Cascade biocatalysis : integrating stereoselective and environmentally friendly reactions / edited by Sergio Riva and Wolf-Dieter Fessner.

Weinheim, Germany : Wiley-VCH, 2014.
1 online resource (489 p.)
Biocatalysis -- Environmental aspects.
Catalysis -- Environmental aspects.
Enzymes -- Biotechnology.
Electronic books.
This ready reference presents environmentally friendly and stereoselective methods of modern biocatalysis. The experienced and renowned team of editor have gathered top international authors for this book. They cover such emerging topics as chemoenzymatic methods and multi-step enzymatic reactions, while showing how these novel methods and concepts can be used for practical applications. Multidisciplinary topics, including directed evolution, dynamic kinetic resolution, and continuous-flow methodology are also discussed. From the contents:- Directed evolution of ligninolytic oxidoreductases: f
Cascade Biocatalysis; Contents; List of Contributors; Preface; Chapter 1 Directed Evolution of Ligninolytic Oxidoreductases: from Functional Expression to Stabilization and Beyond; 1.1 Introduction; 1.2 Directed Molecular Evolution; 1.3 The Ligninolytic Enzymatic Consortium; 1.4 Directed Evolution of Laccases; 1.4.1 Directed Evolution of Low-Redox Potential Laccases; 1.4.2 Directed Evolution of Medium-Redox Potential Laccases; 1.4.3 Directed Evolution of Ligninolytic High-Redox Potential Laccases (HRPLs); 1.5 Directed Evolution of Peroxidases and Peroxygenases
1.6 Saccharomyces cerevisiae Biomolecular Tool Box1.7 Conclusions and Outlook; Acknowledgments; Abbreviations; References; Chapter 2 New Trends in the In Situ Enzymatic Recycling of NAD(P)(H) Cofactors; 2.1 Introduction; 2.2 Recent Advancements in the Enzymatic Methods for the Recycling of NAD(P)(H) Coenzymes and Novel Regeneration Systems; 2.2.1 In Situ Regeneration of Reduced NAD(P)H Cofactors; Formate Dehydrogenase and Glucose Dehydrogenase; Phosphite Dehydrogenase; Hydrogenase; Glucose 6-Phosphate Dehydrogenase; Alcohol Dehydrogenase
2.2.2 In Situ Regeneration of Oxidized NAD(P)+ Cofactors2.2.2.1 Lactate Dehydrogenase; NAD(P)H Oxidase; Alcohol Dehydrogenase; Mediator-Coupled Enzyme Systems; 2.3 Conclusions; Acknowledgments; References; Chapter 3 Monooxygenase-Catalyzed Redox Cascade Biotransformations; 3.1 Introduction; 3.1.1 Scope of this Chapter; 3.1.2 Enzymatic Oxygenation; 3.1.3 Effective Cofactor Recycling; 3.1.4 In Vitro Multistep Biocatalysis; 3.1.5 Combined In Vitro and In Vivo Multistep Biocatalysis; 3.1.6 In Vivo Multistep Biocatalysis; 3.1.7 Chemo-Enzymatic Cascade Reactions
3.1.8 Conclusion and OutlookReferences; Chapter 4 Biocatalytic Redox Cascades Involving ω-Transaminases; 4.1 Introduction; 4.2 General Features of ω-Transaminases; 4.2.1 Cascades to Shift the Equilibrium for Amination; 4.3 Linear Cascade Reactions Involving ω-Transaminases; 4.3.1 Redox and Redox-Neutral Cascade Reactions; 4.3.2 Carbonyl Amination Followed by Spontaneous Ring Closure; 4.3.3 Deracemization of Racemic Amines Employing Two ω-Transaminases; 4.3.4 Cascade Reactions of ω-TAs with Lyases and C-C Hydrolases/Lipases; 4.4 Concluding Remarks; References
Chapter 5 Multi-Enzyme Systems and Cascade Reactions Involving Cytochrome P450 Monooxygenases5.1 Introduction; 5.1.1 Multistep Cascade Reactions; 5.1.2 Cytochrome P450 Monooxygenases; 5.1.3 General Overview of presented cascade types; 5.2 Physiological Cascade Reactions Involving P450s; 5.2.1 Multistep Oxidations Catalyzed by a Single P450; 5.2.2 Multistep Oxidations Catalyzed by Multiple P450s; 5.3 Artificial Cascade Reactions Involving P450s; 5.3.1 Cascade Reactions Involving P450s and Cofactor Regenerating Enzymes; Cofactor Regeneration in Cell-Free Systems (In Vitro)
5.3.2 Cofactor Regeneration in Whole-Cell Biocatalysts
Description based upon print version of record.
Includes bibliographical references and index.
Description based on online resource; title from PDF title page (ebrary, viewed July 8, 2014).
Riva, Sergio, editor.
Fessner, W.-D. (Wolf-Dieter), editor.
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