• Journal of the Korean Chemical Society
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• v.20 no.1
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• pp.48-55
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• 1976

The rate constants of the derivatives of N-(2,4-dinitrophenyl)-benzimidoyl chloride were determined at various pH and a rate equation which can be applied over wide pH range was obtained. The reaction mechanism of hydrolysis of N-(2,4-dinitrophenyl)-benzimidoyl chloride which has not been studied carefully earlier in acidic and basic solution can be fullly explained by the rate equation obtained. The rate equation reveals that, beow pH 7.00, the hydrolysis of benzimidoyl chloride proceeds through $S_N2$ reaction to form a carbonium ion intermediate.Above pH 8.5, however, the hydrolysis proceeds through the $S_N2$ type reaction which depends on hydroxide ion and imidoyl chloride concentration. At pH 7.0∼8.5, two reactions occur competitively.

• Journal of the Korean Chemical Society
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• v.28 no.5
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• pp.328-334
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• 1984

A series of phenyl N-benzenesulfonylchloroformimidate derivatives (p-H, p-Cl, p-CH3 & p-OCH3) were prepared and the hydrolysis of these compounds were studied kinetically at various pH by UV spectrophotometry in 1 ; 4 dioxane-water at $25^{\circ}C$. Hammett ${\rho}$ values measured at pH 5.0 (${\rho}$ = -0.45) and pH 10.0 (${\rho}$ = 0.40) indicate that the reaction proceeds via an azocarbonium ion intermediate in the acidic medium, whereas, it involves direct attack by hydroxide ion on the azomethine carbon atom occurs under the basic medium. The formation of stabilized azocarbonium ion species at pH 5.0 is also consistent with the large solvent effect(m = 1.3-1.5 & n = 5.0-5.5). On the basis of these findings, we may concluded that the hydrolysis of phenyl N-benzenesulfonylchloroformimidate derivatives proceeds by $SN_1$ below pH 8.0, however, above pH 10.0, the hydrolysis proceeds through $SN_2$ and in the range of pH 8.0-10.0, these two reactions occur competitively.

• Microbiology and Biotechnology Letters
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• v.25 no.2
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• pp.109-114
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• 1997

The Oomycete Saprolegnia ferax produces an extracellular $\beta$-amylase, Maximum enzyme yield was attained after 7 days of growth in YNB starch medium (pH 6.5) at 25$\circ$C. The amylase was pu- rified 24-fold by ultrafitration, HPLC DEAE column and HPLC gel filtration. The purfied enzyme was a monomeric glycoprotein with a molecular weight of about 44,000 dalton. The pH and temperature optima were 6.5 and 50$\circ$C, respectively. The enzyme was fairly stable up to 50$\circ$C and at acidic pH region (pH 4.0-7.0). The apparent Km and Vmax values of the enzyme against soluble starch were 0.77 mg/ml and 2,174 $\mu$moles/mg protein, respectively. Amino acid analysis indicated that the enzyme was enriched in alanine, glycine, leucine and acidic amino acid. Starch hydrolysis with the enzyme released maltose but not glucose, whereas maltotriose, Schardinger dextrin ($\alpha$-cyclodextrin) and pullulan were not hydrolysed by the enzyme. The enzyme was inhibited by Schardinger dextrin, p-chloromercuribenzoate(PCMB), CU$^{2+}$' and Hg$^{2+}$. Inhibition of the enzyme by PCMB could be reversed by the addition of cysteine and mercaptoethanol.

• Preventive Nutrition and Food Science
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• v.13 no.4
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• pp.354-361
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• 2008

A novel bacterium isolated from Cheonggukjang was identified as a glutamate-dependent Bacillus subtilis HA with 98.3% similarity to Bacillus subtilis Z99104. Optimization of poly-$\gamma$-glutamic acid ($\gamma$-PGA) production by modulating fermentation factors including carbon sources, nitrogen sources, inorganic salts and fermentation time was investigated. Optimum culture broth for $\gamma$-PGA production consisted of 3% glutamate, 3% glucose and various salts, resulting in the PGA production of 22.5 g/L by shaking culture for 72 hr at $37^{\circ}C$. Average molecular weight of $\gamma$-PGA was determined to be 1,220 kDa through MALLS analysis. The $\gamma$-PGA solution showed a typical pseudoplastic flow behavior, and a great decrease in consistency below pH 6.0 regardless of the same molecular weight of $\gamma$-PGA. The molecular weights of isolated $\gamma$-PGA were drastically decreased by heat treatment in various acidic conditions, resulting in different hydrolysis of $\gamma$-PGA. The consistency of $\gamma$-PGA solution was greatly decreased with increase heating time in acidic conditions.

• Journal of the Korean Society of Tobacco Science
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• v.7 no.1
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• pp.85-92
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• 1985

Extraction efficienties of volatile organic acids in tobacco leaves according to several extraction methods were investigated and contents of volatile organic acids in 16 kinds of tobacco leaf varieties were compared. Extraction efficiency according to simultaneous distillation and extraction was 5 to 10 times higher than that according to solvent extraction, steam distillation, essential oil extraction or continuous extraction and distillation. Total contents of volatile organic acids were 1.62 to 12.94mg per l00g of sample in aromatic tobacco varieties,0.12 to 2.08mg in flue-cured tobacco leaves, and trace in burleys. Among the Korean aromatic tobacco varieties, total contents of volatile organic acids in ST374-3 were the highest, 4.66mg per l00g of sample, and those in Sohyang and Hyangcho were low, 1.69mg and 1.62mg, respectively. Among flue-cured tobacco varieties, those in NC2326 were the highest, 2.08mg per 100g of sample, but those in the other varieties were not more than 0.80mg per 1 00g of sample. Total contents of volatile organic acids in acidic hydrolysis with 0.1 M tartaric acid were higher than in non-acidic condition in all kinds of tobacco varieties.

• Polymer(Korea)
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• v.26 no.4
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• pp.492-500
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• 2002

Oxidized-polyacrylonitrile (oxy-PAN) was prepared by oxidation of PAN fiber at $240^{\circ}C$, followed by base catalyzed hydrolysis reaction. The chemical structure of PAN fiber in various pH conditions was characterized by $^{13}C-NMR$ spectroscopy. The characteristic contraction and expansion behavior of oxy -PAN fiber was observed in acidic and basic medium, respectively. In basic condition, water molecules might be absorbed into the fiber with the movement of charge balancing $Na^+$ ion, on the other hand, the water molecules seemed to be expelled in acidic condition to result in contraction. It was also observed that the facile chemical modification occurred due to free diffusion of aqueous reagent into the hydrophilic PAN fiber, and the morphology was affected by pH condition.

• Journal of Ginseng Research
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• v.38 no.4
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• pp.264-269
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• 2014

Background: In this study, we examined the effects of various enzymes on chemical conversions of ginsenosides in ginseng extract prepared by amylases. Methods: Rapidase, Econase CE, Viscozyme, Ultraflo L, and Cytolase PCL5 were used for secondary enzymatic hydrolysis after amylase treatment of ginseng extract, and ginsenoside contents, skin permeability, and chemical compositions including total sugar, acidic polysaccharide, and polyphenols were determined on the hydrolyzed ginseng extract. Results: Rapidase treatment significantly elevated total ginsenoside contents compared with the control (p < 0.05). In particular, deglycosylated ginsenosides including Rg3, which are known as bioactive compounds, were significantly increased after Rapidase treatment (p < 0.05). The Rapidase-treated group also increased the skin permeability of polyphenols compared with the control, showing the highest level of total sugar content among the enzyme treatment groups. Conclusion: This result showed that Rapidase induced the conversion of ginsenoside glycosides to aglycones. Meanwhile, Cytolase PCL5 and Econase treatments led to a significant increase of uronic acid (acidic polysaccharide) level. Taken together, our data showed that the treatments of enzymes including Rapidase are useful for the conversion and increase of ginsenosides in ginseng extracts or products.

• KSBB Journal
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• v.14 no.2
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• pp.220-224
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• 1999

Lactic acid was reacted with alcohol into lactate ester, and lactate ester produced in esterification reaction was distilled simultaneously with hydrolysis reaction into lactic acid. When the yields of lactic acid recovered by batch reactive distillations with various alcohols were compared, the yield of lactic acid was increased as the volatility of lactate ester was increased. In this batch reactive distillation, because the mixtures condensed in partial condensor were flown to reboiler through distillation column, the recovery yield of lactic acid was affected by operation temperature of partial condensor. Hydrolysis reaction into lactic acid in distillation column rarelyoccurred because of short retention time of lactate ester and water. Lactate ester was reacted into lactic acid in reboiler.

• Korean Journal of Weed Science
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• v.17 no.2
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• pp.135-138
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• 1997

Sulfonylureas are highly active herbicides which can be applied at very low rate(10-50g/ha) to control broadleaf weeds. The nature of this category of compound is, however, very unstable toward hydrolysis. Therefore, the preparation of these compounds as liquid formulation was not possible. Most of the current formulations of sulfonylurea are in dry forms such as water dispersible granule or wettable powder. Even in these dry forms, the active ingredients also encounter significant chemical decomposition. This study involves the preparation of the sulfonylurea salts by reacting the parent compound with base such as sodium hydroxide. The salt becomes stable toward hydrolysis and it turns soluble when diluted with water. This discovery makes the preparation for liquid formulation or soluble granule of sulfonylurea possible. The stoichiometry of base added to the neutral sulfonylurea is controlled quite precisely. The base has to be added enough to quench the acidic impurities in the technical material and to convert the active ingredient into salt. However, the base should not be overused to cause further saponification of the sulfonylurea salts. The chemical nature of these compounds is presented and the chemical reaction is described. New soluble liquid formulation and solid granule formulation of sulfonylurea are suggested.

• Journal of Microbiology and Biotechnology
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• v.20 no.2
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• pp.332-339
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• 2010

The lipase from Mucor racemosus NRRL 3631 was partially purified by fractional precipitation using 60% ammonium sulfate, which resulted in a 8.33-fold purification. The partially purified lipase was then immobilized using different immobilization techniques: physical adsorption, ionic binding, and entrapment. Entrapment in a 4% agar proved to be the most suitable technique (82% yield), as the immobilized lipase was more stable at acidic and alkaline pHs than the free enzyme, plus 100% of the original activity was retained owing to the thermal stability of the immobilized enzyme after heat treatment for 60 min at $45^{\circ}C$. The calculated half-lives (472.5, 433.12, and 268.5 min at 50, 55, and $60^{\circ}C$, respectively) and the activation energy (9.85 kcal/mol) for the immobilized enzyme were higher than those for the free enzyme. Under the selected conditions, the immobilized enzyme had a higher $K_m$ (11.11 mM) and lower $V_{max}$ (105.26 U/mg protein) when compared with the free enzyme (8.33 mM and 125.0 U/mg protein, respectively). The operational stability of the biocatalyst was tested for both the hydrolysis of triglycerides and esterification of fatty acids with glycerol. After 4 cycles, the immobilized lipase retained approximately 50% and 80% of its original activity in the hydrolysis and esterification reactions, respectively.