Oxidation of dibenzothiophene catalyzed by heme-containing enzymes encapsulated in sol-gel glass |
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Authors: | Shuguang Wu Jian Lin Sunney I Chan |
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Institution: | (1) Arthur Amos Noyes Laboratory of Chemical Physics 127-72, California Institute of Technology, 91125 Pasadena, CA |
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Abstract: | We have encapsulated several hemoproteins in the sol-gel glass to catalyze the oxidation reaction of dibenzothiophene (model
for organic sulfur compounds in coal) with hydrogen peroxide. In addition to cytochrome c and myoglobin, which have previously
been encapsulated in sol-gel glasses, two other hemoproteins, horseradish peroxidase and bovine blood hemoglobin, have now
been successfully immobilized in sol-gel media with the retention of their spectroscopic properties. All four hemoproteins
studied also demonstrate similar catalytic activities toward the oxidation of dibenzothiophene as compared with the results
obtained with the proteins in solution. In the case of encapsulated cytochrome c, the more water-soluble S-oxide was obtained
with much higher selectivity over the less water-soluble sulfone (S-oxide/sulfone = 7.1) as compared to what was obtained
in the aqueous/organic medium (S-oxide/sulfone = 2.3). Because of the advantage of easy separation of the encapsulated proteins
from the liquid reaction mixture, it is clear from these studies that the immobilization of active hemoproteins in the solid
glass media could serve as more practical biocatalysts. |
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Keywords: | Dibenzothiophene biooxidation biocatalyst encapsulation sol-gel glass hemoglobin cytochrome c horseradish peroxidase myoglobin |
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