• Journal of Sericultural and Entomological Science
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• v.33 no.1
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• pp.9-12
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• 1991

A study on dyeing-rate for single and mixture dyeing of silk with acid dyes was carried out. Single and mixture dyeings were performed with levelling and milling dyes at 7$0^{\circ}C$ and at pH 3, pH 4 and pH 5, respectively. The results of this study were summerized as follows : 1. C. I. Acid Orange 7. A) At pH 3, dyeing-rate was more fast in the single dyeing than in mixture dyeing at the beginning of dyeing process. B) At pH 4 and 5, dyeing-rates tend to get very similar in single and mixture dyeing. 2. C. I. Acid Blue 138 A) At all pH value, dyeing-rates were more fast in the mixture dyeing than single dyeing at the beginning of dyeing. B) As the time increased, the difference of dyeing-rate and adsorption amounts between single and mixture dyeing was not shown.

• Bulletin of the Korean Chemical Society
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• v.32 no.spc8
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• pp.3145-3148
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• 2011

• Bulletin of the Korean Chemical Society
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• v.31 no.4
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• pp.984-988
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• 2010

1-(Fluoren-2-yl)-benzo[d][1,2,3]triazoles 5a-b were synthesized starting from 2-nitrofluorene. 2-Nitrofluorenes 1a-b were reduced by catalytic hydrogenation, reacted with 2,4-dinitrofluorobenzene followed by catalytic hydrogenation to afford 2-(N-2,4-diaminophenyl)aminofluorenes 4a-b. Diazotization of 4a-b with $NaNO_2/H_2SO_4$ followed by treatment with $H_3PO_2$ gave 5a-b. Sulfonation of 5a-b yielded 7-benzotriazol-1-yl-fluorene-2-sulfonic acids 6a-b. The structures of 5b and 6b were firmly identified by X-ray crystal analysis in addition to $^1H$ NMR, $^{13}C$ NMR, and elemental analysis.

• Journal of Ginseng Research
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• v.27 no.3
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• pp.129-134
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• 2003

When ginsenoside $R_{*}$b1/ and $R_{b2}$ were anaerobically incubated with human fecal microflora, these ginsenosides were metabolized to compound K (IH-901). When ginsenoside $R_{g3}$ was anaerobically incubated with human fecal microflora, the ginsenoside $R_{g3}$ was metabolized it to ginsenoside $R_{h2}$. Among ginsenosides, IH-901 and 20(S)-ginsenoside $R_{h2}$ exhibited the most potent cyotoxicity against tumor cells: 50% cytotoxic concentrations of IH-901 in the media with and without fetal bovine serum (FBS) were 27.1-31.6 $\mu$M and 0.1-0.61 $\mu$M, and those of 20(S)-ginsenoside $R_{h2}$ were 37.5->50 and 0.7-7.1 $\mu$M, respectively. The cytotoxic potency of ginsenosides was IH-901>20(S)-ginsenoside R $h_{h2}$》20(S)-ginsenoside $R_{g3}$>ginsenoside $R_{b1}$(equation omitted) $R_{b2}$.EX>$R_{b2}$./.

• Bulletin of the Korean Chemical Society
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• v.16 no.10
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• pp.994-997
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• 1995

• Applied Chemistry for Engineering
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• v.30 no.4
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• pp.421-428
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• 2019

This paper describes a methode to extract yellow pigment from curcuma and turmeric containing natural color curcumin whose target color indexes of L, a, and b were 87.0 7.43, and 88.2, respectively. The pH range and extraction temperature used for the reaction surface analysis method were from pH 3 to pH 7 and between 40 and $70^{\circ}C$, respectively for both natural products. A central synthesis planning model combined with the method was used to obtain optimal extraction conditions to produce the color close to target. Results and regression equations show that the color space and difference of curcuma and turmeric have the greatest influence on the value. In the case of curcuma, the optimum conditions to satisfy all of the response theoretical values of color coordinates of L (74.67), a (5.69), and b (70.08) were at the pH and temperature of 3.43 and $54.8^{\circ}C$, respectively. The experimentally obtained L, a, and b, values under optimal conditions were 72.92, 5.32, and 72.17, respectively. For the case of turmeric, theoretical numerical color coordinates of L, a, and b, under the pH of 5.22 and temperature of $50.4^{\circ}C$ were 82.02, 7.43, and 72.86 respectively. Whereas, the experiment results were L (81.85), a (5.39), and b (71.58). Both cases showed an error range within 1%. Therefore, it is possible to obtain a low error rate when applying the central synthesis planning model to the reaction surface analysis method as an optimization process of the dye extraction of natural raw materials.

• Bulletin of the Korean Chemical Society
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• v.25 no.7
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• pp.1012-1019
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• 2004

The synthesis of novel group 9 metal complexes containing the S,S'-chelate ligands, $Li_2S_2C_2B_{10}H_{10}$ (2a) and $LiS(S=PMe_2)C_2B_{10}H_{10$} (2b), is described. Two new dinuclear complexes of the type $[{(cod)M}_2(S,S'-S_2C_2B_{10}H_{10})]$ (cod = 1,5-cyclooctadiene; M = Rh (3a), or Ir (3b)) were synthesized by the reaction of chloridebridged dimers $[M({\mu}-Cl)(cod)]_2$ with one molar equivalent of the corresponding dilithium dithiolato ligand $Li_2S_2C_2B_{10}H_{10}$ (2a). X-ray crystal structure analysis of 3a revealed a dinuclear structure in which each (cod)Rh unit is attached to a distinct sulfur atom of a 1,2-dithio-o-carboranyl ligand (2a). Additionally, the electrochemical properties of 3a and 3b were investigated by cyclic voltammetry. In an analogous manner, reaction of the lithium dithiolato ligand $LiS(S=PMe_2)C_2B_{10}H_{10}$ (2b) with $Cp^{\ast}CoI_2(CO)$ produced a mononuclear dithiolato complex, $[Cp^{\ast}CoI{(S,S'-S(S=PMe_2)C_2B_{10}H_{10})}]$ (4), which was characterized by single-crystal X-ray analysis.

• KSBB Journal
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• v.19 no.4
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• pp.250-256
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• 2004

In this work we have cultivated several B. cereus strains in a complex LB medium in order to study the production of phospholipase C (PLC), and among them B. cereus 318 showed the highest productivity of PLC. Some components, i.e., 5 g/L glucose, 5 g/L yeast extract, 5 g/L peptone, 0.5∼1.0 g/L K$_2$HPO$_4$, 0.02∼0.04 g/L ZnSO$_4$$.$7H$_2$O and 3 g/L NaHCO$_3$ were found to be optimal for the high production of PLC by B. cereus 318. Optimal culture temperature and pH were found to be 30$^{\circ}C$ and pH 7.5 for the PLC production, respectively. Optimum reaction temperature and pH of the PLC produced by B. cereus 11 and 318 were 45$^{\circ}C$ and pH 4.0, while they were 50$^{\circ}C$ and pH 7.0 for the PLC by B. cereus 559. The PLC produced by B. cereus was activated by Mn$\^$2+/, Co$\^$2+/ and dimethyl sulfoxide (DMSO), but its activity was inhibited by Cu$\^$2+/ and partially by glycerol, isopropanol and sodium dodecyl sulfate (SDS).

• Korean Journal of Crystallography
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• v.13 no.3_4
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• pp.152-157
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• 2002

The molecular and crystal structure of Tricyclazole, C/sub9/H/sub7/N₃S, has been determined by single crystal x-ray diffraction study. Crystallographic data for title compound: Pca2₁, a=14.889(1) Å, b=7.444(1) Å, c=15.189(2) Å, V=1683.3(3) ų, Z= 8. The molecular structure model was solved by direct methods and refined by full-matrix least-squares. The final reliable factor, R, is 0.047 for 1533 independent reflections (F/sub o//sup 2/)). The asymmetry unit contains two molecules which are in plate conformation, parallel to each other and related by a pseudo four-fold screw on the b-direction.

• Microbiology and Biotechnology Letters
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• v.30 no.1
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• pp.26-32
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• 2002

For commercial production of Korean fermented anchovy sauce through rapid fermentation, a bacterial strain which showed the high protease activity was isolated from a commercially fermented anchovy sauce. The isolate was Bacillus amyloliquefaciens, and named as B. amyloliquefaciens HTP-8. The incubation temperature, initial pH, and cultivation time for optimal production of protease by B. amyloliquefaciens HTP-8 were $30^{\circ}C$, 7.0, and 3 days, respectively. In jar fermenter, B. amyloliquefaciens HTP-8 showed higher protease activity when grown at pH 7.0. The protease was partially purified by 80% ammonium sulfate precipitation and CM-Sephadex C-50 ion exchange chromatography. The partially purified enzyme had specific activity of 103.3 units/mg, yield of 0.4%, and purification fold of 43.0. The optimal pH and temperature for the protease activity were 10.0 and $50^{\circ}C$, respectively. The protease was relatively stable at the pH range of 7.0~12.0 and at the temperatures below 4$0^{\circ}C$. The activity of the enzyme was inhibited by $Ag^{＋}$ /, $Ba^{2＋}$ and selectively inhibited by PMSF, suggesting that it is a serine protease.