dc.contributor.advisor |
Reid, Sharon J |
en_ZA |
dc.contributor.author |
Theron, Grant de V
|
en_ZA |
dc.date.accessioned |
2015-01-13T03:59:24Z |
|
dc.date.available |
2015-01-13T03:59:24Z |
|
dc.date.issued |
2009 |
en_ZA |
dc.identifier.citation |
Theron, G. 2009. L-arginine overproduction in Corynebacterium glutamicum ATCC 13032. University of Cape Town. |
en_ZA |
dc.identifier.uri |
http://hdl.handle.net/11427/12122
|
|
dc.description |
Includes abstract. |
en_ZA |
dc.description |
Includes bibliographical references (p. 155-174). |
en_ZA |
dc.description.abstract |
Corynebacterium glutamicum is widely used for the commercial production of a variety of amino acids, including L-lysine, L-glutamate and L-threonine. With the exception of Larginine, the biosynthesis and regulation of most of these compounds in this bacterium are relatively well characterised in the literature. The research presented here focuses on improving our understanding of the regulation of L-arginine biosynthesis in C. glutamicum. This was performed with the ultimate goal of creating strains capable of producing L-arginine commercially. A novel gene replacement system was initially used for the directed mutation of the Larginine biosynthetic gene cluster in C. glutamicum ATCC 13032. This was met with limited success, however, and the pK19mobsacB vector was thus adopted for further mutagenesis of this region. |
en_ZA |
dc.language.iso |
eng |
en_ZA |
dc.subject.other |
Cell Biology |
en_ZA |
dc.title |
L-arginine overproduction in Corynebacterium glutamicum ATCC 13032 |
en_ZA |
dc.type |
Doctoral Thesis |
|
uct.type.publication |
Research |
en_ZA |
uct.type.resource |
Thesis
|
en_ZA |
dc.publisher.institution |
University of Cape Town |
|
dc.publisher.faculty |
Faculty of Science |
en_ZA |
dc.publisher.department |
Department of Molecular and Cell Biology |
en_ZA |
dc.type.qualificationlevel |
Doctoral |
|
dc.type.qualificationname |
PhD |
en_ZA |
uct.type.filetype |
Text |
|
uct.type.filetype |
Image |
|
dc.identifier.apacitation |
Theron, G. d. V. (2009). <i>L-arginine overproduction in Corynebacterium glutamicum ATCC 13032</i>. (Thesis). University of Cape Town ,Faculty of Science ,Department of Molecular and Cell Biology. Retrieved from http://hdl.handle.net/11427/12122 |
en_ZA |
dc.identifier.chicagocitation |
Theron, Grant de V. <i>"L-arginine overproduction in Corynebacterium glutamicum ATCC 13032."</i> Thesis., University of Cape Town ,Faculty of Science ,Department of Molecular and Cell Biology, 2009. http://hdl.handle.net/11427/12122 |
en_ZA |
dc.identifier.vancouvercitation |
Theron GdV. L-arginine overproduction in Corynebacterium glutamicum ATCC 13032. [Thesis]. University of Cape Town ,Faculty of Science ,Department of Molecular and Cell Biology, 2009 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/12122 |
en_ZA |
dc.identifier.ris |
TY - Thesis / Dissertation
AU - Theron, Grant de V
AB - Corynebacterium glutamicum is widely used for the commercial production of a variety of amino acids, including L-lysine, L-glutamate and L-threonine. With the exception of Larginine, the biosynthesis and regulation of most of these compounds in this bacterium are relatively well characterised in the literature. The research presented here focuses on improving our understanding of the regulation of L-arginine biosynthesis in C. glutamicum. This was performed with the ultimate goal of creating strains capable of producing L-arginine commercially. A novel gene replacement system was initially used for the directed mutation of the Larginine biosynthetic gene cluster in C. glutamicum ATCC 13032. This was met with limited success, however, and the pK19mobsacB vector was thus adopted for further mutagenesis of this region.
DA - 2009
DB - OpenUCT
DP - University of Cape Town
LK - https://open.uct.ac.za
PB - University of Cape Town
PY - 2009
T1 - L-arginine overproduction in Corynebacterium glutamicum ATCC 13032
TI - L-arginine overproduction in Corynebacterium glutamicum ATCC 13032
UR - http://hdl.handle.net/11427/12122
ER -
|
en_ZA |