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Applications of micellar enzymology to clean coal technology [electronic resource].

Published
Washington, D.C. : United States. Dept. of Energy, 1993.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy.
Physical Description
Pages: (6 pages) : digital, PDF file
Additional Creators
United States. Department of Energy. Office of Management, United States. Department of Energy, and United States. Department of Energy. Office of Scientific and Technical Information
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Summary
The sequential addition of enzyme and H[sub 2]O[sub 2] during the reverse micelle incubation was found to enhance sulfoxidation, but levels of EPSn remained low. The triplicate addition of enzyme and H[sub 2]0[sub 2] during the reverse micelle incubation of EPS was found to enhance sulfoxidation to EPSn and unidentified material. Low conversion to EPSn was not due to the inability of the enzyme to oxidize EPSX in reverse micelles, since the latter was demonstrated with both commercially available and enzymatically synthesized EPSx as starting material. Chloroperoxidase in an AOT-isooctane reverse micelle solution also mediated production of a metabolite from DBT with characteristics consistent with DBTSx. The magnitude of conversion was enhanced to 10% of the starting material by triplicate addition of enyme and H[sub 2]0[sub 2]. The identity of this metabolite as DBTSx was verified by GC/MS. Chloroperoxidase in reverse micelles appears therefore to be a versatile catalyst for sulfoxidation of aliphatic and aromatic sulfur-containing model coal compounds.
Report Numbers
E 1.99:doe/pc/89772-t14
doe/pc/89772-t14
Subject(s)
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Note
Published through SciTech Connect.
03/10/1993.
"doe/pc/89772-t14"
"DE93011541"
Walsh, C.T.
Funding Information
FG22-89PC89772
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