous was gained, 1.8mg/h when the initial concentration of phosphorous was 5.0mg/1. When the operating temperature was $30^{\circ}C$, the maximum removal efficiency of phosphorus was obtained. In the case of aeration, when it was increased from 0.5 to 5.0L/min, the removal efficiency of phosphorus was increased. On the other hand, above 7.0 L/min, the removal efficiency of phosphorus did not increased. Using the optimum operation conditions, pilot tests for the effective removal efficiency of phosphorus were carried out for 65 days. The average removal efficiency of phosphorus was $92.0\%$. The average removal efficiency of COD, BOD, and SS were 77.1, 74.2, and $86.4\%$, respectively. from the results, it can be concluded that F-STEP PROCESS using loess ball might be useful process for phosphorus removal.

• The Plant Pathology Journal
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• v.17 no.6
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• pp.365.2-365
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• 2001

• Microbiology and Biotechnology Letters
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• v.27 no.4
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• pp.286-291
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• 1999

By using autoradiography and phosphate medium, high phosphate accumulating bacteria were isolated from the soil of protected cultivation area and activated sludge. Selected strain, PO8, was gram-negative, rod/spherial(0.5~0.6$\times$1.0~1.2${\mu}{\textrm}{m}$ in size) and non-motile. PI4, another selected strain, was gram-negative, rod(0.4~0.5$\times$1.5~1.6${\mu}{\textrm}{m}$ in size) and motile. It also had flagella. According to their morphological, physiological and biochemical properties, the stains were identified as Acinetobacter lwoffi PO8 and Chromobacterium lividum PI4, respectively. A. lowoffi PO8 and C. lividum PI4 cultured in the P-1 medium containing 150ppm phosphate were able to uptake high phosphate up to 92% and 85%, respectively after 24 hours at 3$0^{\circ}C$ during liquid culture.

• Proceedings of the Microbiological Society of Korea Conference
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• 2005.05a
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• pp.191.2-191
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• 2005

• Proceedings of the Korean Society of Plant Pathology Conference
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• 2002.11a
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• pp.58.1-58
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• 2002

• The Plant Pathology Journal
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• v.17 no.6
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• pp.365.3-365
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• 2001

• The Plant Pathology Journal
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• v.17 no.6
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• pp.363.5-364
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• 2001

• Journal of Microbiology and Biotechnology
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• v.9 no.2
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• pp.173-178
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• 1999

The extracellular cytosine deaminase (EC 3.5.4.1) from Chromobacterium violaceum YK 391 was purified 264.7-fold with an overall yield of 14.3%. The enzyme was for the first time homogeneous by the criteria of polyacrylamide gel electrophoresis performed in the absence and in the presence of sodium dodecyl sulfate. The molecular weight of the purified enzyme was estimated to be about 156 kDa. The enzyme consisted of two identical subunits of approximate molecular weight 78 kDa. The isoelectric point of the enzyme was pH 5.55. The enzyme had a pH optimum of 7.5 and a temperature optimum of around 40 to $45^{\circ}C$. Besides cytosine, the enzyme deaminated 5-fluorocytosine, cytidine, 5-methylcytosine, and 6-azacytosine, but not 5-azacytosine. The extracellular cytosine deaminase is believed to be unique because it was active not only on cytosine but also on cytidine. The apparent $K_m$ values for cytosine, 5-fluorocytosine, cytidine, and 5-methylcytosine were determined to be 1.55 mM, 5.52 mM, 10.4 mM, and 67.2 mM, respectively. The enzyme activity was strongly inhibited by heavy metal ions such as $Fe^{2+},Pb^{2+},Cd^{2+},Zn^{2+}, Hg^{2+}, and Cu^{2+}$ at 1 mM, and completely by $\alpha,\alpha$'-dipyridyl, and $\rho$-chloromercuribenzoate at 1 mM, and weakly inhibited by 1mM ο-phenanthroline. The enzyme activity was not affected by various nucleosides and nucleotides.