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dc.contributor.advisorWatkins, Linette M.
dc.contributor.authorMoore, Alysha Michele
dc.date.accessioned2012-06-22T20:32:56Z
dc.date.available2012-06-22T20:32:56Z
dc.date.issued2012-05-22
dc.identifier.urihttps://digital.library.txstate.edu/handle/10877/4175
dc.descriptionPresented to the Honors Committee of Texas State University-San Marcos In Partial Fulfillment of the Requirements For Graduation in the Honors College, May 2012.en_US
dc.description.abstractThe DszB enzyme, found in Rhodococcus erythropolis, is part of a metabolic desulfurization pathway which can be used to remove harmful sulfur from crude oil. The mechanism of this enzyme was studied using inhibition, inactivation, and alternative substrate studies. The possibility of DszB using a covalent mechanism was dismissed but either a non-covalent mechanism or a reversible covalent mechanism is still a viable option for this enzyme. Further studies are needed to better distinguish between the two current mechanism theories.en_US
dc.formatText
dc.format.extent37 pages
dc.format.medium1 file (.pdf)
dc.language.isoen_US
dc.subjectKinetics
dc.subjectBacteria
dc.subjectFuel
dc.subjectDesulfurization
dc.subjectSubstrate
dc.subjectAnalog
dc.subjectPurification
dc.subjectEnzymeen_US
dc.titlePurification and Characterization of 2'-Hydrozybiphenyl-2-Sulfinate Desulfinase (DSZB) using the Substrate Analog Thiourea Dioxideen_US
txstate.documenttypeThesis
thesis.degree.departmentHonors College
thesis.degree.disciplineChemistry and Biochemistry
thesis.degree.grantorTexas State University
txstate.departmentHonors College


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