Peroxidase oxidations of hydroquinone and p-cresol in AOT reversed micelles |
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Authors: | H Noritomi K Iwamoto M Seno |
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Institution: | (1) Institute of Industrial Science, The University of Tokyo, Roppongi, Minato-ku, Tokyo, Japan;(2) Present address: Institute of Materials Science, University of Tsukuba, Tsukuba, Ibaraki, Japan |
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Abstract: | The enzymatic activities of horseradish peroxidase solubilized in reversed micelles of bis(2-ethylhexyl)sodium sulfosuccinate formed in octane at various
o values (
o=H2O]/AOT]) were investigated by studying the catalytic oxidation of hydroquinone and p-cresol. These enzymatic reactions obeyed Michaelis-Menten kinetics. The turnover number of the enzymatic reaction of hydroquinone solubilized in the water pool increased with a decrease in
o value. On the other hand, the dependence of the turnover number of the enzymatic reaction of p-cresol solubilized in octane on the
o value was similar to that in the case of hydroquinone, although even at higher
o values the turnover number was smaller than that in water. Furthermore, it was suggested by spectrophotometric and circular dichroism measurements that the conformational change of enzyme induced the change in enzymatic activity. |
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Keywords: | Reversed micelle horseradishperoxidase andoxidation |
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