Publications by authors named "Keungarp Ryu"

The interactive inhibitory effects of pH and chloride on the catalysis of laccase from Trametes versicolor were investigated by studying the alteration of inhibition characteristics of sodium chloride at different pHs for the oxidation of 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid). At pH 3.0, the addition of sodium chloride (50 mM) brought about a 40-fold increase in Km(app) and a 4-fold decrease in Vmax(app).

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The ionic liquid, 1-butyl-3-methylimidazolium methylsulfate ([BMIM][MeSO(4)]), was used to investigate the catalytic mechanism of horseradish peroxidase (HRP). The ionic liquid decreased both K(m) and k(cat) values for the HRP-catalyzed oxidation of guaiacol (2-methoxyphenol) by H(2)O(2). These studies imply that [BMIM][MeSO(4)] inhibits the enzyme in an uncompetitive manner.

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The dependence of the catalytic properties of horseradish peroxidase on the structural changes of ionic liquids was investigated with two water-miscible ionic liquids, N-butyl-3- methypyridinium tetrafluoroborate ([BMPy][BF4]) and 1-butyl- 3-methylimidazolium methylsulfate ([BMIM][MeSO4]), each of which shares an anion (BF4 -) or a cation (BMIM+) with 1-butyl- 3-methylimidazolium tetrafluoroborate ([BMIM][BF4]), respectively. The oxidation of guaiacol (2-methoxyphenol) with H2O2 was used as a model reaction. In order to minimize the effect of solution viscosity on the kinetic constants of the enzymatic catalysis, the enzymatic reactions for the kinetic study were performed in water-ionic liquid mixtures containing 25% (v/v) ionic liquid at maximum.

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The effect of pH on anaerobic hydrogen production was investigated under various pH conditions ranging from pH 3 to 10. When the modified Gompertz equation was applied to the statistical analysis of the experimental data, the hydrogen production potential and specific hydrogen production rate at pH 5 were 1,182 ml and 112.5 ml/g biomass-h, respectively.

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The effect of a water-miscible ionic liquid, 1-butyl-3-methylimidazolium tetrafluoroborate ([BMIM][BF4]), on the horseradish peroxidase (HRP)-catalyzed oxidation of 2-methoxyphenol (guaiacol) with hydrogen peroxide (H2O2) was investigated. HRP maintains its high activity in the aqueous mixtures containing various concentrations of the ionic liquid and even in 90% (v/v) ionic liquid. In order to minimize the effect of solution viscosity on the kinetic constants of HRP catalysis, the enzymatic reactions in the subsequent kinetic study were performed in water-ionic liquid mixtures containing 25% (v/v) ionic liquid at maximum.

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The effects of a water-miscible ionic liquid, 1-butyl-3-methylimidazolium tetrafluoroborate ([BMIM][BF(4)]), on both thermodynamics and kinetic mechanism of the horseradish peroxidase (HRP)-catalyzed oxidation of guaiacol (2-methoxyphenol) by H(2)O(2) were investigated. The ionic liquid stabilized the ground state of guaiacol by causing an 8-fold increase of K(m) from 3 to 23 mM upon the addition of 25% (v/v) [BMIM][BF(4)]. In addition, the effect of [BMIM][BF(4)] in decreasing the k(cat) value of HRP catalysis was described by a non-competitive inhibition mechanism.

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Horseradish peroxidase (HRP) was immobilized on carboxylated multi-wall carbon nanotubes in the presence of a coupling reagent, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide. The immobilized HRP maintained its oxidative activity for guaiacol over a broad range of pH values (4-9). An electrode of graphite rod, 6 mm diam.

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