Applications of micellar enzymology to clean coal technology

Technical Report · Wed Mar 10 00:00:00 EST 1993

DOI:https://doi.org/10.2172/6704298· OSTI ID:6704298

Walsh, C T

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.

• Research Organization: Boston Univ., MA (United States). School of Medicine
• Sponsoring Organization: USDOE; USDOE, Washington, DC (United States)
• DOE Contract Number: FG22-89PC89772
• OSTI ID: 6704298
• Report Number(s): DOE/PC/89772-T14; ON: DE93011541
• Country of Publication: United States
• Language: English

Related Subjects

01 COAL, LIGNITE, AND PEAT
59 BASIC BIOLOGICAL SCIENCES
COAL PREPARATION
BIODEGRADATION
ORGANIC SULFUR COMPOUNDS
CATALYTIC EFFECTS
ENZYMES
HYDROGEN PEROXIDE
INCUBATION
OXIDATION
PROGRESS REPORT
CHEMICAL REACTIONS
DECOMPOSITION
DOCUMENT TYPES
HYDROGEN COMPOUNDS
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
PEROXIDES
PROTEINS
010300* - Coal
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550700 - Microbiology