Biocatalysis for green chemistry and chemical process development [[electronic resource] /] / edited by Junhua (Alex) Tao, Romas Kazlauskas |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, c2011 |
Descrizione fisica | 1 online resource (493 p.) |
Disciplina | 660.6/3 |
Altri autori (Persone) |
TaoJunhua
KazlauskasR. J <1956-> (Romas J.) |
Soggetto topico |
Environmental chemistry - Industrial applications
Enzymes - Biotechnology Green technology Química verda Enzims Biocatàlisi Aplicacions industrials Ecotecnologia |
Soggetto genere / forma | Llibres electrònics |
ISBN |
1-283-17573-8
9786613175731 1-118-02829-5 1-118-02828-7 1-118-02830-9 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | Overview of biotechnology tools for green synthesis: enzymes, cells and their tunability by engineering -- How green can the industry become with biotechnology -- Emerging enzymes and their synthetic applications -- Reaction efficiencies and green chemistry metrics of biotransformations -- Application and case studies - pharmaceuticals and fine chemicals -- Biocatalytic routes to chiral intermediates for development of drugs -- Transglutaminase for protein drug modification: pegylation and beyond -- Microbial production of plant-derived pharmaceutical natural products through metabolic engineering: artemisinin and beyond -- Toward greener therapeutic proteins -- Application and case studies ? flavor & fragrance, agrochemicals and fine chemicals -- Opportunities for biocatalysis in the flavor, fragrance and cosmetic industry -- Application of biocatalysis in the agrochemical industry -- Green production of fine chemicals by isolated enzymes -- Whole cell production of fine chemicals and intermediates -- Application and case studies ? polymers and renewable chemicals -- Green chemistry for the production of biodegradable, biorenewable, biocompatible polymers -- Enzymatic degradation of lignocellulosic biomass -- Bioconversion of renewables-plant oils -- Microbial bioprocesses for industrial scale chemical production. |
Record Nr. | UNINA-9910130871103321 |
Hoboken, N.J., : John Wiley & Sons, c2011 | ||
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Lo trovi qui: Univ. Federico II | ||
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Hydrolases in organic synthesis [[electronic resource] ] : regio- and stereoselective biotransformations / / Uwe T. Bornscheuer and Romas J. Kazlauskas |
Autore | Bornscheuer U. T (Uwe Theo), <1964-> |
Edizione | [2nd ed.] |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
Descrizione fisica | 1 online resource (369 p.) |
Disciplina | 547.2 |
Altri autori (Persone) | KazlauskasR. J <1956-> (Romas J.) |
Soggetto topico |
Catalysis
Hydrolases Organic compounds - Synthesis |
Soggetto genere / forma | Electronic books. |
ISBN |
1-280-85420-0
9786610854202 3-527-60754-4 3-527-60712-9 |
Classificazione | 35.74 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Hydrolases in Organic Synthesis; Preface for the 2(nd) edition; Preface for the 1(st) edition; Acknowledgments; Contents; 1 Introduction; 2 Designing Enantioselective Reactions; 2.1 Kinetic Resolutions; 2.1.1 Recycling and Sequential Kinetic Resolutions; 2.1.2 Dynamic Kinetic Resolutions; 2.1.2.1 Introduction; 2.1.2.2 Racemization by Protonation/Deprotonation; 2.1.2.3 Racemization by Addition/Elimination; 2.1.2.4 Racemization by Nucleophilic Substitution; 2.1.2.5 Racemization by Oxidation/Reduction; 2.1.2.6 Related Strategies; 2.2 Asymmetric Syntheses
3 Choosing Reaction Media: Water and Organic Solvents3.1 Hydrolysis in Water; 3.2 Transesterifications and Condensations in Organic Solvents; 3.2.1 Increasing the Catalytic Activity in Organic Solvents; 3.2.1.1 Choosing the Best Organic Solvent for High Activity; 3.2.2 Increasing the Enantioselectivity in Organic Solvents; 3.2.3 Water Content and Water Activity; 3.3 Other Reaction Media; 3.3.1 Ionic Liquids; 3.3.2 Reverse Micelles; 3.3.3 Supercritical Fluids; 3.4 Immobilization; 3.4.1 Introduction; 3.4.1.1 Increasing the Surface Area to Increase Catalytic Activity 4 Protein Sources and Optimization of Biocatalyst Performance4.1 Accessing Biodiversity; 4.2 Creating Improved Biocatalysts; 4.2.1 Directed Evolution; 4.2.1.1 Methods to Create Mutant Libraries; 4.2.1.2 Assay Systems; 4.2.1.3 Selected Examples; 4.2.2 Focused Directed Evolution; 4.3 Catalytic Promiscuity in Hydrolases; 4.3.1 Reactions Involving Functional Group Analogs; 4.3.1.1 Perhydrolases; 4.3.2 Aldol and Michael additions Catalyzed by Hydrolases; 4.3.2.1 Aldol Additions; 4.3.2.2 Michael-Type Additions; 4.3.3 Modifications to Introduce New Reactivity in Hydrolases 4.3.3.1 Enantioselective Reduction of Hydroperoxides with Selenosubtilisin4.3.3.2 Vanadate-Modified Phosphatases as Peroxidases; 5 Lipases and Esterases; 5.1 Availability, Structures and Properties; 5.1.1 Lipases; 5.1.1.1 Classification of Lipases; 5.1.1.2 General Features of PPL, PCL, CRL, CAL-B, and RML; 5.1.2 Esterases; 5.1.3 Lipases and Esterases are α/β Hydrolases; 5.1.4 Lid or Flap in Interfacial Activation of Lipases; 5.1.5 Substrate Binding Site in Lipases and Esterases; 5.1.6 Designing Reactions with Lipases and Esterases; 5.1.6.1 Acyl Donor for Acylation Reactions 5.1.7 Assays for Lipases and Esterases5.1.7.1 Requirements for a Suitable Assay; 5.1.7.2 How to Distinguish Between Lipase, Esterase, and Protease; 5.2 Survey of Enantioselective Lipase-Catalyzed Reactions; 5.2.1 Alcohols; 5.2.1.1 Secondary Alcohols; 5.2.1.2 Primary Alcohols; 5.2.1.3 Other Alcohols, Amines, and Alcohol Analogs; 5.2.2 Carboxylic Acids; 5.2.2.1 General Considerations; 5.2.2.2 Carboxylic Acids with a Stereocenter at the α-Position; 5.2.2.3 Carboxylic Acids with a Stereocenter at the β-Position; 5.2.2.4 Other Carboxylic Acids; 5.2.2.5 Double Enantioselection; 5.2.2.6 Anhydrides 5.2.3 Lactones |
Record Nr. | UNINA-9910144323603321 |
Bornscheuer U. T (Uwe Theo), <1964->
![]() |
||
Weinheim, : Wiley-VCH | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Hydrolases in organic synthesis [[electronic resource] ] : regio- and stereoselective biotransformations / / Uwe T. Bornscheuer and Romas J. Kazlauskas |
Autore | Bornscheuer U. T (Uwe Theo), <1964-> |
Edizione | [2nd ed.] |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
Descrizione fisica | 1 online resource (369 p.) |
Disciplina | 547.2 |
Altri autori (Persone) | KazlauskasR. J <1956-> (Romas J.) |
Soggetto topico |
Catalysis
Hydrolases Organic compounds - Synthesis |
ISBN |
1-280-85420-0
9786610854202 3-527-60754-4 3-527-60712-9 |
Classificazione | 35.74 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Hydrolases in Organic Synthesis; Preface for the 2(nd) edition; Preface for the 1(st) edition; Acknowledgments; Contents; 1 Introduction; 2 Designing Enantioselective Reactions; 2.1 Kinetic Resolutions; 2.1.1 Recycling and Sequential Kinetic Resolutions; 2.1.2 Dynamic Kinetic Resolutions; 2.1.2.1 Introduction; 2.1.2.2 Racemization by Protonation/Deprotonation; 2.1.2.3 Racemization by Addition/Elimination; 2.1.2.4 Racemization by Nucleophilic Substitution; 2.1.2.5 Racemization by Oxidation/Reduction; 2.1.2.6 Related Strategies; 2.2 Asymmetric Syntheses
3 Choosing Reaction Media: Water and Organic Solvents3.1 Hydrolysis in Water; 3.2 Transesterifications and Condensations in Organic Solvents; 3.2.1 Increasing the Catalytic Activity in Organic Solvents; 3.2.1.1 Choosing the Best Organic Solvent for High Activity; 3.2.2 Increasing the Enantioselectivity in Organic Solvents; 3.2.3 Water Content and Water Activity; 3.3 Other Reaction Media; 3.3.1 Ionic Liquids; 3.3.2 Reverse Micelles; 3.3.3 Supercritical Fluids; 3.4 Immobilization; 3.4.1 Introduction; 3.4.1.1 Increasing the Surface Area to Increase Catalytic Activity 4 Protein Sources and Optimization of Biocatalyst Performance4.1 Accessing Biodiversity; 4.2 Creating Improved Biocatalysts; 4.2.1 Directed Evolution; 4.2.1.1 Methods to Create Mutant Libraries; 4.2.1.2 Assay Systems; 4.2.1.3 Selected Examples; 4.2.2 Focused Directed Evolution; 4.3 Catalytic Promiscuity in Hydrolases; 4.3.1 Reactions Involving Functional Group Analogs; 4.3.1.1 Perhydrolases; 4.3.2 Aldol and Michael additions Catalyzed by Hydrolases; 4.3.2.1 Aldol Additions; 4.3.2.2 Michael-Type Additions; 4.3.3 Modifications to Introduce New Reactivity in Hydrolases 4.3.3.1 Enantioselective Reduction of Hydroperoxides with Selenosubtilisin4.3.3.2 Vanadate-Modified Phosphatases as Peroxidases; 5 Lipases and Esterases; 5.1 Availability, Structures and Properties; 5.1.1 Lipases; 5.1.1.1 Classification of Lipases; 5.1.1.2 General Features of PPL, PCL, CRL, CAL-B, and RML; 5.1.2 Esterases; 5.1.3 Lipases and Esterases are α/β Hydrolases; 5.1.4 Lid or Flap in Interfacial Activation of Lipases; 5.1.5 Substrate Binding Site in Lipases and Esterases; 5.1.6 Designing Reactions with Lipases and Esterases; 5.1.6.1 Acyl Donor for Acylation Reactions 5.1.7 Assays for Lipases and Esterases5.1.7.1 Requirements for a Suitable Assay; 5.1.7.2 How to Distinguish Between Lipase, Esterase, and Protease; 5.2 Survey of Enantioselective Lipase-Catalyzed Reactions; 5.2.1 Alcohols; 5.2.1.1 Secondary Alcohols; 5.2.1.2 Primary Alcohols; 5.2.1.3 Other Alcohols, Amines, and Alcohol Analogs; 5.2.2 Carboxylic Acids; 5.2.2.1 General Considerations; 5.2.2.2 Carboxylic Acids with a Stereocenter at the α-Position; 5.2.2.3 Carboxylic Acids with a Stereocenter at the β-Position; 5.2.2.4 Other Carboxylic Acids; 5.2.2.5 Double Enantioselection; 5.2.2.6 Anhydrides 5.2.3 Lactones |
Record Nr. | UNINA-9910830217203321 |
Bornscheuer U. T (Uwe Theo), <1964->
![]() |
||
Weinheim, : Wiley-VCH | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Hydrolases in organic synthesis [[electronic resource] ] : regio- and stereoselective biotransformations / / Uwe T. Bornscheuer and Romas J. Kazlauskas |
Autore | Bornscheuer U. T (Uwe Theo), <1964-> |
Edizione | [2nd ed.] |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
Descrizione fisica | 1 online resource (369 p.) |
Disciplina | 547.2 |
Altri autori (Persone) | KazlauskasR. J <1956-> (Romas J.) |
Soggetto topico |
Catalysis
Hydrolases Organic compounds - Synthesis |
ISBN |
1-280-85420-0
9786610854202 3-527-60754-4 3-527-60712-9 |
Classificazione | 35.74 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Hydrolases in Organic Synthesis; Preface for the 2(nd) edition; Preface for the 1(st) edition; Acknowledgments; Contents; 1 Introduction; 2 Designing Enantioselective Reactions; 2.1 Kinetic Resolutions; 2.1.1 Recycling and Sequential Kinetic Resolutions; 2.1.2 Dynamic Kinetic Resolutions; 2.1.2.1 Introduction; 2.1.2.2 Racemization by Protonation/Deprotonation; 2.1.2.3 Racemization by Addition/Elimination; 2.1.2.4 Racemization by Nucleophilic Substitution; 2.1.2.5 Racemization by Oxidation/Reduction; 2.1.2.6 Related Strategies; 2.2 Asymmetric Syntheses
3 Choosing Reaction Media: Water and Organic Solvents3.1 Hydrolysis in Water; 3.2 Transesterifications and Condensations in Organic Solvents; 3.2.1 Increasing the Catalytic Activity in Organic Solvents; 3.2.1.1 Choosing the Best Organic Solvent for High Activity; 3.2.2 Increasing the Enantioselectivity in Organic Solvents; 3.2.3 Water Content and Water Activity; 3.3 Other Reaction Media; 3.3.1 Ionic Liquids; 3.3.2 Reverse Micelles; 3.3.3 Supercritical Fluids; 3.4 Immobilization; 3.4.1 Introduction; 3.4.1.1 Increasing the Surface Area to Increase Catalytic Activity 4 Protein Sources and Optimization of Biocatalyst Performance4.1 Accessing Biodiversity; 4.2 Creating Improved Biocatalysts; 4.2.1 Directed Evolution; 4.2.1.1 Methods to Create Mutant Libraries; 4.2.1.2 Assay Systems; 4.2.1.3 Selected Examples; 4.2.2 Focused Directed Evolution; 4.3 Catalytic Promiscuity in Hydrolases; 4.3.1 Reactions Involving Functional Group Analogs; 4.3.1.1 Perhydrolases; 4.3.2 Aldol and Michael additions Catalyzed by Hydrolases; 4.3.2.1 Aldol Additions; 4.3.2.2 Michael-Type Additions; 4.3.3 Modifications to Introduce New Reactivity in Hydrolases 4.3.3.1 Enantioselective Reduction of Hydroperoxides with Selenosubtilisin4.3.3.2 Vanadate-Modified Phosphatases as Peroxidases; 5 Lipases and Esterases; 5.1 Availability, Structures and Properties; 5.1.1 Lipases; 5.1.1.1 Classification of Lipases; 5.1.1.2 General Features of PPL, PCL, CRL, CAL-B, and RML; 5.1.2 Esterases; 5.1.3 Lipases and Esterases are α/β Hydrolases; 5.1.4 Lid or Flap in Interfacial Activation of Lipases; 5.1.5 Substrate Binding Site in Lipases and Esterases; 5.1.6 Designing Reactions with Lipases and Esterases; 5.1.6.1 Acyl Donor for Acylation Reactions 5.1.7 Assays for Lipases and Esterases5.1.7.1 Requirements for a Suitable Assay; 5.1.7.2 How to Distinguish Between Lipase, Esterase, and Protease; 5.2 Survey of Enantioselective Lipase-Catalyzed Reactions; 5.2.1 Alcohols; 5.2.1.1 Secondary Alcohols; 5.2.1.2 Primary Alcohols; 5.2.1.3 Other Alcohols, Amines, and Alcohol Analogs; 5.2.2 Carboxylic Acids; 5.2.2.1 General Considerations; 5.2.2.2 Carboxylic Acids with a Stereocenter at the α-Position; 5.2.2.3 Carboxylic Acids with a Stereocenter at the β-Position; 5.2.2.4 Other Carboxylic Acids; 5.2.2.5 Double Enantioselection; 5.2.2.6 Anhydrides 5.2.3 Lactones |
Record Nr. | UNINA-9910840613603321 |
Bornscheuer U. T (Uwe Theo), <1964->
![]() |
||
Weinheim, : Wiley-VCH | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|