• Bulletin of the Korean Chemical Society
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• v.1 no.3
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• pp.78-82
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• 1980

Solutions of $Cd^{2+}$, $Co^{2+}$ and $Ni^{2+}$ were mixed with the solutions of hydroxycarboxylic acids such as salicylic, lactic and mandelic acids in the presence of cation exchange resin at room temperature. The distribution ratios of the metal ions between resin and solution were measured, using radioactive metal ions as tracer. From the observed variation of the distribution ratios with the acid anion concentrations, it was concluded that $Cd^{2+}$, $Co^{2+}$ and $Ni^{2+}$ formed the one-to-one complexes with salicylate, lactate and mandelate ions in aqueous, 20 % ethanol-water and 20 % acetone-water solutions. The results of the present study indicated that the relative stabilities of the metal-acid complexes in solution increased in the order: $Cd^{2+}$ <$Co^{2+}$ <$Ni^{2+}$ complexes. Salicylate

• Bulletin of the Korean Chemical Society
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• v.14 no.6
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• pp.692-696
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• 1993

Prediction of retention times in transition metal-mandelate and transition metal-tartrate complex systems were studied on the cation exchanger. Plots of k' vs [mandelate] and k' vs [tartrate] were obtained under the condition of a constant competing cation concentration. The equation to predict the retention time of transition metal ion was derived from the ion exchange equilibria. Individual capacity factors (${k_1}',\;{k_2}'$) and stability constants ($K_1,\;K_2$) of the complexes were calculated from the non-linear least square method. Good resolution of the transition metals was predicted by the stepwise equation in the gradient method. The values of retention times from the calculation and the experiment agreed well each other.

• Bulletin of the Korean Chemical Society
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• v.12 no.6
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• pp.629-632
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• 1991

The rate constants for the formation and dissociation of nickel(II) and cobalt(II) complexes with mandelate have been determined by the pressure-jump relaxation study. The forward and reverse rate constants for the mandelate complex formation reactions were obtained to be $k_f=3.60{\times}10^4\;M^{-1}s^{-1}$ and $k_r=1.73{\times}10^2\;s^{-1}$ for the nickel(II), and $k_f=1.75{\times}10^5\;M^{-1}s{-1}$ and $2.33{\times}10^3\;s^{-1}$ for the cobalt(II) in aqueous solution of zero ionic strength ($(\mu{\to}0)\;at\;25^{\circ}C$. The results were interpreted by the use of the multistep complex formation mechanism. The rate constants evaluated for each individual steps in the multistep mechanism draw a conclusion that the rate of the reaction would be controlled by the chelate ring closure step in concert with the solvent exchange step in the nickel(II) complexation, while solely by the chelate ring closure step for the cobalt(II) complex.

• Bulletin of the Korean Chemical Society
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• v.25 no.5
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• pp.599-600
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• 2004

• Bulletin of the Korean Chemical Society
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• v.12 no.3
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• pp.352-354
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• 1991

• Journal of Microbiology and Biotechnology
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• v.30 no.2
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• pp.244-247
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• 2020

We have expressed extracellular poly(3-hydroxybutyrate) (PHB) depolymerase of Ralstonia pickettii T1 on the Escherichia coli surface using Pseudomonas OprF protein as a fusion partner by C-terminal deletion-fusion strategy. Surface display of depolymerase was confirmed by flow cytometry, immunofluorescence microscopy and whole cell hydrolase activity. For the application, depolymerase was used as an immobilized catalyst of enantioselective hydrolysis reaction for the first time. After 48 h, (R)-methyl mandelate was completely hydrolyzed, and (S)-mandelic acid was produced with over 99% enantiomeric excess. Our findings suggest that surface displayed depolymerase on E. coli can be used as an enantioselective biocatalyst.

• Journal of Pharmaceutical Investigation
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• v.40 no.1
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• pp.15-21
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• 2010

Sibutramine is an orally administered centrally-acting antiobesity agent and inhibits both noradrenaline(norephinephirine) and serotonin(5-HT) reuptake. These effects are contributed by its active metabolites, M1 and M2. However, as the free base form of sibutramine is an oil form in room temperature, it had the problem of handling and stability. Thus, this drug should be used in the form of acid salt form in the pharmaceutical application. Unfortunately, anhydrous sibutramine hydrochloride is highly hygroscopic and unstable. In order to solve the hygroscopicity of the anhydrous salt form, another sibutramine acid salt form must be developed as a hydrate form. In this study. to overcome these problems, various of sibutramine acid salt forms were prepared with the pharmaceutically available salts such as maleate, esylate, mandelate, camsylate, besylate, salicylate, tartrate, isethionate and malate forms, and their physicochemical properties were investigated. Sibutramine malate was selected for excellent solubility and stability among the listed salt forms above. Its pharmacokinetic parameters were evaluated in rats comparing with sibutramine HCl, resulting in similar parameters. In vitro dissolution study of sibutramine malate-loaded capsule was performed comparison with commercial product ($Reductil^{(R)}$) in pH 1.2, pH 4.0, pH 6.8 and water medium. Our results indicated that there were no significant differences in their dissolution profiles were similar in all tested medium. Thus, sibutramine malate-loaded capsule should be a potential candiate due to its excellent solubility, good stability and biosimilar absorption.

• KSBB Journal
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• v.14 no.3
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• pp.264-272
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• 1999

Benzoylformate was converted to benzaldehyde by whole cell enzyme from Pseudomonas putida KCTC 1751. We investigated the effect of the composition of the growth medium on th accumulation of benzoylformate decarboxylase in the microbial cell. We prepared a calcium alginate capsule containing Pseudomonas putida cells to develop a reusable whole cell enzyme. Pseudomonas putida cells were inoculated in the capsule and cultured in M1 medium for 1 day followed by cultivation in M3 medium for 3 days. The dry cell density reached 77.75 g/L on the basis of the inner volume of the capsule. The specific activity of encapsulated whole cell benzoylformate decarboxylase was half as high as that of free whole cell enzyme. The activity of encapsulated whole cell benzoylformate decarboxylase was half as high as that of free whole cell enzyme. The activity of encapsulated whole cell benzoylformate decarboxylase decreased 20 % after use for 20 batches and 40% after use for 30 batches. The dry cell density reduced about 10 % after 30 trials.