|
Poster Presentation 6-31
Enzyme Specificity during C-S Bond Cleavage in Biodesulfurization of Petroleum Feedstocks
Abhijeet P. Borole1 and Choo Y. Hamilton2
1Life Sciences Division, Oak Ridge National Laboratory 1 Bethel Valley Road, P O Box 2008, Oak Ridge TN 37831-6226
2The University of Tennessee, Joint Institute for the Energy and the Environment
Telephone: (865) 576-7421; Fax: (865) 574-6442; E-mail: borolea@ornl.gov
Biodesulfurization offers a potential alternative for reducing sulfur levels in diesel to below 30 ppm. Some of the bottlenecks in commercializing the process include low enzyme activity, narrow specificity, and complexities in post-reaction oil-water separation. Here, we address the specificity of the enzymes to determine the capability of existing biocatalysts for diesel desulfurization. Secondly, the role of host organism on sulfur removal will also be studied by using different organisms hosting the same enzymes. Various model compounds were chosen from the previously known recalcitrant class of organosulfur compounds. Studies were conducted with three different hosts, Rhodococcus, Pseudomonas, and E. coli hosting the dsz genes to desulfurize model compounds as well as actual feedstocks. Specific rates for conversion of model compounds as well as chromatograms showing transformation to desulfurized products will be presented.
|