Investigation of the Cosolvent Effect on Six Isoenzymes of PLE in the Enantioselective Hydrolysis of Selected a,a-Disubstituted Malonate Esters

Authors

Maureen E. Smith, University of Southern MississippiFollow
Souvik Banerjee, University of Southern Mississippi
Yongliang Shi, University of Southern MississippiFollow
Marlen Schmidt, Enzymicals AG
Uwe T. Bornscheur, Greifswald University
Douglas S. Masterson, University of Southern MississippiFollow

Document Type

Article

Publication Date

4-1-2012

Department

Chemistry and Biochemistry

School

Mathematics and Natural Sciences

Abstract

Six pigs in a pot: Pig liver esterase (PLE) is among the most widely studied esterase enzymes utilized in organic synthesis. Here we illustrate that the six recombinantly produced isoenzymes of PLE exhibit varying enantioselectivity during the hydrolysis of α,α‐disubstituted malonate esters in cosolvent mixtures. We have observed a rare cosolvent‐induced reversal of enantioselectivity for isoenzyme PLE 6 in the hydrolysis of a phthalimide‐containing α,α‐disubstituted malonate ester.

Publication Title

ChemCatChem

Volume

4

Issue

4

First Page

472

Last Page

475

Recommended Citation

Smith, M. E., Banerjee, S., Shi, Y., Schmidt, M., Bornscheur, U. T., Masterson, D. S. (2012). Investigation of the Cosolvent Effect on Six Isoenzymes of PLE in the Enantioselective Hydrolysis of Selected a,a-Disubstituted Malonate Esters. ChemCatChem, 4(4), 472-475.
Available at: https://aquila.usm.edu/fac_pubs/8867