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Cascade biocatalysis : integrating stereoselective and environmentally friendly reactions / / edited by Sergio Riva and Wolf-Dieter Fessner
| Cascade biocatalysis : integrating stereoselective and environmentally friendly reactions / / edited by Sergio Riva and Wolf-Dieter Fessner |
| Pubbl/distr/stampa | Weinheim, Germany : , : Wiley-VCH, , 2014 |
| Descrizione fisica | 1 online resource (489 p.) |
| Disciplina | 660.2995 |
| Soggetto topico |
Biocatalysis - Environmental aspects
Catalysis - Environmental aspects Enzymes - Biotechnology |
| ISBN |
3-527-68251-1
3-527-68249-X 3-527-68248-1 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
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; 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 Dehydrogenase 2.2.2 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 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; 5.3.1.1 Cofactor Regeneration in Cell-Free Systems (In Vitro) 5.3.2 Cofactor Regeneration in Whole-Cell Biocatalysts |
| Record Nr. | UNINA-9910132186003321 |
| Weinheim, Germany : , : Wiley-VCH, , 2014 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Cascade biocatalysis : integrating stereoselective and environmentally friendly reactions / / edited by Sergio Riva and Wolf-Dieter Fessner
| Cascade biocatalysis : integrating stereoselective and environmentally friendly reactions / / edited by Sergio Riva and Wolf-Dieter Fessner |
| Pubbl/distr/stampa | Weinheim, Germany : , : Wiley-VCH, , 2014 |
| Descrizione fisica | 1 online resource (489 p.) |
| Disciplina | 660.2995 |
| Soggetto topico |
Biocatalysis - Environmental aspects
Catalysis - Environmental aspects Enzymes - Biotechnology |
| ISBN |
3-527-68251-1
3-527-68249-X 3-527-68248-1 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
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; 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 Dehydrogenase 2.2.2 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 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; 5.3.1.1 Cofactor Regeneration in Cell-Free Systems (In Vitro) 5.3.2 Cofactor Regeneration in Whole-Cell Biocatalysts |
| Record Nr. | UNINA-9910820091703321 |
| Weinheim, Germany : , : Wiley-VCH, , 2014 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Modern biocatalysis [[electronic resource] ] : stereoselective and environmentally friendly reactions / / edited by Wolf-Dieter Fessner and Thorleif Anthonsen
| Modern biocatalysis [[electronic resource] ] : stereoselective and environmentally friendly reactions / / edited by Wolf-Dieter Fessner and Thorleif Anthonsen |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2009 |
| Descrizione fisica | 1 online resource (401 p.) |
| Disciplina | 660.634 |
| Altri autori (Persone) |
FessnerW.-D (Wolf-Dieter)
AnthonsenThorleif |
| Soggetto topico |
Enzymes - Biotechnology
Catalysis |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-282-02547-3
9786612025471 3-527-62383-3 3-527-62384-1 |
| Classificazione |
58.30
35.17 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Modern Biocatalysis; Contents; Preface; List of Contributors; 1: Fluorescence Assays for Biotransformations; 1.1 Introduction; 1.2 Alcohol Dehydrogenases (ADHs) and Aldolases; 1.2.1 Chiral Fluorogenic ADH Substrates; 1.2.2 Fluorogenic Aldolase Probes; 1.2.3 Transaldolases and Transketolases; 1.2.4 Enolase Probe; 1.3 Lipases and Esterases; 1.3.1 Assays on Solid Support; 1.3.2 The Clips-O Substrates with Periodate; 1.3.3 Esters of Fluorogenic Cyanohydrins and Hydroxyketones; 1.3.4 Fluorogenic Acyloxymethyl Ethers; 1.3.5 FRET-Lipase Probes; 1.4 Other Hydrolases; 1.4.1 Epoxide Hydrolases
1.4.2 Amidases and Proteases1.4.3 Phosphatases; 1.5 Baeyer-Villigerases; 1.6 Conclusion; Acknowledgment; References; 2: Immobilization as a Tool for Improving Enzymes; 2.1 Introduction; 2.2 Adsorption/Electrostatic Interactions; 2.2.1 Van der Waals Interactions; 2.2.2 Hydrogen Bonds; 2.2.3 Ionic Interactions; 2.3 Encapsulation; 2.4 Covalent Binding/Cross-linking; 2.5 Conclusion; Acknowledgments; References; 3: Continuous-flow Microchannel Reactors with Surface-immobilized Biocatalysts; 3.1 Introduction 3.2 Biocatalytic Synthesis Using Microreaction Technology with Free and Immobilized Enzymes3.3 Novel Microfluidic Immobilized Enzyme Reactors; 3.3.1 Microreactor Design; 3.3.2 Enzyme Immobilization; 3.4 Enzymatic Hydrolysis of Lactose; 3.4.1 Catalytic Effectiveness of Immobilized CelB; 3.4.2 Continuous Conversion of Lactose; 3.5 Biocatalytic Process Intensification Using Microreaction Technology; 3.6 Conclusions and Outlook; Acknowledgements; References; 4: Activity and Stability of Proteases in Hydrophilic Solvents; 4.1 Introduction 4.2 Activity and Selectivity of Proteases in Synthesis of Carbohydrate Fatty Acid Esters4.3 Enzyme Stability and Conformation; 4.4 Solvent Engineering; 4.5 Conclusion; References; 5: Importance of Enzyme Formulation for the Activity and Enantioselectivity of Lipases in Organic Solvents; 5.1 Introduction; 5.2 Lipase Formulations and their Activity and Enantioselectivity in Neat Organic Solvent; 5.3 Why do Additives Affect the Activity and Enantioselectivity of Lipases in Organic Solvent?; 5.4 Conclusions; References 6: Direct Esterification with Dry Mycelia of Molds: a (Stereo)selective, Mild and Efficient Method for Obtaining Structurally Diverse Esters6.1 Mycelia and Biotransformations in Organic Media; 6.2 Screening and Microbiological Aspects; 6.3 Production of Acetates; 6.4 Stereoselective Esterifications of Racemic Alcohols; 6.5 Stereoselective Esterifications of Racemic Carboxylic Acids; 6.6 Partition Phenomena and Equilibrium of Esterification Reactions; 6.7 Conclusions; References; 7: Factors Affecting Enantioselectivity: Allosteric Effects; 7.1 How to Provide Enantiopure Compounds 7.1.1 Kinetic Resolution of Racemic Mixtures Catalyzed by Enzymes |
| Record Nr. | UNINA-9910145260603321 |
| Weinheim, : Wiley-VCH, c2009 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Modern biocatalysis [[electronic resource] ] : stereoselective and environmentally friendly reactions / / edited by Wolf-Dieter Fessner and Thorleif Anthonsen
| Modern biocatalysis [[electronic resource] ] : stereoselective and environmentally friendly reactions / / edited by Wolf-Dieter Fessner and Thorleif Anthonsen |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2009 |
| Descrizione fisica | 1 online resource (401 p.) |
| Disciplina | 660.634 |
| Altri autori (Persone) |
FessnerW.-D (Wolf-Dieter)
AnthonsenThorleif |
| Soggetto topico |
Enzymes - Biotechnology
Catalysis |
| ISBN |
1-282-02547-3
9786612025471 3-527-62383-3 3-527-62384-1 |
| Classificazione |
58.30
35.17 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Modern Biocatalysis; Contents; Preface; List of Contributors; 1: Fluorescence Assays for Biotransformations; 1.1 Introduction; 1.2 Alcohol Dehydrogenases (ADHs) and Aldolases; 1.2.1 Chiral Fluorogenic ADH Substrates; 1.2.2 Fluorogenic Aldolase Probes; 1.2.3 Transaldolases and Transketolases; 1.2.4 Enolase Probe; 1.3 Lipases and Esterases; 1.3.1 Assays on Solid Support; 1.3.2 The Clips-O Substrates with Periodate; 1.3.3 Esters of Fluorogenic Cyanohydrins and Hydroxyketones; 1.3.4 Fluorogenic Acyloxymethyl Ethers; 1.3.5 FRET-Lipase Probes; 1.4 Other Hydrolases; 1.4.1 Epoxide Hydrolases
1.4.2 Amidases and Proteases1.4.3 Phosphatases; 1.5 Baeyer-Villigerases; 1.6 Conclusion; Acknowledgment; References; 2: Immobilization as a Tool for Improving Enzymes; 2.1 Introduction; 2.2 Adsorption/Electrostatic Interactions; 2.2.1 Van der Waals Interactions; 2.2.2 Hydrogen Bonds; 2.2.3 Ionic Interactions; 2.3 Encapsulation; 2.4 Covalent Binding/Cross-linking; 2.5 Conclusion; Acknowledgments; References; 3: Continuous-flow Microchannel Reactors with Surface-immobilized Biocatalysts; 3.1 Introduction 3.2 Biocatalytic Synthesis Using Microreaction Technology with Free and Immobilized Enzymes3.3 Novel Microfluidic Immobilized Enzyme Reactors; 3.3.1 Microreactor Design; 3.3.2 Enzyme Immobilization; 3.4 Enzymatic Hydrolysis of Lactose; 3.4.1 Catalytic Effectiveness of Immobilized CelB; 3.4.2 Continuous Conversion of Lactose; 3.5 Biocatalytic Process Intensification Using Microreaction Technology; 3.6 Conclusions and Outlook; Acknowledgements; References; 4: Activity and Stability of Proteases in Hydrophilic Solvents; 4.1 Introduction 4.2 Activity and Selectivity of Proteases in Synthesis of Carbohydrate Fatty Acid Esters4.3 Enzyme Stability and Conformation; 4.4 Solvent Engineering; 4.5 Conclusion; References; 5: Importance of Enzyme Formulation for the Activity and Enantioselectivity of Lipases in Organic Solvents; 5.1 Introduction; 5.2 Lipase Formulations and their Activity and Enantioselectivity in Neat Organic Solvent; 5.3 Why do Additives Affect the Activity and Enantioselectivity of Lipases in Organic Solvent?; 5.4 Conclusions; References 6: Direct Esterification with Dry Mycelia of Molds: a (Stereo)selective, Mild and Efficient Method for Obtaining Structurally Diverse Esters6.1 Mycelia and Biotransformations in Organic Media; 6.2 Screening and Microbiological Aspects; 6.3 Production of Acetates; 6.4 Stereoselective Esterifications of Racemic Alcohols; 6.5 Stereoselective Esterifications of Racemic Carboxylic Acids; 6.6 Partition Phenomena and Equilibrium of Esterification Reactions; 6.7 Conclusions; References; 7: Factors Affecting Enantioselectivity: Allosteric Effects; 7.1 How to Provide Enantiopure Compounds 7.1.1 Kinetic Resolution of Racemic Mixtures Catalyzed by Enzymes |
| Record Nr. | UNINA-9910830040103321 |
| Weinheim, : Wiley-VCH, c2009 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Modern biocatalysis : stereoselective and environmentally friendly reactions / / edited by Wolf-Dieter Fessner and Thorleif Anthonsen
| Modern biocatalysis : stereoselective and environmentally friendly reactions / / edited by Wolf-Dieter Fessner and Thorleif Anthonsen |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2009 |
| Descrizione fisica | 1 online resource (401 p.) |
| Disciplina | 660.634 |
| Altri autori (Persone) |
FessnerW.-D (Wolf-Dieter)
AnthonsenThorleif |
| Soggetto topico |
Enzymes - Biotechnology
Catalysis |
| ISBN |
1-282-02547-3
9786612025471 3-527-62383-3 3-527-62384-1 |
| Classificazione |
58.30
35.17 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Modern Biocatalysis; Contents; Preface; List of Contributors; 1: Fluorescence Assays for Biotransformations; 1.1 Introduction; 1.2 Alcohol Dehydrogenases (ADHs) and Aldolases; 1.2.1 Chiral Fluorogenic ADH Substrates; 1.2.2 Fluorogenic Aldolase Probes; 1.2.3 Transaldolases and Transketolases; 1.2.4 Enolase Probe; 1.3 Lipases and Esterases; 1.3.1 Assays on Solid Support; 1.3.2 The Clips-O Substrates with Periodate; 1.3.3 Esters of Fluorogenic Cyanohydrins and Hydroxyketones; 1.3.4 Fluorogenic Acyloxymethyl Ethers; 1.3.5 FRET-Lipase Probes; 1.4 Other Hydrolases; 1.4.1 Epoxide Hydrolases
1.4.2 Amidases and Proteases1.4.3 Phosphatases; 1.5 Baeyer-Villigerases; 1.6 Conclusion; Acknowledgment; References; 2: Immobilization as a Tool for Improving Enzymes; 2.1 Introduction; 2.2 Adsorption/Electrostatic Interactions; 2.2.1 Van der Waals Interactions; 2.2.2 Hydrogen Bonds; 2.2.3 Ionic Interactions; 2.3 Encapsulation; 2.4 Covalent Binding/Cross-linking; 2.5 Conclusion; Acknowledgments; References; 3: Continuous-flow Microchannel Reactors with Surface-immobilized Biocatalysts; 3.1 Introduction 3.2 Biocatalytic Synthesis Using Microreaction Technology with Free and Immobilized Enzymes3.3 Novel Microfluidic Immobilized Enzyme Reactors; 3.3.1 Microreactor Design; 3.3.2 Enzyme Immobilization; 3.4 Enzymatic Hydrolysis of Lactose; 3.4.1 Catalytic Effectiveness of Immobilized CelB; 3.4.2 Continuous Conversion of Lactose; 3.5 Biocatalytic Process Intensification Using Microreaction Technology; 3.6 Conclusions and Outlook; Acknowledgements; References; 4: Activity and Stability of Proteases in Hydrophilic Solvents; 4.1 Introduction 4.2 Activity and Selectivity of Proteases in Synthesis of Carbohydrate Fatty Acid Esters4.3 Enzyme Stability and Conformation; 4.4 Solvent Engineering; 4.5 Conclusion; References; 5: Importance of Enzyme Formulation for the Activity and Enantioselectivity of Lipases in Organic Solvents; 5.1 Introduction; 5.2 Lipase Formulations and their Activity and Enantioselectivity in Neat Organic Solvent; 5.3 Why do Additives Affect the Activity and Enantioselectivity of Lipases in Organic Solvent?; 5.4 Conclusions; References 6: Direct Esterification with Dry Mycelia of Molds: a (Stereo)selective, Mild and Efficient Method for Obtaining Structurally Diverse Esters6.1 Mycelia and Biotransformations in Organic Media; 6.2 Screening and Microbiological Aspects; 6.3 Production of Acetates; 6.4 Stereoselective Esterifications of Racemic Alcohols; 6.5 Stereoselective Esterifications of Racemic Carboxylic Acids; 6.6 Partition Phenomena and Equilibrium of Esterification Reactions; 6.7 Conclusions; References; 7: Factors Affecting Enantioselectivity: Allosteric Effects; 7.1 How to Provide Enantiopure Compounds 7.1.1 Kinetic Resolution of Racemic Mixtures Catalyzed by Enzymes |
| Record Nr. | UNINA-9910876609703321 |
| Weinheim, : Wiley-VCH, c2009 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||