<p>In this study G. pallidus RAPc8 NHase mutants were screened for reduced substrate inhibition compared to the wild type enzyme. Wild type and mutant enzymes were expressed and purified using hydrophobic interaction chromatography. Amidase coupled enzyme stop assays were conducted using 3-cyanopyridine as a substrate, whereas continuous enzyme kinetics were conducted using acrylonitrile as a substrate.</p>
| Identifer | oai:union.ndltd.org:netd.ac.za/oai:union.ndltd.org:uwc/oai:UWC_ETD:http%3A%2F%2Fetd.uwc.ac.za%2Findex.php%3Fmodule%3Detd%26action%3Dviewtitle%26id%3Dgen8Srv25Nme4_1166_1307514664 |
| Date | January 2009 |
| Creators | Mketsu, Moses Clive Masisange |
| Source Sets | South African National ETD Portal |
| Language | English |
| Detected Language | English |
| Type | Thesis and dissertation |
| Format | |
| Coverage | ZA |
| Rights | Copyright: University of the Western Cape |
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