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Full-Text Articles in Physical Sciences and Mathematics
Enzyme, Cosolvent, And Substrate Interactions In Ple Hydrolysis Reactions And Evaluation Of The Stability Of An Unnatural Glutathione Analogue, Maureen Elizabeth Smith
Enzyme, Cosolvent, And Substrate Interactions In Ple Hydrolysis Reactions And Evaluation Of The Stability Of An Unnatural Glutathione Analogue, Maureen Elizabeth Smith
Dissertations
Prochiral diester malonates have been hydrolyzed in the presence of Pig Liver Esterase (PLE). Several of the diesters produced the respective half-ester in moderate to high enantioselectivity. A series of cosolvent assays were performed to evaluate the ability of the cosolvent to influence the enantioselective outcome of the hydrolysis reactions. Ethanol produced the largest changes in enantioselectivity of all solvents evaluated. The isoenzymes of PLE were also evaluated and provided very different enantioselective outcomes than that of crude PLE. A series of NMR titrations was performed to explore the interactions between the substrates and ethanol cosolvents.
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