05548nam 2200697 450 991013218600332120200520144314.03-527-68251-13-527-68249-X3-527-68248-1(CKB)3710000000139316(EBL)1718754(OCoLC)881887767(SSID)ssj0001305566(PQKBManifestationID)11691961(PQKBTitleCode)TC0001305566(PQKBWorkID)11249129(PQKB)10099098(OCoLC)884588782(MiAaPQ)EBC1718754(Au-PeEL)EBL1718754(CaPaEBR)ebr10887095(CaONFJC)MIL622042(PPN)22460595X(EXLCZ)99371000000013931620140710h20142014 uy 0engur|n|---|||||txtccrCascade biocatalysis integrating stereoselective and environmentally friendly reactions /edited by Sergio Riva and Wolf-Dieter FessnerWeinheim, Germany :Wiley-VCH,2014.©20141 online resource (489 p.)Description based upon print version of record.3-527-33522-6 Includes bibliographical references and index.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 Peroxygenases1.6 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; 2.2.1.1 Formate Dehydrogenase and Glucose Dehydrogenase; 2.2.1.2 Phosphite Dehydrogenase; 2.2.1.3 Hydrogenase; 2.2.1.4 Glucose 6-Phosphate Dehydrogenase; 2.2.1.5 Alcohol Dehydrogenase2.2.2 In Situ Regeneration of Oxidized NAD(P)+ Cofactors2.2.2.1 Lactate Dehydrogenase; 2.2.2.2 NAD(P)H Oxidase; 2.2.2.3 Alcohol Dehydrogenase; 2.2.2.4 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 Reactions3.1.8 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; ReferencesChapter 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; 5.3.1.1 Cofactor Regeneration in Cell-Free Systems (In Vitro)5.3.2 Cofactor Regeneration in Whole-Cell BiocatalystsThis 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: fBiocatalysisEnvironmental aspectsCatalysisEnvironmental aspectsEnzymesBiotechnologyBiocatalysisEnvironmental aspects.CatalysisEnvironmental aspects.EnzymesBiotechnology.660.2995Riva SergioFessner W.-D(Wolf-Dieter),MiAaPQMiAaPQMiAaPQBOOK9910132186003321Cascade biocatalysis1920121UNINA