• Journal of Korean Society on Water Environment
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• v.23 no.3
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• pp.377-384
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• 2007

This study has carried out a performance of dimensionally stable anode for the purpose of decolorization of Rhodamine B (RhB) in water. Seven kinds of 1, 2 and 3 component electrodes were prepared by plating and thermal deposition, which were coated by the oxides of Pt, Ru, Ir, Sn-Sb, Ir-Sn-Sb, Ru-Sn-Sb and Ru-Sn-Ti on Ti metal surface, respectively. Performance for RhB decolorization of the seven electrodes lay in: Ru-Sn-Ti/Ti ${\fallingdotseq}$ Ru-Sn-Sb/Ti > Ir-Sn-Sb/Ti > Sn-Sb/Ti > Ru/Ti > Ir/Ti > Pt/Ti. The effects of electrode area and distance, electrolyte type and concentration, current density and pH were investigated on the decolorization of RhB using Ru-Sn-Ti/Ti electrode. Decolorization of RhB was not influenced by electrode area and distance largely, however wattage was influenced by them. NaCl was superior to the decolorization of RhB than $Na_2SO_4$. Optimum NaCl dosage and current density were 0.5 g/L and $0.183A/cm^2$, respectively. The pH effect of decolorization of RhB was not significant within the range of 3-7.

• Journal of the Korean Chemical Society
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• v.59 no.3
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• pp.209-214
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• 2015

The formation of complexes between SO₂ and acetic acid was studied theoretically. The ab initio and DFT calculations were performed with MP2 and B3LYP methods using 6-311++G(d,p), aug-cc-pVDZ and aug-cc-pVTZ basis sets. Six stable complexes were identified, and three stable bidentate complexes, C1, C2 and C3, were formed between SO₂ and syn-acetic acid, which is more stable form of acetic acid. Anti-acetic acid also form three complexes, C4, C5 and C6, with SO₂. C4 is bidentate and C5, C6 are monodentate complexes, which are less stable. The most stable complex, C1 has S⋯O=C and O⋯H-O interactions, and the S⋯O and O⋯H distances are less than the sum of van der Waals radii. The vibrational frequencies of complexes were calculated and were compared with those of monomers. The frequency shifts after formation of complex were found, and the overall pattern of frequency shifts relative to monomers is similar among the six complexes.

• Korean Journal of Microbiology
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• v.30 no.4
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• pp.305-309
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• 1992

Cytosine deaminase (EC 3.5.4.1) from BaciNus stc~urorhermophilus was partially purified 7.2-fold with an overall yield of 52.7%. The partially purified enzyme deiiminated cytosine only.but not 5-methylcytosine and 5-fluorocytosine. The apparent Michaclis constant. Km valuefor cytosine was 5.9 mM. The enzyme was relatively stable in the range of pH 4.0 to 7.0.furthermore extremely thermo-stable : more than 75'X) of the activity was remained afterheating at 80$^{\circ}$C for I0 min at pH 6.5. The enzyme had a pH optimum at around pH7.0 to 7.5. and temperature optimum at 35 to 31$^{\circ}$C. And the activation energ (En value)determined from an Arrhenius plot was 26 Kcal/mol. The enzyme activity was stronglyinhibited by heavy metal ions such as Cd", Hg". Cut' at 1 mM, anJ by o-phenanthroline,and p-chloromcrcuribcnzoate at I mM. But the enrymc activity was activatetl increased byGMP, and CMP at 1 mM.ased by GMP, and CMP at 1 mM.

• Food Science and Biotechnology
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• v.15 no.3
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• pp.453-457
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• 2006

Activity and stability of kiwifruit actinidine was determined in various conditions of pH, salt, and temperature using N-${\alpha}$-CBZ-lysine P-nitrophenyl ester as the substrate. Actinidine activity was low below pH 6, and undetectable below pH 3. The enzyme was stable in a pH range of 6.0-8.5. At $4^{\circ}C$ the enzyme was inactive in the presence of greater than 36% vinegar and in 2 M NaCl. Actinidine at $25^{\circ}C$ was unstable in 24% vinegar but stable in up to 3 M NaCl. With regard to freeze-thaw stability, actinidine retained 85% residual activity after being frozen at $-20^{\circ}C$ for 3 days. Based on Arrenius and Lineweaver-Burk plots, actinidine became unstable at greater than $45^{\circ}C$ with only 30% residual activity remaining after 6 min. The Km, kcat, and kcat/Km values of actinidine were $56\;{\mu}M$, 67/sec, and $1.2\;{\mu}M/sec$, respectively.

• Journal of Mushroom
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• v.18 no.4
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• pp.303-310
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• 2020

The cultivation of Sparassis crispa in the beginning of the 2000s in South Korea, and the cultivar 'Neowul' bred in the Chonbuk Agricultural Research and Extension Service were registered first in 2016. However, there is no manual for the cultivation of Sparassis crispa, and therefore, there remains a big difference in its harvest rate across farms. Herein, we aimed to study the primordium formation conditions of Sparassis crispa 'Neowul' according to the medium pH, medium moisture content, and inoculum volume of liquid spawn and develop a stable production technology. We found the annual yield per bottle relating to the cultivation period, harvest rate, and the weight of fruiting body to be the highest at 363.6 g in the area cultivated at pH 3.8. However, it is thought that cultivation by adjusting the pH to 3.9±1 would be necessary for stable production, considering that at pH 3.6, the yield sharply reduced to 189.5 g. Moreover, the culture period was shorter at pH 4.0 compared with that at pH3.8, and the cultivation period at pH 4.0 was the same as that at pH 3.8. No significant difference in the weight of the fruiting body at different conditions was recognized. Additionally, it is difficult to regulate the pH precisely in practical applications in the farms. It is thought that 341.8 g Sparassis crispa will be produced per bottle annually if the medium moisture content is adjusted to 65%, liquid spawn inoculum volume is equivalent to 4% of the medium volume, and the humidity in the culture room is set to below 50%.

• Microbiology and Biotechnology Letters
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• v.15 no.6
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• pp.436-440
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• 1987

Pullulanase gene (pul) of Klebsiella pneumoniae NFB-320 which was cloned previously in Escherichia coli with plasmid pBR322. The gene was analyzed with various restriction enzymes. The cloned gene was contained within n 10 kb BamHI DNA fragment. We constructed the restriction map of the hybrid plasmid pYKL451. The optimum temperatures for pullulanases produced in E. coli (pYKL451) and K. pneumoniae NFB-320 were almost the same, 50-55 $^{\circ}C$. The optimum pHs for the reaction of the enzymes produced by E. coli (pYKL451) and K. pneumoniae NFB-320 was 6.0. Both enzyme preparations were stable under the range of pH 5.0 to 10.0 when those were kept at 40 $^{\circ}C$ for 90 min and were stable until 40 $^{\circ}C$ when allowed to stand for 1hr at various temperatures.

• Microbiology and Biotechnology Letters
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• v.20 no.2
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• pp.164-168
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• 1992

Enzymatic properties of avicelase, carboxymethyl cellulase (CMCase) and P-glucosidase produced by Cellulomonas sp. YE-5 were studied. Optimal temperature and pH of avicelase were 40t and 6.0, and those of CMCase and P-glucosidase were $45^{\circ}C$ and 6.5. Avicelase and CMCase were stable between pH 5.0 and 9.5, and &glucosidase was stable between pH 5.5 and 8.0. Avicelase and P-glucosidase were inactivated when incubated at $35^{\circ}C$ for 6 hrs, and CMCase was at $40^{\circ}C$ for 6 hrs. All cellulases were strongly inhibited by $Cu^{2+} \; and \; Zn^{2+}. K_m$ values of avicelase for avicel, CMCase I and CMCase II for CM-cellulose, and ($\beta$-glucosidase for p-nitrophenyl-$\beta$-D-glucoside (PNPG) were 4.76, 16.4, 16.4 $\mu g$/ml and 3.51 mM, respectively.

• 한국정보디스플레이학회:학술대회논문집
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• 2004.08a
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• pp.265-268
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• 2004

We have developed a highly efficient and stable blue organic electroluminescent device (OLED) based on the blue fluorescent p-bis(p-N,N-diphenyl-aminostyryl)benzene (DSA-Ph) dopant in a morphologically stable high-bandgap host material, 2-methyl-9,10-di(2-naphthyl)anthracene (MADN), which achieved an EL efficiency of 9.7 cd/A and 5.5 lm/W at 20 mA/$cm^2$ and 5.7 V with a Commission Internationale d'Eclairage coordinates of(x = 0.16, y = 0.32). This sky blue device which could also alleviate the problematic current induced quenching at high current achieved a half-decay lifetime ($t_{1\;2}$) of 46,000 h at an initial brightness of 100 cd/$m^2$.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.28 no.6
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• pp.728-735
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• 1995

The peptidyl prolyl cis-trans isomerase(PPlase, EC 5.2.2.8) from Bacillus stearothermophilus SIC1 was extracted from the cells treated with by lysozyme. PPlase was purified from the cell extracts by heat treatment, ammonium sulfate precipitation, ion exchange chromatography and finally gel filtration (FPLC). The purity of purified the enzyme after Superose 12 column chromatography was examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE). The molecular weight of the purified PPlase was estimated as 18,000 by SDS-PAGE. The 39 amino acid residues from the N-terminus were determined by the protein sequencer. The enzyme showed the optimum pH at 8.0 and was stable at the range of pH 7.0 to 8.0. The enzyme was considerably stable after heat treatment at $60^{\circ}C$ for 30 minutes, and the enzyme was quite stable up to $65^{\circ}C$. The presence of the PPlase in the refolding solution accelerated the isomerization rate of the assay peptide.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.6
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• pp.621-628
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• 1991

Heat-stable enterotoxin(ST) from enterotoxigenic E. coli eKT-53($ST^{+}\;LT^{-}$, transformant from isolate KM-7) that was produced in succinate salts medium. The culture supernatant(crude ST) was purifed by mulitpled steps and investigated some characterization of the ST. The heatstability of purified ST activity was completely lost by treating at $100^{\circ}C$ for 30minutes. ST activity was lost by treatment at pH 1 and 12 conditions, while the activity was not reduced by treatment at pH 2~10, and then the ${\alpha}-amylase$ and pepsin was not decreased activity but disulfide reducing agnets was lost the activity. The molecular weight of the purified ST was approximately 4,200, the isoelectric point was about 4.0.