Date of Award
5-2008
Document Type
Thesis
Degree Name
Master of Science (MS)
College/School
College of Science and Mathematics
Department/Program
Chemistry and Biochemistry
Thesis Sponsor/Dissertation Chair/Project Chair
James Dyer
Committee Member
Saliya DeSilva
Committee Member
Mark Whitener
Abstract
The [beta]-oxidation system in sunflower (Helianthus annuus L.) cotyledons is distinguished by the existence of two different thiolase isoforms, Thiolase I (acetoacetyl-CoA thiolase, EC 2.3.1.9 AACT) and Thiolase II (3-oxoacyl-CoA thiolase, EC 2.3.1.16 OACT). Glyoxysomal AACT is the last enzyme in the p-oxidation of fatty acids in plant glyoxysomes. Glyoxysomal AACT has been successfully cloned, expressed and purified from sunflower cotyledons (Dyer et al., 2006). In this paper we investigate the optimal conditions for both expression and purification. These include the choice of vector, the growth conditions and the purification parameters for the maximum possible yield of AACT protein.
File Format
Recommended Citation
Maina, Anthony Muriithi, "Optimization of Expression and Purification of Acetoacetyl-CoA Thiolase from Sunflower" (2008). Theses, Dissertations and Culminating Projects. 1199.
https://digitalcommons.montclair.edu/etd/1199