{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84874"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84874","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Enantioselective Epoxidation of Alkenes by Chloroperoxidase and the Development of a Chloroperoxidase Expression System","abstract":"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.","abstract_html":"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.","abstract_has_math":false,"creators":["Allain, Eric Joseph"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Hager, Lowell P."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:28:17Z","date_published":"2015-09-25T22:28:17Z","updated_at":"2026-07-22T22:26:24Z","subjects":["Chemistry, Organic"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9717245"],"render_values":[{"text":"(MiAaPQ)AAI9717245","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84874","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Hager, Lowell P."]},{"key":"dc:creator","label":"Author","values":["Allain, Eric Joseph"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:28:17Z","10000-01-01","1997"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry, Organic"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/84874","(MiAaPQ)AAI9717245"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["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.","Made available in DSpace on 2015-09-25T22:28:17Z (GMT). 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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. 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