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학술저널
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한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제19권 제7호
발행연도
2009.1
수록면
713 - 717 (5page)

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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. Similarly to the previously reported results for [BMIM][BF4], as the concentration of [BMPy][BF4] increased, the Km value increased with a decrease in the kcat value: the Km value increased markedly from 2.8 mM in 100% water to 12.6 mM in 25% (v/v) ionic liquid, indicating that ionic liquid significantly weakens the binding affinity of guaiacol to the enzyme. On the contrary, [BMIM][MeSO4] decreased the Km value to 1.4 mM in 25% (v/v) ionic liquid. [BMIM][MeSO4] also decreased kcat more than 3- folds [from 13.8 s-1 in 100% water to 4.1 s-1 in 25% (v/v) ionic liquid]. These results indicate that the ionic liquids interact with the enzyme at the molecular level as well as at a macroscopic thermodynamic scale. Specifically, the anionic component of the ionic liquids influenced the catalysis of horseradish peroxidase in different ways.

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