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Investigation Of How Hydrogen Bonding Affects The Enantiomeric Excess Of Pig Liver Esterase Promoted Hydrolysis Of Pro-Chiral Substrates, Jacob E. Pruett
Investigation Of How Hydrogen Bonding Affects The Enantiomeric Excess Of Pig Liver Esterase Promoted Hydrolysis Of Pro-Chiral Substrates, Jacob E. Pruett
Honors Theses
Pig Liver Esterase is a cost effective enzyme for ester hydrolysis. In our group, it is vital for creating chiral molecules for the synthesis of unnatural amino acids of potential biological importance. It has been previously found that the enantiomeric excess (%ee) of the PLE hydrolysis reaction increases drastically with the addition of co-solvents that are able to both accept and donate hydrogen bonds. This research endeavors to see if substrates of enhanced hydrogen bonding ability also increase the stereoselectivity of PLE hydrolyses. Diester malonate was covalently linked with a furan ring in both the third and second position from …