Green Biocatalysis

 
 
John Wiley & Sons Inc (Verlag)
  • erschienen am 9. Mai 2016
  • |
  • 792 Seiten
 
E-Book | PDF mit Adobe DRM | Systemvoraussetzungen
978-1-118-82235-7 (ISBN)
 
Green Biocatalysis presents an exciting green technology that uses mild and safe processes with high regioselectivity and enantioselectivity. Bioprocesses are carried out under ambient temperature and atmospheric pressure in aqueous conditions that do not require any protection and deprotection steps to shorten the synthetic process, offering waste prevention and using renewable resources.
Drawing on the knowledge of over 70 internationally renowned experts in the field of biotechnology, Green Biocatalysis discusses a variety of case studies with emphases on process R&D and scale-up of enzymatic processes to catalyze different types of reactions. Random and directed evolution under process conditions to generate novel highly stable and active enzymes is described at length. This book features:
* A comprehensive review of green bioprocesses and application of enzymes in preparation of key compounds for pharmaceutical, fine chemical, agrochemical, cosmetic, flavor, and fragrance industries using diverse enzymatic reactions
* Discussion of the development of efficient and stable novel biocatalysts under process conditions by random and directed evolution and their applications for the development of environmentally friendly, efficient, economical, and sustainable green processes to get desired products in high yields and enantiopurity
* The most recent technological advances in enzymatic and microbial transformations and cuttingedge topics such as directed evolution by gene shuffling and enzyme engineering to improve biocatalysts
With over 3000 references and 800 figures, tables, equations, and drawings, Green Biocatalysis is an excellent resource for biochemists, organic chemists, medicinal chemists, chemical engineers, microbiologists, pharmaceutical chemists, and undergraduate and graduate students in the aforementioned disciplines.
1. Auflage
  • Englisch
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  • USA
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  • 28,57 MB
978-1-118-82235-7 (9781118822357)
1118822358 (1118822358)
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Ramesh N. Patel, Ph.D., has 44 years of experience in pharmaceutical and chemical industries. He obtained his Ph.D. in Biochemistry from the University of Texas, Austin, and completed an NIH and ACS Postdoctoral Research Fellowship in Biology from Yale University, New Haven. His professional experience includes working in Bristol-Myers Squibb and ExxonMobil Research and Engineering, where he has a record of achievements including over 175 original publications, 79 process patents, and over 113 invited/external presentations. Dr. Patel is the recipient of the 2004 Biotechnology Lifetime Achievement Award from the American Oil Chemists' Society, the 2008 Biocat Industrial Research Award from the International Congress on Biocatalysis, and the 2012 Distinction of Academic Award from the International Society of World Academy of Biocatalysis and Agricultural Biotechnology. Currently he is working as a consultant in Biocatalysis and Biotechnology.
  • Intro
  • Title Page
  • Copyright Page
  • Contents
  • Preface
  • About the Editor
  • Contributors
  • Chapter 1 Biocatalysis and Green Chemistry
  • 1.1 INTRODUCTION TO SUSTAINABLE DEVELOPMENT AND GREEN CHEMISTRY
  • 1.2 GREEN CHEMISTRY METRICS
  • 1.3 ENVIRONMENTAL IMPACT AND SUSTAINABILITY METRICS
  • 1.4 SOLVENTS
  • 1.5 THE ROLE OF CATALYSIS
  • 1.6 BIOCATALYSIS AND GREEN CHEMISTRY
  • 1.7 EXAMPLES OF GREEN BIOCATALYTIC PROCESSES
  • 1.7.1 A Chemoenzymatic Process for Pregabalin
  • 1.7.2 A Three-Enzyme Process for Atorvastatin Intermediate
  • 1.7.3 Enzymatic Synthesis of Sitagliptin
  • 1.7.4 Biocatalytic Synthesis of the Fragrance Chemical (-) Ambrox (Ambrafuran)
  • 1.8 CONCLUSIONS AND FUTURE PROSPECTS
  • REFERENCES
  • Chapter 2 Enzymatic Synthesis of Chiral Amines using ?-Transaminases, Amine Oxidases, and the Berberine Bridge Enzyme
  • 2.1 INTRODUCTION
  • 2.2 SYNTHESIS OF CHIRAL AMINES USING ?-TRANSAMINASES
  • 2.2.1 ?-Transaminases: Definition and General Facts
  • 2.2.2 Stereoselective Transformations Involving ?-TAs
  • 2.2.3 Asymmetric Amination of Ketones
  • 2.2.4 Asymmetric Amination of Linear Ketones
  • 2.2.5 Asymmetric Amination of Cyclic Ketones
  • 2.2.6 Application in the Synthesis of Pharmaceutically Active Ingredients
  • 2.2.7 Amination of Ketones in Organic Solvents
  • 2.2.8 Asymmetric Amination of Keto Acids: Synthesis of Nonnatural Amino Acids
  • 2.2.9 Amination of Aldehydes
  • 2.2.10 Cascade Reactions Involving ?-TAs
  • 2.2.11 Cascades Initiated by ?-TAs: Synthesis of Chiral Heterocycles
  • 2.2.12 Multienzyme Cascades Involving ?-TA-Catalyzed Amination of Ketones
  • 2.2.13 Deracemization of Primary Amines
  • 2.2.14 Perspective
  • 2.3 AMINE OXIDASES
  • 2.3.1 Amino Acid Oxidases
  • 2.3.2 Cascade Reactions Involving AAOs
  • 2.3.3 Monoamine Oxidases
  • 2.3.4 Cascade Reactions Involving Monoamine Oxidases
  • 2.3.5 Perspective
  • 2.4 BERBERINE BRIDGE ENZYMES
  • 2.5 CONCLUSIONS
  • REFERENCES
  • Chapter 3 Decarboxylation and Racemization of Unnatural Compounds using Artificial Enzymes Derived from Arylmalonate Decarboxylase
  • 3.1 INTRODUCTION
  • 3.2 DISCOVERY OF A BACTERIAL a-ARYL-a-METHYLMALONATE DECARBOXYLASE
  • 3.3 PURIFICATION AND CHARACTERIZATION OF THE DECARBOXYLASE (AMDase)
  • 3.4 CLONING OF THE AMDase GENE
  • 3.5 STEREOCHEMICAL COURSE OF AMDase-CATALYZED DECARBOXYLATION
  • 3.6 DIRECTED EVOLUTION OF AMDase TO AN ARTIFICIAL PROFEN RACEMASE
  • 3.7 INVERSION OF ENANTIOSELECTIVITY DRAMATICALLY IMPROVES CATALYTIC ACTIVITY
  • 3.8 FUTURE PROSPECTS
  • REFERENCES
  • Chapter 4 Green Processes for the Synthesis of Chiral Intermediates for the Development of Drugs
  • 4.1 INTRODUCTION
  • 4.2 SAXAGLIPTIN: ENZYMATIC SYNTHESIS OF (S)-N-BOC-3-HYDROXYADAMANTYLGLYCINE
  • 4.3 SITAGLIPTIN: ENZYMATIC SYNTHESIS OF CHIRAL AMINE
  • 4.4 VANLEV: ENZYMATIC SYNTHESIS OF (S)-6-HYDROXYNORLEUCINE
  • 4.5 VANLEV: ENZYMATIC SYNTHESIS OF ALLYSINE ETHYLENE ACETAL
  • 4.6 VANLEV: ENZYMATIC SYNTHESIS OF THIAZEPINE
  • 4.7 TIGEMONAM: ENZYMATIC SYNTHESIS OF (S)-ß-HYDROXYVALINE
  • 4.8 AUTOIMMUNE DISEASES: ENZYMATIC SYNTHESIS OF (S)-NEOPENTYLGLYCINE
  • 4.9 ATAZANAVIR: ENZYMATIC SYNTHESIS OF (S)-TERTIARY LEUCINE
  • 4.10 THROMBIN INHIBITOR (INOGATRAN): SYNTHESIS OF (R)-CYCLOHEXYLALANINE
  • 4.11 GAMMA SECRETASE INHIBITOR: ENZYMATIC SYNTHESIS OF (R)-5,5,5-TRIFLUORONORVALINE
  • 4.12 NK1/NK2 DUAL ANTAGONISTS: ENZYMATIC DESYMMETRIZATION OF DIETHYL 3-[3',4'-DICHLOROPHENYL] GLUTARATE
  • 4.13 PREGABALIN: ENZYMATIC SYNTHESIS OF ETHYL (S)-3-CYANO-5-METHYLHEXANOATE
  • 4.14 CHEMOKINE RECEPTOR MODULATOR: ENZYMATIC SYNTHESIS OF (1S,2R)-2-(METHOXYCARBONYL)CYCLOHEX- 4-ENE-1-CARBOXYLIC ACID
  • 4.15 ENZYMATIC SYNTHESIS OF (3S,5R)-3-(AMINOMETHYL)- 5-METHYLOCTANOIC ACID
  • 4.16 ATORVASTATIN (LIPITOR): ENZYMATIC DESYMMETRIZATION OF 3-HYDROXYGLUTARONITRILE
  • 4.17 ANTICANCER DRUGS: ENZYMATIC SYNTHESIS OF TAXANE SIDE CHAIN
  • 4.18 ANTIDIABETIC AND CNS DRUGS: ENZYMATIC HYDROLYSIS OF DIMETHYL BICYCLO[2.2.1]HEPTANE-1,4-DICARBOXYLATE
  • 4.19 CLOPIDOGREL (PLAVIX): ENZYMATIC PREPARATION OF 2-CHLOROMANDELIC ACID ESTERS
  • 4.20 aNTIVIRAL DRUG: REGIOSELECTIVE ENZYMATIC ACYLATION OF RIBAVIRIN
  • 4.21 ANTICHOLESTEROL DRUG: ENZYMATIC ACYLATION OF ALCOHOL
  • 4.22 SAXAGLIPTIN: ENZYMATIC SYNTHESIS OF (5S)-4,5-DIHYDRO-1H-PYRROLE-1,5 DICARBOXYLIC ACID, 1-(1,1-DIMETHYLETHYL)-5-ETHYL ESTER
  • 4.23 MONTELUKAST: SYNTHESIS OF INTERMEDIATE FOR LTD4 ANTAGONISTS
  • 4.24 ATAZANAVIR: ENZYMATIC SYNTHESIS OF (1S,2R)- [3-CHLORO-2-HYDROXY-1 (PHENYLMETHYL) PROPYL]-CARBAMIC ACID,1,1-DIMETHYL-ETHYL ESTER
  • 4.25 ATORVASTATIN: ENZYMATIC SYNTHESIS OF (R)-4-CYANO-3-HYDROXYBUTYRATE
  • 4.26 ANTIANXIETY DRUG: ENZYMATIC SYNTHESIS OF 6-HYDROXYBUSPIRONE
  • 4.27 PROTEASE INHIBITOR: ENZYMATIC SYNTHESIS OF (R)-3-(4-FLUOROPHENYL)-2-HYDROXY PROPIONIC ACID
  • 4.28 DERMATOLOGICAL AND ANTICANCER DRUGS: ENZYMATIC SYNTHESIS OF 2-(R)-HYDROXY-2-(1',2',3',4'-TETRAHYDRO-1',1',4',4'-TETRAMETHYL-6'-NAPHTHALENYL)ACETATE
  • 4.29 ANTIPSYCHOTIC DRUG: ENZYMATIC REDUCTION OF 1-(4-FLUOROPHENYL)4-[4-(5-FLUORO-2-PYRIMIDINYL) 1-PIPERAZINYL]-1-BUTANONE
  • 4.30 CHOLESTEROL-LOWERING AGENTS: ENZYMATIC SYNTHESIS OF (3S,5R)-DIHYDROXY-6-(BENZYLOXY) HEXANOIC ACID, ETHYL ESTER
  • 4.31 ANTIMIGRAINE DRUGS: ENZYMATIC SYNTHESIS OF (R)-2-AMINO-3-(7-METHYL-1H-INDAZOL-5-YL) PROPANOIC ACID
  • 4.32 ANTIDIABETIC DRUG (GLP-1 MIMICS): ENZYMATIC SYNTHESIS OF (S)-AMINO-3-[3-{6-(2-METHYLPHENYL)} PYRIDYL]-PROPIONIC ACID
  • 4.33 EPHEDRINE: SYNTHESIS OF (R)-PHENYLACETYLCARBINOL
  • 4.34 ZANAMIVIR: ENZYMATIC SYNTHESIS OF N-ACETYLNEURAMINIC ACID
  • 4.35 EPIVIR: ENZYMATIC DEAMINATION PROCESS FOR THE SYNTHESIS OF (2´R-CIS)-2´-DEOXY-3-THIACYTIDINE
  • 4.36 HMG-CoA REDUCTASE INHIBITORS: ALDOLASE-CATALYZED SYNTHESIS OF CHIRAL LACTOL
  • 4.37 BOCEPREVIR: OXIDATION OF 6,6-DIMETHYL-3-AZABICYCLO[3.1.0]HEXANE BY MONOAMINE OXIDASE
  • 4.38 CRIXIVAN: ENZYMATIC SYNTHESIS OF INDANDIOLS
  • 4.39 POTASSIUM CHANNEL OPENER: PREPARATION OF CHIRAL EPOXIDE AND TRANS-DIOL
  • 4.40 EPOTHILONES (ANTICANCER DRUGS): EPOTHILONE B AND EPOTHILONE F
  • 4.41 ß-ADRENERGIC BLOCKING AGENTS: SYNTHESIS OF INTERMEDIATES FOR PROPRANOLOL AND DENOPAMINE
  • 4.42 CONCLUSION
  • REFERENCES
  • Chapter 5 Dynamic Kinetic Resolution of Alcohols, Amines, and Amino Acids
  • 5.1 INTRODUCTION
  • 5.1.1 Kinetic and Dynamic Kinetic Resolution
  • 5.1.2 Enzymes as the Resolution Catalysts for DKR
  • 5.1.3 The Enantioselectivity of Enzymes in DKR
  • 5.1.4 Metal (Complexes) as the Racemization Catalysts for DKR
  • 5.2 DYNAMIC KINETIC RESOLUTION OF SECONDARY ALCOHOLS
  • 5.3 DYNAMIC KINETIC RESOLUTION OF AMINES AND AMINO ACIDS
  • 5.4 APPLICATIONS OF DYNAMIC KINETIC RESOLUTION
  • 5.5 SUMMARY
  • APPENDIX: LIST OF ABBREVIATIONS
  • REFERENCES
  • Chapter 6 Recent Developments in Flavin-Based Catalysis: Enzymatic Sulfoxidation
  • 6.1 INTRODUCTION
  • 6.2 ENZYMATIC SULFOXIDATION CATALYZED BY FLAVOPROTEIN OXIDASES
  • 6.3 USE OF FLAVOPROTEIN MONOOXYGENASES FOR THE SYNTHESIS OF CHIRAL SULFOXIDES
  • 6.3.1 Sulfoxidations Catalyzed by Baeyer-Villiger Monooxygenases
  • 6.3.2 Oxidative Processes Employing Styrene Monooxygenases
  • 6.3.3 Enzymatic Sulfoxidations Catalyzed by Flavin-Containing Monooxygenases
  • 6.4 ASYMMETRIC SULFOXIDATION USING FLAVINS AS CATALYSTS
  • 6.5 SUMMARY AND OUTLOOK
  • REFERENCES
  • Chapter 7 Development of Chemoenzymatic Processes: An Industrial Perspective
  • 7.1 INTRODUCTION
  • 7.2 SYNTHETIC ROUTE DESIGN AND INTEGRATION OF BIOCATALYSIS
  • 7.3 SCREENING AND BIOCATALYST SELECTION
  • 7.4 CHEMOENZYMATIC PROCESS DEVELOPMENT
  • 7.4.1 Reaction Engineering versus Enzyme Engineering
  • 7.4.2 Product Isolation
  • 7.4.3 Scale-Up of Enzymatic Processes
  • 7.4.4 Enzyme Supply Scenarios
  • 7.4.5 Manufacture of APIs using Enzymes: Quality and Safety Aspects
  • 7.5 CONCLUSIONS
  • REFERENCES
  • Chapter 8 Epoxide Hydrolases and their Application in Organic Synthesis
  • 8.1 INTRODUCTION
  • 8.2 SOURCES AND REACTION MECHANISM OF EHs
  • 8.2.1 Sources of EHs
  • 8.2.2 Heterologous Expression of EHs
  • 8.2.3 Reaction Mechanisms of EHs
  • 8.3 DIRECTED EVOLUTION AND GENETIC ENGINEERING OF EHs
  • 8.4 IMMOBILIZED EHs AND REACTIONS IN NONAQUEOUS MEDIA
  • 8.4.1 Immobilization of EHs
  • 8.4.2 EH-Catalyzed Reactions in Organic Solvent- or Ionic Liquid-Containing Media
  • 8.5 MONOFUNCTIONAL EPOXIDES AS CHIRAL BUILDING BLOCKS FOR THE SYNTHESIS OF BIOLOGICALLY ACTIVE COMPOUNDS
  • 8.5.1 Monosubstituted Aromatic Epoxides
  • 8.5.2 Disubstituted Aromatic Epoxides
  • 8.5.3 Nonaromatic Epoxides
  • 8.5.4 meso-Epoxides
  • 8.6 PREPARATION OF VALUABLE CHIRAL BUILDING BLOCKS FOR THE SYNTHESIS OF BIOLOGICALLY ACTIVE COMPOUNDS STARTING FROM BIFUNCTIONAL EPOXIDES
  • 8.6.1 Halogenated Epoxides
  • 8.6.2 Epoxyamide
  • 8.6.3 Protected Epoxy Alcohols
  • 8.6.4 Epoxy Ester
  • 8.6.5 Epoxy Aldehyde
  • 8.7 APPLICATION TO NATURAL PRODUCT SYNTHESIS
  • 8.7.1 Disparlure
  • 8.7.2 Linalool
  • 8.7.3 Bisabolol
  • 8.7.4 Frontalin
  • 8.7.5 Mevalonolactone
  • 8.7.6 Myrcenediol and Beer Aroma
  • 8.7.7 Pityol
  • 8.7.8 Pestalotin: Jamaican Rum Constituent
  • 8.7.9 Panaxytriol
  • 8.7.10 Fridamycin E
  • 8.8 BIENZYMATIC PROCESS IMPLYING ONE EPOXIDE HYDROLASE
  • 8.9 CONCLUSIONS
  • REFERENCES
  • Chapter 9 Enantioselective Acylation of Alcohol and Amine Reactions in Organic Synthesis
  • 9.1 INTRODUCTION
  • 9.1.1 General Considerations for Hydrolase-Catalyzed Reactions
  • 9.1.2 Serine Hydrolase Mechanism for the Acylation of Alcohols and Amines
  • 9.1.3 Use of Organic Solvents for Hydrolase-Catalyzed Acylation Reactions
  • 9.2 ENANTIOSELECTIVE ACYLATION OF ALCOHOLS
  • 9.2.1 Classical Kinetic Resolution of Racemic Alcohols
  • 9.2.2 Dynamic Kinetic Resolution of Racemic Alcohols
  • 9.2.3 Desymmetrization of Diols
  • 9.2.4 Selected Examples of Acylation Reaction with Interest for the Pharmaceutical Industry
  • 9.3 ACYLATION OF AMINES
  • 9.3.1 Kinetic Resolution of Racemic Amines
  • 9.3.2 Dynamic Kinetic Resolution of Racemic Amines
  • 9.3.3 Selected Examples of Acylation Reactions with Interest for the Pharmaceutical Industry
  • 9.4 CONCLUSIONS
  • REFERENCES
  • Chapter 10 Recent Advances in Enzyme-Catalyzed Aldol Addition Reactions
  • 10.1 INTRODUCTION
  • 10.2 PYRUVATE-DEPENDENT ALDOLASES
  • 10.2.1 N-Acetylneuraminic Acid Aldolase
  • 10.2.2 Other Pyruvate-Dependent Aldolases
  • 10.2.3 Structure-Guided Pyruvate Aldolase Modification
  • 10.3 DIHYDROXYACETONE PHOSPHATE (DHAP)-DEPENDENT ALDOLASES, d-FRUCTOSE-6-PHOSPHATE ALDOLASE (FSA) AND TRANSALDOLASES
  • 10.3.1 DHAP-Dependent Aldolases
  • 10.3.2 Iminocyclitol, Pipecolic Acids, Homoiminocyclitols, and Aminocyclitol Synthesis
  • 10.3.3 Synthesis of Polyhydroxylated Pipecolic Acids and Homoiminocyclitols
  • 10.3.4 Aminocyclitol Synthesis
  • 10.3.5 DHA-Utilizing Enzymes
  • 10.3.6 Iminocyclitol, Pipecolic Acid, Homoiminocyclitols, and Aminocyclitol Synthesis
  • 10.3.7 Carbohydrates, Deoxysugars, and Sugar Phosphate Synthesis
  • 10.4 THREONINE ALDOLASES
  • 10.4.1 2-Deoxy-d-Ribose 5-Phosphate Aldolase
  • 10.5 ALDOL TYPE REACTIONS CATALYZED BY NON-ALDOLASES
  • 10.6 COMPUTATIONAL DE NOVO ENZYME DESIGN
  • 10.7 CONCLUSIONS AND PERSPECTIVES
  • REFERENCES
  • Chapter 11 Enzymatic Asymmetric Reduction of Carbonyl Compounds
  • 11.1 INTRODUCTION
  • 11.2 MECHANISMS
  • 11.3 PREPARATION OF BIOCATALYSTS
  • 11.3.1 Screening of Enzymes from Culturable Microorganisms
  • 11.3.2 Screening of Enzymes using Metagenomes
  • 11.3.3 Screening of Enzymes of Microorganisms of Known Genome Data
  • 11.3.4 Mutation of Enzymes
  • 11.3.5 Hyperthermophilic Enzyme as a Biocatalyst
  • 11.3.6 Photosynthetic Organism as a Biocatalyst "Photobiocatalyst"
  • 11.4 SOLVENT ENGINEERING
  • 11.4.1 Organic Solvent
  • 11.4.2 CO2
  • 11.4.3 Ionic Liquid
  • 11.5 EXAMPLES FOR BIOCATALYTIC ASYMMETRIC REDUCTIONS
  • 11.5.1 Reduction of Ketones
  • 11.5.2 Reduction of Diketones
  • 11.5.3 Dynamic Kinetic Resolution Through Reduction
  • 11.6 CONCLUSIONS
  • REFERENCES
  • Chapter 12 Nitrile-Converting Enzymes and their Synthetic Applications
  • 12.1 INTRODUCTION
  • 12.2 SCREENING METHODOLOGY
  • 12.2.1 Screening Metagenomic Libraries
  • 12.2.2 Database Mining
  • 12.2.3 Construction of Enzyme Variants
  • 12.3 NITRILASES
  • 12.3.1 Arylacetonitrilases
  • 12.3.2 Aromatic Nitrilases
  • 12.3.3 Aliphatic Nitrilases
  • 12.3.4 Plant Nitrilases and their Bacterial Homologues
  • 12.4 NITRILE HYDRATASES
  • 12.4.1 Fe-type Nitrile Hydratase
  • 12.4.2 Co-type Nitrile Hydratase
  • 12.5 CONCLUSIONS
  • ACKNOWLEDGEMENTS
  • REFERENCES
  • Chapter 13 Biocatalytic Epoxidation for Green Synthesis
  • 13.1 INTRODUCTION
  • 13.2 ENZYMES FOR ASYMMETRIC EPOXIDATION
  • 13.2.1 Monooxygenases
  • 13.2.2 Chloroperoxidases
  • 13.3 APPLICATION OF BIOEPOXIDATION IN ORGANIC SYNTHESIS
  • 13.3.1 Asymmetric Epoxidation of Aliphatic Alkenes
  • 13.3.2 Asymmetric Epoxidation of Aromatic Alkenes
  • 13.4 PROTEIN ENGINEERING FOR BIOCATALYTIC EPOXIDATION REACTION
  • 13.4.1 Screening Methods
  • 13.4.2 Examples of Engineered Enzymes for Biocatalytic Epoxidation Reactions
  • 13.5 CONCLUSIONS AND OUTLOOK
  • ACKNOWLEDGMENTS
  • REFERENCES
  • Chapter 14 Dynamic Kinetic Resolution via Hydrolase-Metal Combo Catalysis
  • 14.1 INTRODUCTION
  • 14.2 DKR OF SECONDARY ALCOHOLS
  • 14.2.1 Racemization Catalysts for DKR of sec-Alcohols
  • 14.2.2 Synthetic Applications of the DKR of sec-Alcohols
  • 14.3 DKR OF AMINES
  • 14.3.1 Racemization Catalyst for the DKR of Amines
  • 14.3.2 Synthetic Applications of the DKR of Amines
  • 14.4 CONCLUSION
  • REFERENCES
  • Chapter 15 Discovery and Engineering of Enzymes for Peptide Synthesis and Activation
  • 15.1 INTRODUCTION
  • 15.2 CLASSIFICATION OF ENZYMES FOR PEPTIDE COUPLING
  • 15.3 SERINE AND CYSTEINE PROTEASES FOR PEPTIDE SYNTHESIS
  • 15.3.1 Chymotrypsin, Trypsin, and Related Enzymes
  • 15.3.2 Subtilisin-Like Enzymes
  • 15.3.3 Other Serine Hydrolases
  • 15.3.4 Aminopeptidases
  • 15.3.5 Peptidases Accepting ß-Amino Acids
  • 15.3.6 d-Amino Acid-Specific Peptidases
  • 15.3.7 Sulfhydryl Peptidases
  • 15.3.8 Sortase
  • 15.3.9 Metalloproteases in Peptide Synthesis
  • 15.3.10 Aspartic Proteases in Peptide Synthesis
  • 15.4 PROTEASE DISCOVERY
  • 15.4.1 Metagenomics
  • 15.4.2 Proteases from Thermophiles
  • 15.4.3 Solvent-Tolerant Proteases
  • 15.4.4 Proteases from Salt-Resistant Organisms
  • 15.5 PROTEASES ENGINEERED FOR IMPROVED SYNTHESIS
  • 15.5.1 Solvent-Resistant and Thermostable Subtilase Mutants
  • 15.5.2 Thermostable Thermolysin Variants
  • 15.5.3 Increasing Aminolysis to Hydrolysis Ratio by Protein Engineering
  • 15.5.4 Protein Engineering of Trypsin-Like Proteases
  • 15.5.5 Computational Design
  • 15.6 ENZYMES FOR PEPTIDE TERMINAL MODIFICATION
  • 15.6.1 Subtilisins for C-Terminal Peptide Modification
  • 15.6.2 C-Terminal Activation by Lipase
  • 15.6.3 Peptide Deformylase
  • 15.6.4 Peptide Amidases for C-Terminal Modification
  • 15.6.5 Enzymes for N-Terminal Modification
  • 15.6.6 Enzymes for Peptide Cyclization
  • 15.7 CONCLUSIONS
  • REFERENCES
  • Chapter 16 Biocatalysis for Drug Discovery and Development
  • 16.1 INTRODUCTION
  • 16.2 SINGLE ENZYMATIC REACTIONS
  • 16.2.1 Hydrolytic Reaction
  • 16.2.2 Reduction
  • 16.2.3 Oxidation
  • 16.2.4 C-C Bond-Forming Reaction
  • 16.2.5 Michael-Type Reaction
  • 16.2.6 Diels-Alder Reaction
  • 16.2.7 Pictet-Spengler Reaction
  • 16.2.8 Terpene Cyclization
  • 16.2.9 Transfer Reaction
  • 16.2.10 Fluorination
  • 16.2.11 Other Reactions
  • 16.2.12 Bifunctional Enzymes
  • 16.3 MULTIENZYME BIOCATALYTIC REACTIONS
  • 16.3.1 One-Pot Cascade Reactions
  • 16.3.2 Whole-Cell Biocatalysts
  • 16.3.3 Multistep Biocatalytic Conversions
  • 16.4 FUTURE PERSPECTIVE: BIOCATALYSTS FOR THE PHARMACEUTICAL INDUSTRY
  • 16.4.1 Biocatalyst Discovery: New Enzymes, New Chemistries
  • 16.4.2 Biocatalyst Development: Improvement of Desired Properties
  • 16.4.3 Integration of Biocatalytic Processes
  • 16.5 CONCLUSION
  • REFERENCES
  • Chapter 17 Application of Aromatic Hydrocarbon Dioxygenases
  • 17.1 INTRODUCTION
  • 17.2 CHALLENGES IN AROMATIC HYDROCARBON DIOXYGENASE APPLICATIONS
  • 17.3 PROTEIN ENGINEERING TO IMPROVE ENZYMATIC ACTIVITY AND ALTER SUBSTRATE SPECIFICITY
  • 17.4 PROTEIN ENGINEERING FOR THE PRODUCTION OF SPECIFIC CHEMICALS
  • 17.5 STRAIN MODIFICATION FOR THE DEVELOPMENT OF NEW BIODEGRADATION PATHWAYS
  • 17.6 PHYTOREMEDIATION: THE EXPRESSION OF BACTERIAL DIOXYGENASES IN PLANT SYSTEMS FOR BIOREMEDIATION PURPOSES
  • 17.7 CONCLUDING REMARKS
  • ACKNOWLEDGMENTS
  • REFERENCES
  • Chapter 18 Ene-reductases and their Applications
  • 18.1 INTRODUCTION
  • 18.2 SUBSTRATE CLASSES AND INDUSTRIAL APPLICATIONS
  • 18.3 MULTIENZYME REACTIONS
  • 18.4 ALTERNATIVE HYDRIDE SOURCES
  • 18.5 IMPROVEMENTS OF PRODUCTIVITY, STEREOSELECTIVITY, AND/OR CONVERSION
  • REFERENCES
  • Chapter 19 Recent Developments in Aminopeptidases, Racemases, and Oxidases
  • 19.1 AMINOPEPTIDASE
  • 19.1.1 Discovery of d-Stereospecific Aminopeptidase and its Utilization for Dynamic Kinetic Resolution
  • 19.1.2 Discovery of d-Aminopeptidase, d-Amino Acid Amidase, and Alkaline d-Peptidase
  • 19.1.3 Structure of d-Aminopeptidase (DAP)
  • 19.1.4 Structure of d-Amino Acid Amidase (DaaA)
  • 19.2 RACEMASE
  • 19.2.1 Synthesis of d-Amino Acids by Optical Resolution and Dynamic Kinetic Resolution
  • 19.2.2 Structure of ACL Racemase
  • 19.2.3 In Silico Identification of ACL Racemases
  • 19.3 AMINO ACID OXIDASE
  • 19.3.1 Development of Novel R-Stereoselective Amine Oxidase
  • 19.3.2 Design of R-Stereoselective Amine Oxidase
  • 19.3.3 Deracemization Reaction with R-Stereoselective AOx
  • 19.3.4 Structure of the Mutant Porcine Kidney d-Amino Acid Oxidase (Y228L, R283G)
  • REFERENCES
  • Chapter 20 Biocatalytic Cascades for API Synthesis
  • 20.1 INTRODUCTION
  • 20.2 MULTIENZYMATIC BIOCATALYSIS
  • 20.2.1 Rationale
  • 20.2.2 Biocatalytic Cascade Concepts
  • 20.3 PROCESS ASPECTS FOR MULTISTEP BIOCATALYSIS
  • 20.3.1 Balancing Reaction Schemes
  • 20.3.2 Biocatalytic Reactor Options
  • 20.3.3 Process Intensification
  • 20.3.4 Continuous Processes
  • 20.3.5 Process Integration
  • 20.4 PROCESS DEVELOPMENT
  • 20.5 BIOCATALYTIC CASCADE EXAMPLES
  • 20.5.1 Linear Cascades
  • 20.5.2 Parallel Cascades
  • 20.5.3 Cyclic Cascades
  • 20.5.4 Orthogonal Cascades
  • 20.5.5 Linear-Parallel
  • 20.5.6 Linear-Cyclic
  • 20.5.7 Complex Cascades
  • 20.5.8 Convergent Parallel Cascade
  • 20.6 FUTURE OUTLOOK
  • 20.6.1 Protein Engineering
  • 20.6.2 Flow Chemistry and Process Intensification
  • REFERENCES
  • Chapter 21 Yeast-Mediated Stereoselective Synthesis
  • 21.1 INTRODUCTION
  • 21.2 REDUCTIONS OF ALDEHYDES AND KETONES
  • 21.3 REDUCTION OF THIOCARBONYLS OR SULFUR-CONTAINING COMPOUNDS
  • 21.4 REDUCTION OF FUNCTIONALIZED CARBONYL AND DICARBONYL COMPOUNDS
  • 21.5 REDUCTION OF KETO ESTERS
  • 21.6 HYDROLYSIS OF ESTERS
  • 21.7 IMMOBILIZED BAKER'S YEAST
  • 21.8 WHOLE-CELL BIOCATALYSIS IN IONIC LIQUIDS AND DEEP EUTECTIC SOLVENTS
  • 21.9 C-C BOND-FORMING AND BREAKING REACTIONS
  • 21.10 MISCELLANEOUS REACTIONS
  • 21.11 CONCLUSIONS
  • REFERENCES
  • Chapter 22 Biocatalytic Introduction of Chiral Hydroxy Groups using Oxygenases and Hydratases
  • 22.1 INTRODUCTION
  • 22.2 REGIO- AND STEREOSELECTIVE HYDROXYLATION OF PROPYLBENZENE AND 3-CHLOROSTYRENE BY CYTOCHROME P450 BM-3 AND ITS MUTANT
  • 22.3 REGIO- AND STEREOSELECTIVE HYDROXYLATION OF ALIPHATIC AMINO ACIDS BY FE(II)/a-KETOGLUTARATE-DEPENDENT DIOXYGENASES
  • 22.3.1 l-Isoleucine 4-Hydroxylase
  • 22.3.2 Fe/aKG-DOs Closely Homologous with l-Isoleucine 4-Hydroxylase
  • 22.3.3 l-Leucine 5-Hydroxylase
  • 22.3.4 N-Succinyl l-Leucine 3-Hydroxylase
  • 22.3.5 Catalytic Properties of the Aliphatic Amino Acid Hydroxylases
  • 22.3.6 Practical Use of Fe(II)/a-Ketoglutarate-Dependent Dioxygenases Coupled with Cosubstrate Generation System
  • 22.4 REGIO- AND STEREOSELECTIVE HYDRATION OF UNSATURATED FATTY ACIDS BY A NOVEL FATTY ACID HYDRATASE
  • 22.4.1 Linoleic Acid ?9 Hydratase
  • 22.4.2 Efficient Enzymatic Production of Hydroxy Fatty Acids by Linoleic Acid ?9 Hydratase
  • 22.5 CONCLUSION
  • ACKNOWLEDGMENT
  • REFERENCES
  • Chapter 23 Asymmetric Synthesis with Recombinant Whole-Cell Catalysts
  • 23.1 INTRODUCTION
  • 23.2 THE DESIGN/CONSTRUCTION OF WHOLE-CELL CATALYSTS
  • 23.3 BIOTRANSFORMATIONS WITH WHOLE-CELL CATALYSTS
  • 23.3.1 Hydrolysis Reactions
  • 23.3.2 Hydration and Dehydration Reactions
  • 23.3.3 C-C Bond-Forming Reactions
  • 23.3.4 Reduction Reactions
  • 23.3.5 Oxidation Reactions
  • 23.4 CONCLUSION
  • REFERENCES
  • Chapter 24 Lipases and Esterases as User-Friendly Biocatalysts in Natural Product Synthesis
  • 24.1 INTRODUCTION
  • 24.2 DESYMMETRIZATION OF PROCHIRAL OR meso-DIOLS AND DIACETATES
  • 24.2.1 Desymmetrization of meso-Compounds with 1,2-Stereogenic Centers
  • 24.2.2 Desymmetrization of meso-Compounds with 1,3- and 1,5-Stereogenic Centers
  • 24.2.3 Desymmetrization of Prochiral Compounds with a Single Stereogenic Center
  • 24.3 KINETIC RESOLUTION OF RACEMIC ALCOHOLS
  • 24.3.1 Kinetic Resolution of (±)-Primary Alcohols
  • 24.3.2 Kinetic Resolution of Acyclic (±)-Secondary Alcohols
  • 24.3.3 Kinetic Resolution of Cyclic (±)-Secondary Alcohols
  • 24.4 PREPARATION OF ENANTIOPURE INTERMEDIATE(S) FROM A MIXTURE OF STEREOISOMERS
  • 24.4.1 (1S,4R)-4-t-Butyldimethylsilyloxy-3-Chloro-2-Cyclopenten-1-ol (54)
  • 24.4.2 (4R,5S)-5-Hydroxy-4-Methyl-3-Hexanone (55)
  • 24.4.3 (3R,14R,26R)-3,26-Diacetoxy-14-Methyl-1,2-bis(trimethylsilyl)octacosa-4,24-Diene-1,27-Diyne (60)
  • 24.5 CONCLUSION
  • ACKNOWLEDGMENTS
  • REFERENCES
  • Chapter 25 Hydroxynitrile Lyases for Biocatalytic Synthesis of Chiral Cyanohydrins
  • 25.1 INTRODUCTION
  • 25.2 DISCOVERY OF HYDROXYNITRILE LYASES: BIOPROSPECTING
  • 25.2.1 Screening Plants Based on Detection of Activity
  • 25.2.2 Isolation of HNL Proteins and Identification of the Encoding Genes
  • 25.2.3 Database Mining
  • 25.2.4 Heterologous Expression
  • 25.3 APPLICATIONS OF HYDROXYNITRILE LYASES
  • 25.3.1 Cyanohydrins
  • 25.3.2 ß-Nitro Alcohols
  • 25.4 STRUCTURAL AND MECHANISTIC ASPECTS
  • 25.5 ENGINEERING OF HYDROXYNITRILE LYASES
  • 25.5.1 Substrate Scope, Activity, and Enantioselectivity
  • 25.5.2 Stability
  • 25.5.3 Expression
  • 25.5.4 New Catalytic Activities
  • 25.6 REACTION ENGINEERING AND REACTION SYSTEMS
  • 25.6.1 Reaction Systems
  • 25.6.2 Immobilization of HNLs
  • 25.7 CONCLUSION
  • ACKNOWLEDGMENT
  • REFERENCES
  • Chapter 26 Biocatalysis: Nitrilases in Organic Synthesis
  • 26.1 INTRODUCTION
  • 26.2 NITRILASE DISCOVERY
  • 26.2.1 Conventional Screening
  • 26.2.2 Metagenomic Mining
  • 26.2.3 Genome Mining
  • 26.3 NITRILASE IMPROVEMENT
  • 26.3.1 Culture Optimization
  • 26.3.2 Nitrilase Reengineering
  • 26.4 APPLICATIONS IN ORGANIC SYNTHESIS
  • 26.4.1 Production of Glycolic Acid
  • 26.4.2 Production of Iminodiacetic Acid
  • 26.4.3 Production of Indole-3-Acetic Acid
  • 26.4.4 Conversion of Phenylacetonitrile and its Derivates
  • 26.4.5 Regioselective Hydrolysis of Dinitriles
  • 26.4.6 Degradation of Benzonitrile Herbicides
  • 26.5 CONCLUSIONS AND FUTURE PROSPECTS
  • ACKNOWLEDGMENTS
  • REFERENCES
  • Chapter 27 Biotechnology for the Production of Chemicals, Intermediates, and Pharmaceutical Ingredients
  • 27.1 INTRODUCTION
  • 27.2 VALUE CHAINS AND MARKETS
  • 27.2.1 Pharmaceuticals
  • 27.2.2 Medical Technology (MedTech)
  • 27.2.3 Food and Feed
  • 27.2.4 Flavor and Fragrance
  • 27.2.5 Cosmetics and Personal Care
  • 27.2.6 Polymers
  • 27.2.7 Surfactants and Lubricants
  • 27.2.8 Commodity Chemicals
  • 27.2.9 Energy
  • 27.2.10 Other Markets and Products
  • 27.3 THE TOOLBOX
  • 27.3.1 The Current Toolbox
  • 27.3.2 The Future Toolbox
  • 27.4 SUSTAINABILITY, GREEN PREMIUM PRICING, AND SUBSIDIES
  • 27.5 REGULATORY ASPECTS AND PUBLIC PERCEPTION
  • 27.6 INNOVATION (NOT ONLY IN THE LABORATORY!)
  • 27.7 CONCLUSIONS
  • ACKNOWLEDGMENTS
  • REFERENCES
  • Chapter 28 Microbial Transformations of Pentacyclic Triterpenes
  • 28.1 INTRODUCTION
  • 28.2 TYPICAL BIOTRANSFORMATIONS IN THE LUPANE FAMILY
  • 28.3 TYPICAL BIOTRANSFORMATIONS IN THE OLEANE FAMILY
  • 28.4 TYPICAL BIOTRANSFORMATIONS IN THE URSANE FAMILY
  • 28.5 MICROBIAL TRANSFORMATIONS OF OTHER PTs
  • 28.6 GLYCOSYLATIONS AND DEGLYCOSYLATIONs
  • 28.7 CONCLUSION AND PERSPECTIVES
  • REFERENCES
  • Chapter 29 Transaminases and their Applications
  • 29.1 INTRODUCTION
  • 29.2 GENERAL PROPERTIES OF TRANSAMINASES
  • 29.2.1 Classification as Pyridoxal-5'-Phosphate-Dependent Enzymes
  • 29.2.2 Classification Based on Substrate Scope
  • 29.2.3 Reaction Mechanism
  • 29.2.4 Enantioselectivity of Transaminases
  • 29.3 SYNTHESIS STRATEGIES WITH TRANSAMINASES
  • 29.3.1 Synthesis of Chiral Amines
  • 29.3.2 Synthesis of Canonical and Noncanonical Amino Acids
  • 29.3.3 Synthesis of ß-Amino Acids
  • 29.3.4 Synthesis of Amino Alcohols
  • 29.3.5 Transaminase-Catalyzed Reactions with Whole Cells
  • 29.4 APPROACHES TO OPTIMIZE THE TRANSAMINASE-CATALYZED REACTIONS
  • 29.4.1 Protein Engineering by Rational Enzyme Design
  • 29.4.2 Protein Engineering by Directed Evolution
  • 29.4.3 Immobilization of Transaminases
  • 29.4.4 Process Development: A Fast Way to Identify Appropriate Transaminases
  • 29.4.5 ?-Transaminases in Organic Solvents
  • 29.5 CONCLUSION
  • REFERENCES
  • Index
  • EULA

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