An investigation into the biocatalytic application of the thermostable nitrile hydratase from the thermophilic strain Geobacillus pallidus RAPc8

dc.contributor.advisorBurton, Stephanie Gailen_ZA
dc.contributor.authorChiyanzu, Idanen_ZA
dc.date.accessioned2014-07-31T11:13:13Z
dc.date.available2014-07-31T11:13:13Z
dc.date.issued2008en_ZA
dc.descriptionIncludes abstract.
dc.descriptionIncludes bibliographical references (leaves 190-215).
dc.description.abstractNitrile hydratases (NHases) are bacterial metalloenzymes that catalyze the hydration of nitriles to their corresponding amides. The enzymes have been found in several microorganisms and participate in the metabolism of nitrile compounds as source of carbon and nitrogen. The commercial use of NHases is well recognized and has prompted research interest as well as the application of the enzymes in the manufacture of commodity amide chemicals. This has largely been due to the versatile nature of the enzymes, associated with their physiochemical properties and broad substrate specificity. However, the widespread application of nitrile-converting enzymes in the industrial processes has been restricted in part by the thermal instability of the mesophilic-derived enzymes, and thus there is an increased focus on NHases from thermophilic microorganisms. A novel moderately thermophilic microorganism, Geobacillus pallidus RAPc8, was isolated by our collaborators (Pereira and co-workers, 1998). The strain has an optimal growth temperature of 65oC and constutitively expresses a thermostable nitrile hydratase. The gene cluster containing the nitrile hydratase were cloned, sequenced, and inducibly expressed in E. coli BL21 (DE3) to levels of approximately 49 U/mg. The NHase was purified by four steps including heat treatment, ammonium sulfate precipitation, hydrophobic interaction chromatography and ion exchange chromatography.en_ZA
dc.identifier.apacitationChiyanzu, I. (2008). <i>An investigation into the biocatalytic application of the thermostable nitrile hydratase from the thermophilic strain Geobacillus pallidus RAPc8</i>. (Thesis). University of Cape Town ,Faculty of Engineering & the Built Environment ,Department of Chemical Engineering. Retrieved from http://hdl.handle.net/11427/5367en_ZA
dc.identifier.chicagocitationChiyanzu, Idan. <i>"An investigation into the biocatalytic application of the thermostable nitrile hydratase from the thermophilic strain Geobacillus pallidus RAPc8."</i> Thesis., University of Cape Town ,Faculty of Engineering & the Built Environment ,Department of Chemical Engineering, 2008. http://hdl.handle.net/11427/5367en_ZA
dc.identifier.citationChiyanzu, I. 2008. An investigation into the biocatalytic application of the thermostable nitrile hydratase from the thermophilic strain Geobacillus pallidus RAPc8. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Chiyanzu, Idan AB - Nitrile hydratases (NHases) are bacterial metalloenzymes that catalyze the hydration of nitriles to their corresponding amides. The enzymes have been found in several microorganisms and participate in the metabolism of nitrile compounds as source of carbon and nitrogen. The commercial use of NHases is well recognized and has prompted research interest as well as the application of the enzymes in the manufacture of commodity amide chemicals. This has largely been due to the versatile nature of the enzymes, associated with their physiochemical properties and broad substrate specificity. However, the widespread application of nitrile-converting enzymes in the industrial processes has been restricted in part by the thermal instability of the mesophilic-derived enzymes, and thus there is an increased focus on NHases from thermophilic microorganisms. A novel moderately thermophilic microorganism, Geobacillus pallidus RAPc8, was isolated by our collaborators (Pereira and co-workers, 1998). The strain has an optimal growth temperature of 65oC and constutitively expresses a thermostable nitrile hydratase. The gene cluster containing the nitrile hydratase were cloned, sequenced, and inducibly expressed in E. coli BL21 (DE3) to levels of approximately 49 U/mg. The NHase was purified by four steps including heat treatment, ammonium sulfate precipitation, hydrophobic interaction chromatography and ion exchange chromatography. DA - 2008 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 2008 T1 - An investigation into the biocatalytic application of the thermostable nitrile hydratase from the thermophilic strain Geobacillus pallidus RAPc8 TI - An investigation into the biocatalytic application of the thermostable nitrile hydratase from the thermophilic strain Geobacillus pallidus RAPc8 UR - http://hdl.handle.net/11427/5367 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/5367
dc.identifier.vancouvercitationChiyanzu I. An investigation into the biocatalytic application of the thermostable nitrile hydratase from the thermophilic strain Geobacillus pallidus RAPc8. [Thesis]. University of Cape Town ,Faculty of Engineering & the Built Environment ,Department of Chemical Engineering, 2008 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/5367en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDepartment of Chemical Engineeringen_ZA
dc.publisher.facultyFaculty of Engineering and the Built Environment
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherChemical Engineeringen_ZA
dc.titleAn investigation into the biocatalytic application of the thermostable nitrile hydratase from the thermophilic strain Geobacillus pallidus RAPc8en_ZA
dc.typeDoctoral Thesis
dc.type.qualificationlevelDoctoral
dc.type.qualificationnamePhDen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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