Understanding Kinetic Resolution by Hydrolases: Maximizing Enantioselectivity (SpringerBriefs in Molecular Science)

Preface
Acknowledgements
Contents
Abbreviations
1 Understanding Enzymatic Kinetic Resolution
	1.1 Enzymatic Kinetic Resolution (EKR): Importance
	1.2 Negativities of Enzymatic Kinetic Resolutions
	1.3 Enzymatic Kinetic Resolution: Understanding the Process
	1.4 Kinetic Resolution and Desymmetrization
	References
2 Essential Parameters: Determination and Significance
	2.1 Parameters of EKR
		2.1.1 Enantiomeric Excess (ee)
		2.1.2 Determination of ee
		2.1.3 Enantioselectivity, E: Concepts in Biocatalysis
	2.2 Enantioselectivity, Enantiomeric Excess and Conversion During the Course of an EKR
		2.2.1 Dependence of the Substrate ee on Conversion
		2.2.2 “E is More Significant than ee”
		2.2.3 Dependence of the Product ee on Conversion
	2.3 Condition for a High Enantioselectivity
	References
3 Enantioselectivity: The Decisive Factors
	3.1 Factors Affecting Enantioselectivity
		3.1.1 Effect of Temperature
		3.1.2 Effect of Water Content
		3.1.3 Effect of the Presence of Water Miscible Organic Co-solvents
		3.1.4 Effect of Immobilization
		3.1.5 Choice of the Acyl Donor: EKR via Transacylation
	3.2 Uses of Lipases for Kinetic Resolution: Examples
	3.3 Use of Proteases for EKR
	3.4 Opposite Enantiopreference by Hydrolases: The Kazlauskas’ Model
	References
4 Dynamic Kinetic Resolution
	4.1 DKR: Understanding the Process
	4.2 DKR of Secondary Alcohols and Amines: Use of Ruthenium
		4.2.1 Use of Lipase-Ruthenium Combination
		4.2.2 DKR: Use of Subtilisin–Ruthenium Combination
	4.3 DKR of Secondary Alcohols and Amines: Use of Palladium
		4.3.1 Palladium as Heterogeneous Catalyst
		4.3.2 Use of Palladium Nanocatalyst
		4.3.3 Use of Pd-Enzyme Immobilized Hybrid Catalyst
	References
Index