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An Investigation of the Interaction of Co‐Solvent with Substrates in the Pig Liver Esterase‐Catalyzed Hydrolysis of Malonate Esters
Author(s) -
Smith Maureen E.,
Fibinger Michael P. C.,
Bornscheuer Uwe T.,
Masterson Douglas S.
Publication year - 2015
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201500597
Subject(s) - chemistry , hydrolysis , hydrogen bond , substrate (aquarium) , esterase , malonate , catalysis , solvent , enantioselective synthesis , ethanol , pig liver , molecule , solvent effects , organic chemistry , enzyme , oceanography , geology
Previously, we have reported the effect of several co‐solvents, including ethanol, on the enantioselective outcome of pig liver esterase (PLE) hydrolysis reactions. The greatest improvements were observed in those substrates that contained an atom capable of forming a hydrogen bond in the sidechain portion of the molecule. To further explore the interaction between substrate and ethanol, a second series of substrates were synthesized, in which the hydrogen bonding atoms of the side chain were modified, and subjected to PLE hydrolysis. Substrates containing atoms capable of forming hydrogen bonds showed the largest equilibrium constants. However, a large equilibrium constant did not always produce significant changes in enantioselectivity as hypothesized. Finally, molecular modeling experiments were performed to obtain a better understanding of the interactions. These experiments revealed that there are substrate–enzyme interactions that can be influenced by the addition of ethanol.