Enantioselective Epoxidation of Alkenes by Chloroperoxidase and the Development of a Chloroperoxidase Expression System

Chloroperoxidase from Caldariomyces fumago has the characteristics of a promising industrial catalyst. Chloroperoxidase is inexpensive to produce and relatively stable and able to catalyze a large number of potentially useful reactions. However, the majority of the reactions studied occur with a lack of any enzyme induced stereoselectivity. Chloroperoxidase, in this report, is shown to catalyze the epoxidation reaction of a number of alkenes in a highly enantioselective manner with enantiomeric excesses between 50% and 97%. Good substrates were generally non-polar cis-alkenes of less than nine carbons in length. Unsubstituted terminal alkenes were shown to inactivate the enzyme. The recent determination of the three dimensional structure by x-ray crystallography and ongoing research in the development of an expression system for chloroperoxidase could open the door for a number of experiments concerning the mechanism of the epoxidation reaction. Also the possibility of improving the utility of chloroperoxidase in asymmetric epoxidations through directed evolution and site-directed mutagenesis remains an exciting prospect for the future.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Allain, Eric Joseph

Contributors dc:contributor

• Hager, Lowell P.

• Chemistry, Organic

Language dc:language

eng

Identifier

(MiAaPQ)AAI9717245

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84874