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Abstract
Alcohol dehydrogenases (ADHs) are enzymes that catalyze the reversible reduction ofcarbonyl compounds to their corresponding alcohols. In chapter 2, we study the effect ofhydrostatic pressure on stereospecificity of secondary ADH (SADH) fromThermoanaerobacter ethanolicus catalyzed oxidation of alcohols. Under high pressureconditions of 137.5 MPa and at 298K, the enantiomeric ratio (E) can be enhanced to 13.5compared 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 acomprehensive SADH mutant library at W110; and we used phenylacetone as a modelsubstrate to study the effectiveness of our library. We are pleased to note that five of ourmutants gave reductions at >99.9% e.e. and two of the mutants showed an E of over 100for (S)-1-phenyl-2-propanol.