• 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.

• Journal of Microbiology and Biotechnology
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• v.19 no.10
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• pp.1184-1190
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• 2009

A thermostable extracellular $\beta$-mannanase from the culture supernatant of a fungus Aspergillus niger gr was purified to homogeneity. SDS-PAGE of the purified enzyme showed a single protein band of molecular mass 66 kDa. The $\beta$-mannanase exhibited optimum catalytic activity at pH 5.5 and $55^{\circ}C$. It was thermostable at $55^{\circ}C$, and retained 50% activity after 6 h at $55^{\circ}C$. The enzyme was stable at a pH range of 3.0 to 7.0. The metal ions $Hg^{2+}$, $Cu^{2+}$, and $Ag^{2+}$ inhibited complete enzyme activity. The inhibitors tested, EDTA, PMSF, and 1,10-phenanthroline, did not inhibit the enzyme activity. N-Bromosuccinimide completely inhibited enzyme activity. The relative substrate specificity of enzyme towards the various mannans is in the order of locust bean gum>guar gum>copra mannan, with $K_m$ of 0.11, 0.28, and 0.33 mg/ml, respectively. Since the enzyme is active over a wide range of pH and temperature, it could find potential use in the food-processing industry.

• Journal of Applied Biological Chemistry
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• v.49 no.4
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• pp.135-139
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• 2006

A alkalophilic strain, Bacillus licheniformis MH31 producing an alkaline protease was isolated from mine soil of Boryeong in Korea. Production of a high level of alkaline protease was achieved 42 h after incubation when the bacterium was grown at pH 9.0 and $35^{\circ}C$ in Horikoshi medium supplemented with 0.5%(w/v) starch and 1%(w/v) skim milk as carbon and nitrogen source, respectively. The molecular weight of partially purified enzyme was estimated to be 30 kDa by SDS-PAGE and its optimum pH was pH 10. The enzyme showed optimum temperature at $50^{\circ}C$, and was stable up to $60^{\circ}C$ after 1 h incubation. The protease was strongly inhibited by 1 mM of PMSF which was known well as strong inhibitor of serine proteases, but almost not inhibited by 5 mM of EDTA and 1,10-phenanthroline. When the protein hydrolysis products of 1% skim milk by partially purified protease was compared with available commercial proteases using HPLC analysis, most of hydrolysis products were detected below molecular weight of 10,000 and the hydrolysis ratio of purified enzyme was 24.8% lower than those(above 32%) of commercial proteases.

• The Korean Journal of Mycology
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• v.33 no.2
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• pp.75-80
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• 2005

A carboxymethyl cellulase (CMCase) has been purified from Loweporus roseoalbus. The molecular weight of the purified CMCase was estimated to be 28.5 kDa by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The maximum activity of the purified CMCase was observed at pH 4.0 and $30^{\circ}C$, and stable for pH 3 to 5 to maintain 60% activity. The CMCase activity was activated by SDS and inhibited by PMSF and 1,10-phenanthroline. The enzyme activity was also decreased by the addition of ethylene diamine tetraacetic acid (EDTA), suggesting that the purified CMCase is metalloenzyme.

• Bulletin of the Korean Chemical Society
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• v.34 no.12
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• pp.3547-3552
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• 2013

Single crystal EPR and optical studies of a mixed ligand zinc(II) complex doped with VO(II) ion is carried out to establish the structural properties. The angular variation of vanadyl hyperfine lines indicates a single site, with spin Hamiltonian parameters as: $g_{xx}=1.985$, $g_{yy}=1.979$, $g_{zz}=1.943$; $A_{xx}=8.71$, $A_{yy}=6.41$ and $A_{zz}=17.80$ mT. By comparing the direction cosines of principal g and A values with the direction cosines of metalligand bonds, it has been confirmed that the vanadyl ion has entered the lattice interstitially. The exact interstitial position of VO(II) in host lattice has been calculated using the fractional coordinates of atoms in the host lattice out of many assumptions. The EPR and optical data have been confirmed to obtain various bonding parameters, from which the nature of the bonding in the complex is discussed. FT-IR confirms the formation of structure of host lattice.

• Bulletin of the Korean Chemical Society
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• v.32 no.9
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• pp.3255-3260
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• 2011

Two novel binuclear metal-organic coordination complexes $[Cd_2(L)_2(bpy)_2(H_2O)_2]{\cdot}6H_2O$ (1), $[Cd_2(L)_2(phen)_2-(H_2O)_2]{\cdot}2H_2O$ (2) (where L = 2-methylquinoline-3,4-dicarboxylate dianion, bpy = 2,2'-bipyridine, phen = 1,10-phenanthroline) have been synthesized under hydrothermal conditions and characterized by single crystal Xray diffraction, spectral method (IR), elemental analysis and thermal gravimetric analysis (TGA). Both 1 and 2 consist of two Cd(II) atoms bridged by two monoatomic bridging carboxylate groups from two L ligands, and the second carboxylate group of each L is monodentately coordinated to Cd(II), creating a sevenmembered chelating ring. The coordination at each metal nucleus is completed by a water molecule and a chelating bidentate molecule. The 3D structures of the complexes are stabilized by ${\pi}-{\pi}$ stacking interactions and hydrogen-bonds.

• 한국정보디스플레이학회:학술대회논문집
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• 2005.07b
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• pp.1280-1283
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• 2005

A novel zinc complex, Zn(phen)q, was synthesized from 1,10-phenanthroline (phen) and 8-hydroxyquinoline (q) as organic ligands and its electroluminescent (EL) properties were characterized. The structure of Zn(phen)q was elucidated by FT-IR, UV-Vis and XPS. The complex Zn(phen)q showed thermal stability up to $300^{\circ}C$ under nitrogen flow, which was measured by TGA and DSC. The photoluminescence (PL) of the Zn(phen)q was measured from the THF solution and the solid film on quartz substrate. The PL emission of Zn(phen)q exhibited green light centered at about 505nm. The EL devices were fabricated by the vacuum deposition. The EL devices having the structure of ITO/a-NPD/Zn(phen)q/Li:Al were studied, where 4,4'-bis[N-(1-naphthyl)-N-phenylamino]biphenyl(a-NPD) used as a hole transport layer(HTL). a-NPD has high Tg of $96^{\circ}C$ and thus makes the device thermally stable. The EL emission of Zn(phen)q exhibited also green light centered at 532nm.

• Biotechnology and Bioprocess Engineering:BBE
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• v.10 no.6
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• pp.593-598
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• 2005

A collagenolytic enzyme, produced by Vibrio vulnificus CYK279H, was purified by ultrafiltration, dialysis, Q-Sepharose ion exchange and Superdex-200 gel chromatography. The enzyme from the supernatant was purified 13.2 fold, with a yield of 11.4%. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be approximately 35.0kDa. The N-terminal sequence of the enzyme was determined as Gly-Asp-Pro-Cys-Met-Pro-Ile-Ile-Ser-Asn. The optimum temperature and pH for the enzyme activity were $35^{\circ}C$ and 7.5, respectively. The enzyme activity was stable within the pH and temperature ranges 6.8-8.0 and $20{\sim}35^{\circ}C$, respectively. The purified enzyme was strongly activated by $Zn^{2+},\;Li^{2+},\;and\;Ca^{2+}$, but inhibited by $Cu^{2+}$. In addition, the enzyme was strongly inhibited by 1, 10-phenanthroline and EDTA. The purified enzyme was suggested to be a neutral metalloprotease.

• Transactions on Electrical and Electronic Materials
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• v.11 no.3
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• pp.145-148
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• 2010

White organic light emitting devices were fabricated to improve the stability through a structural change using the two peak emission method. The fabricated devices were composed of indium tin oxide (100 nm)/ $\alpha$-NPD (30 nm)/4,40-bis(2,20-diphenylvinyl)-1,10-biphenyl (DPVBi, d: variable)/DPVBi: Rubrene (40 nm)/2,9-dimethyl-4,7-diphenyl-1,10-phenanthroline(5 nm)/ $Alq_3$(5 nm)/ Al (100 nm). A DPVBi for blue emissions was used as the host material in the emitters. The doping concentration of the Rubrene was fixed at 2.0% (by weight). The white emission with Commission Internationale De L'Eclairage coordinates of (0.3342, 0.3439) occurred at 14 V with a thickness d of 1 nm. It was insensitive to the drive voltage, and the devices had a maximum luminance of $211\;cd/cm^2$. At 19 V, the current density and maximum external quantum efficiency were $173\;mAcm^2$ and 0.478%, respectively.

• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.22 no.4
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• pp.327-332
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• 2009

In the devices structure of ITO/N,N'-diphenyl-N,N' bis (3-methylphenyl)-1,1'-biphenyl-4,4'-diamine (TPD) /tris (8-hydroxyquinoline)aluminum$(Alq_3)$electron-transport-layer(ETL)(2,9-Dimethyl-4,7-diphenyl-1,10-phenanthroline(BCP))/Al, we have studied the efficiency improvement of organic light-emitting diodes depending on the thickness variation of BCP using electron transport layer. The thickness of TPD and $Alq_3$ was manufactured 40 nm, 60 nm under a base pressure of $5{\times}10^{-6}$ Torr using at thermal evaporation, respectively. The TPD and $Alq_3$ layer were evaporated to be deposition rate of $2.5{\AA}/s$. And the BCP was evaporated to be a4 a deposition of $1.0{\AA}/s$. As the experimental results, we found that the luminous efficiency and the external quantum efficiency of the device is superior to others when thickness of BCP is 5 nm. Also, operating voltage is lowest. Compared to the ones from the devices without BCP layer, the luminous efficiency and the external quantum efficiency were improved by a factor of four hundred ninty and five hundred, respectively. And operating voltage is reduced to about 2 V.