• Food Science and Biotechnology
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• v.14 no.5
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• pp.651-655
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• 2005

Enzymatic hydrolysis of shark (Squatina oculata) cartilage (SC) was optimized by response surface methodology (RSM) for chondroitin sulfate (CS) preparation. Among 11 commercial proteases, Maxazyme NNP showed highest productivity (CS yield per enzyme cost) of CS. Optimal hydrolysis conditions determined by RSM were 1.63% and 2.87 hr for enzyme concentration and hydrolysis time ($r^2\;=\;0.9527$, p<0.0l), respectively and highest yield of hydrolysate under the conditions was 42.3%. The yield ($43.1{\pm}2.1%$) and CS content ($24.8{\pm}0.1%$) of hydrolysate at optimal condition verified statistical optimization of SC enzymatic hydrolysis was valid.

• Proceedings of the Korea Society of Poultry Science Conference
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• 2004.11a
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• pp.26-27
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• 2004

This study was conducted to evaluate the value of chicken keel cartilage as a source of mucopoly-saccharide-protein containing chondroitin sulfate (CS) and to find the optimum extraction conditions. The hot water extraction and alcalase hydrolysis methods were performed for extraction mucopolysaccharide in lyophilized chicken keel cartilage. The most efficient condition was hydrolysis with 2 % alcalase in 10 volumes of distilled water for 120 min. The yield of hydrolysate and CS content were 75.87 % and 25.61 %, respectively. For further separation of CS from hydrolysate by alcalase, ethanol precipitation was performed. The yield of ethanol precipitate and its CS content were 21.41 % and 46.31 %, respectively.

• Archives of Pharmacal Research
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• v.27 no.6
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• pp.662-669
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• 2004

The highly water-soluble monomethoxypoly(ethyleneglycol) (mPEG) prod rugs of cyciosporin A(CsA) were synthesized. These prod rugs were prepared by initially preparing intermediate in the form of carbonate at the 3'-positions of CsA with chloromethyl chloroformate, in the pres-ence of a base to provide a 3'-carbonated CsA intermediate. Reaction of the CsA intermediate with mPEG derivative in the presence of a base provides the desired water-soluble prod rugs. As a model, we chose molecular weight 5 kDa mPEG in the reaction with CsA to give water soluble prodrugs. To prove that the prod rug is decomposed in the body to produce CsA, the enzymatic hydrolysis test was conducted using human liver homogenate at $37^{\circ}C$. The prodrug was decomposed in human liver homogenate to produce the active material, CsA, and the hydrolysis half-life ($t_{1/2}$) of the prodrug, KI-306 was 2.2 minutes at $37^{\circ}C$. However, a demon-stration of non-enzymatic conversion in pH 7.4 phosphate buffer was provided by the fact that the half-life ($t_{1/2}$) is 21 hours at 37$^{\circ}C$. The hydrolysis test in rat whole blood was also conducted. The hydrolysis was seen with half-life ($t_{1/2}$) of about 9.9, 65.0, 14.2, 3.4, 2.1 9.5, and 1.6 minutes for KI-306, 309, 312, 313, 315, 316, and 317, respectively. This is the ideal for CsA prodrug. The pharmacokinetic study of the prodrug, KI-306, in comparison to the commer-cial product (Sandimmune Neoral Solution) was also carried out after single oral dose. Each rat received 7 mg／kg of CsA equivalent dose. Especially, the prodrug KI-306 exhibits higher AUC and $C_{max}$ than the conventional Neoral. The AUC and $C_{max}$ were increased nearly 1.5 fold. The kinetic value was also seen with $T_{max}$ of about 1.43 and 2.44 hours for KI-306 and Neoral, respectively.

• Analytical Science and Technology
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• v.5 no.4
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• pp.443-454
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• 1992

The analysis, hydrolysis mechanism, oxidation, reduction, thermal decomposition and metabolism of irritant materials such as chloroacetophenone isomers, bromophenylacetonitrile isomers, o-chlorobenzylidenemalononitrile(CS), and ethylisothiocyanate, etc. are interested in forensic science. We had studied hydrolysis of CS in 10% MeOH-$H_2O$ and 10% dioxane-$H_2O$ at pH 1.0~11.0 and various temperatures. As a result, we identified o-chlorobenzaldehyde and malononitrile that were formed by hydrolysis of CS by using gas chromatography/mass spectrometry, UV/Vis spectrometry, and polarographic method.

• The Plant Pathology Journal
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• v.40 no.3
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• pp.261-271
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• 2024

Sulfur is one of the inorganic elements used by plants to develop and produce phytoalexin to resist certain diseases. This study reported a method for preparing a material for plant disease resistance. Sulfur nanoparticles (SNPs) stabilized in the chitosan-Cu²⁺ (CS-Cu²⁺) complex were synthesized by hydrolysis of Na₂S₂O₃ in an acidic medium. The obtained SNPs/CS-Cu²⁺ complex consisting of 0.32% S, 4% CS, and 0.7% Cu (w/v), contained SNPs with an average size of ~28 nm as measured by transmission electron microscopy images. The X-ray diffraction pattern of the SNPs/CS-Cu²⁺ complex showed that SNPs had orthorhombic crystal structures. Interaction between SNPs and the CS-Cu²⁺ complex was also investigated by ultraviolet-visible. Results in vitro nematicidal effect of materials against Meloidogyne incognita showed that SNPs/CS-Cu²⁺ complex was more effective in killing second-stage juveniles (J2) nematodes and inhibiting egg hatching than that of CS and CS-Cu²⁺ complex. The values of LC₅₀ in killing J2 nematodes and EC₅₀ in inhibiting egg hatching of SNPs/CS-Cu²⁺ complex were 75 and 51 mg/l, respectively. These values were lower than those of CS and the CS-Cu²⁺ complex. The test results on the nematicidal effect against M. incognita on coffee pots showed that the SNPs/CS-Cu²⁺ complex was 100% effective at a concentration of 150 mg/l. Therefore, the SNPs/CS-Cu²⁺ complex could be considered as a biochemical material with potential for agricultural applications to control root-knot nematodes.

• Proceedings of the Korean Vacuum Society Conference
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• 2011.02a
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• pp.338-338
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• 2011

The behavior of hydroxide ions on water-ice films was studied by using $Cs^+$ reactive ion scattering (RIS), low energy sputtering (LES) and temperature-programmed desorption (TPD). A $Cs^+$ beam of a low kinetic energy (<100 eV) from $Cs^+$ ion gun was scattered at the film surface, and then $Cs^+$ projectiles pick up the neutral molecules on the surface as $Cs^+$-molecule clusters form (RIS process). In LES process, the preexisting ions on the surface are desorbed by the $Cs^+$ beam impact. The water-ice films made of a thick (>50 BL) $H_2$O layer and a thin $D_2O$ overlayer were controlled in temperatures 90~140K. We prepared hydroxide ions by using Na atoms which proceeded hydrolysis reaction either on the ice film surface or at the interface of the $H_2O$ and $D_2O$ layers.[1] The migration of hydroxide ions from the $H_2O/D_2O$ interface to the top of the film was examined as afunction of time. From this experiment, we show that hydroxide ions tend to reside at the water-ice surface. We also investigated the H/D exchange reactions of $H_2O$ and $D_2O$ molecules mediated by hydroxide ions to reveal the mechanism of migration of hydroxide to the ice surface.

• Journal of the Korean Chemical Society
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• v.24 no.1
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• pp.1-7
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• 1980

Solvolysis rate constants for methylchloroformate, methylthionochloroformate, methylthiolchloroformate and methyldithiochloroformate have been determined conductometrically in methanol, ethanol and ethanol-water mixtures and activation parameters have been derived. Results show that methylchloroformate solvolyzes through $S_N2$ process while methyldithiochloroformate solvolyzes by $S_N1$ process in all the solvent systems. The rate of hydrolysis decreased in the order, $CH_3S(CS)Cl>CH_3S(CO)Cl>CH_3O(CS)Cl>CH_3O(CO)Cl$ which corresponds to the order of decreasing $S_N1$ character. In methanol, $CH_3S(CS)Cl$ solvolyzed via the $S_N1$ mechanism while the others solvolyzed via the $S_N2$ process. In ethanol, however, $S_N2$ character was dominant for all the compounds, except methyldithiochloroformate, for which $S_N1$ character was still strong enough to accelerate the rate of ethanolysis. In ethanol-water mixtures, $CH_3S(CS)Cl$ and $CH_3S(CS)Cl$ solvolyzed via $S_N2$ process in ethanol-rich region while the $S_N1$ character increased greatly in water-rich region for the solvolysis of these compounds. The order of $S_N1$ character for solvolysis in water-rich region was the same as the order of hydrolysis rate.

• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 2003.09a
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• pp.293-297
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• 2003

A series of laboratory experiments was conducted to investigate the fixation characteristics of poly(vinylalcohol)-poly(methacrylic acid)(PVA-PMAA) mixed solution on the soluble (equation omitted)-radionuclides. Using the potentiometric titration technique, it was found out that the PVA and PMAA in a solution form intermacromolecular complex. The mobilized portion of each radionuclide by water from sand surface treated with a fixative was measured by ${\gamma}$-ray spectroscopy, The mobilized portion of minor radionuclides such as $^{241}$ Am, $^{154}$ Eu, $^{155}$ Eu and $^{144}$ Ce were higher than those of $^{134}$ Cs and $^{137}$ Cs. The capability of PVA-PMAA system was better among the candidate solutions for the fixation of total (equation omitted)-radioactivity, $^{134,137}$Cs which is composed of more than 85 % of total ${\gamma}$-radioactivity could be fixed effectively by the PVA-PMAA solution.

• Textile Coloration and Finishing
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• v.6 no.1
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• pp.33-43
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• 1994

In the present work, to clarify the mechanism of the neutral salt effect on the alkaline hydrolysis of PET, many salts with different cations like LiCl, NaCl, KCl, CsCl were added to the aqueous alkaline solutions. Then PET was hydrolyzed with aqueous solutions of many salts in alkali metal hydroxides under various conditions. Some conclusions obtained from the experimental results were summarized as follows. The reaction rate of the alkaline hydrolysis of PET was increased by the addition of neutral salts and In k was increased nearly linearly with the square root of ionic strength of reaction medium. This fact suggested that the ionic strength effect by Debye-Huckel and Bronsted theory was exerted on the reaction. The specific salt effect was also observed. The reaction rate was increased with the increase in the electrophilicity of cations of neutral salts, i. e., in the order of $Cs^+$/ < $K^+$/ $a^+$/ $i^$^+$. It was considered that the reaction rate was increased in the order of C $s^+$. < $K^+$. $a^+$. $i^+$. because the lowering effect of the cations on the negative charge of PET surface was increased with the electrophilicity of cations. It was thought that $E_{a}$ was increased because the cations of neutral salts decreased the negative charge of PET surface. It, however, was inferred from the increase in ${\Delta}$S＊ and the decrease in the ${\Delta}$G＊ that the cations of neutral salts associated with PET increased the collision frequency between carbonyl carbon and OH- ion and then accelerated the reaction rate.te.

• Journal of Microbiology and Biotechnology
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• v.17 no.8
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• pp.1291-1299
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• 2007

Two ${\beta}$-1,4-glucanases (DI and DIII fractions) were purified to homogeneity from the culture filtrate of a cellulolytic bacteria, Cellulomonas sp. CS 1-1, which was classified as a novel species belonging to Cellulomonas uda based on chemotaxanomic and phylogenetic analyses. The molecular mass was estimated as 50,000 Da and 52,000 Da for DI and DIII, respectively. Moreover, DIII was identified as a glycoprotein with a pI of 3.8, and DI was identified as a non-glycoprotein with a pI of 5.3. When comparing the ratio of the CMC-saccharifying activity and CMC-liquefying activity, DI exhibited a steep slope, characteristic of an endoglucanase, whereas DIII exhibited a low slope, characteristic of an exoglucanase. The substrate specificity of the purified enzymes revealed that DI efficiently hydrolyzed CMC as well as xylan, whereas DIII exhibited a high activity on microcrystalline celluloses, such as Sigmacells. A comparison of the hydrolysis patterns for pNP-glucosides (DP 2-5) using an HPLC analysis demonstrated that the halosidic bond 3 from the nonreducing end was the preferential cleavage site for DI, whereas bond 2, from which the cellobiose unit is split off, was the preferential cleavage site for DIII. The partial N-terminal amino acid sequences for the purified enzymes were $^1Ala-Gly-Ser-Thr-Leu-Gln-Ala-Ala-Ala-Ser-Glu-Ser-Gly-Arg-Tyr^{15}$-for DI and $^1Ala-Asp-Ser-Asp-Phe-Asn-Leu-Tyr-Val-Ala-Glu-Asn-Ala-Met-Lys^{15}$-for DIII. The apparent sequences exhibited high sequence similarities with other bacterial ${\beta}$-1,4-glucanases as well as ${\beta}$-1,4-xylanases.