Show simple item record

dc.contributor.authorPatel, Jay Mayank
dc.date.accessioned2014-03-04T21:03:32Z
dc.date.available2014-03-04T21:03:32Z
dc.date.issued2013-05
dc.identifier.otherpatel_jay_m_201305_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/patel_jay_m_201305_ms
dc.identifier.urihttp://hdl.handle.net/10724/28863
dc.description.abstractAlcohol dehydrogenases (ADHs) are enzymes that catalyze the reversible reduction of carbonyl compounds to their corresponding alcohols. In chapter 2, we study the effect of hydrostatic pressure on stereospecificity of secondary ADH (SADH) from Thermoanaerobacter ethanolicus catalyzed oxidation of alcohols. Under high pressure conditions of 137.5 MPa and at 298K, the enantiomeric ratio (E) can be enhanced to 13.5 compared to 3.9 at room temperature and pressure for (S)-2-hexanol over (R)-2-hexanol. In chapter 3, site saturation mutagenesis approach was adopted in creating a comprehensive SADH mutant library at W110; and we used phenylacetone as a model substrate to study the effectiveness of our library. We are pleased to note that five of our mutants gave reductions at >99.9% e.e. and two of the mutants showed an E of over 100 for (S)-1-phenyl-2-propanol.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectBiocatalysis
dc.subjectAlcohol dehydrogenase
dc.subjectThermoanaerobacter ethanolicus
dc.subjectAsymmetric synthesis
dc.titleEffects of temperature and pressure on enantiospecificity of novel secondary alcohol dehydrogenase mutants from Thermoanaerobacter ethanolicus
dc.typeThesis
dc.description.degreeMS
dc.description.departmentChemistry
dc.description.majorChemistry
dc.description.advisorRobert Phillips
dc.description.committeeRobert Phillips
dc.description.committeeJin Xie
dc.description.committeeVladimir V. Popik


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record