{"product_id":"green-biocatalysis-isbn-9781118822296","title":"Green Biocatalysis","description":"\u003cp\u003e\u003ci\u003eGreen Biocatalysis\u003c\/i\u003e 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.\u003c\/p\u003e \u003cp\u003eDrawing on the knowledge of over 70 internationally renowned experts in the field of biotechnology, \u003ci\u003eGreen Biocatalysis\u003c\/i\u003e discusses a variety of case studies with emphases on process R\u0026amp;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: \u003c\/p\u003e \u003cul\u003e \u003cli\u003eA 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\u003c\/li\u003e \u003cli\u003eDiscussion 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\u003c\/li\u003e \u003cli\u003eThe 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\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003e With over 3000 references and 800 figures, tables, equations, and drawings, \u003ci\u003eGreen Biocatalysis\u003c\/i\u003e is an excellent resource for biochemists, organic chemists, medicinal chemists, chemical engineers, microbiologists, pharmaceutical chemists, and undergraduate and graduate students in the aforementioned disciplines.\u003c\/p\u003e Preface xix \u003cp\u003eAbout the Editor xxiii\u003c\/p\u003e \u003cp\u003eContributors xxv\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 1 Biocatalysis and Green Chemistry 1\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRoger A. Sheldon\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction to Sustainable Development and Green Chemistry 1\u003c\/p\u003e \u003cp\u003e1.2 Green Chemistry Metrics 2\u003c\/p\u003e \u003cp\u003e1.3 Environmental Impact and Sustainability Metrics 4\u003c\/p\u003e \u003cp\u003e1.4 Solvents 5\u003c\/p\u003e \u003cp\u003e1.5 The Role of Catalysis 6\u003c\/p\u003e \u003cp\u003e1.6 Biocatalysis and Green Chemistry 6\u003c\/p\u003e \u003cp\u003e1.7 Examples of Green Biocatalytic Processes 8\u003c\/p\u003e \u003cp\u003e1.8 Conclusions and Future Prospects 13\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 2 Enzymatic Synthesis of Chiral Amines using ω-Transaminases, Amine Oxidases, and the Berberine Bridge Enzyme 17\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eEduardo Busto, Robert C. Simon, Nina Richter, and Wolfgang Kroutil\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 17\u003c\/p\u003e \u003cp\u003e2.2 Synthesis of Chiral Amines using ω]Transaminases 18\u003c\/p\u003e \u003cp\u003e2.3 Amine Oxidases 34\u003c\/p\u003e \u003cp\u003e2.4 Berberine Bridge Enzymes 50\u003c\/p\u003e \u003cp\u003e2.5 Conclusions 52\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 3 Decarboxylation and Racemization of Unnatural Compounds using Artificial Enzymes Derived from Arylmalonate Decarboxylase 59\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eKenji Miyamoto\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 59\u003c\/p\u003e \u003cp\u003e3.2 Discovery of a Bacterial α]Aryl]α]Methylmalonate Decarboxylase 61\u003c\/p\u003e \u003cp\u003e3.3 Purification and Characterization of the Decarboxylase (Amdase) 61\u003c\/p\u003e \u003cp\u003e3.4 Cloning of the Amdase Gene 62\u003c\/p\u003e \u003cp\u003e3.5 Stereochemical Course of Amdase]Catalyzed Decarboxylation 62\u003c\/p\u003e \u003cp\u003e3.6 Directed Evolution of Amdase to an Artificial Profen Racemase 63\u003c\/p\u003e \u003cp\u003e3.7 Inversion of Enantioselectivity Dramatically Improves Catalytic Activity 65\u003c\/p\u003e \u003cp\u003e3.8 Future Prospects 68\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 4 Green Processes for the Synthesis of Chiral Intermediates for the Development of Drugs 71\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRamesh N. Patel\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction 71\u003c\/p\u003e \u003cp\u003e4.2 Saxagliptin: Enzymatic Synthesis of (S)]N]Boc]3]Hydroxyadamantylglycine 71\u003c\/p\u003e \u003cp\u003e4.3 Sitagliptin: Enzymatic Synthesis of Chiral Amine 72\u003c\/p\u003e \u003cp\u003e4.4 Vanlev: Enzymatic Synthesis of (S)]6]Hydroxynorleucine 73\u003c\/p\u003e \u003cp\u003e4.5 Vanlev: Enzymatic Synthesis of Allysine Ethylene Acetal 74\u003c\/p\u003e \u003cp\u003e4.6 Vanlev: Enzymatic Synthesis of Thiazepine 74\u003c\/p\u003e \u003cp\u003e4.7 Tigemonam: Enzymatic Synthesis of (S)]β]Hydroxyvaline 76\u003c\/p\u003e \u003cp\u003e4.8 Autoimmune Diseases: Enzymatic Synthesis of (S)]Neopentylglycine 76\u003c\/p\u003e \u003cp\u003e4.9 Atazanavir: Enzymatic Synthesis of (S)]Tertiary Leucine 77\u003c\/p\u003e \u003cp\u003e4.10 Thrombin Inhibitor (Inogatran): Synthesis of (R)]Cyclohexylalanine 78\u003c\/p\u003e \u003cp\u003e4.11 Gamma Secretase Inhibitor: Enzymatic Synthesis of (R)]5,5,5]Trifluoronorvaline 79\u003c\/p\u003e \u003cp\u003e4.12 NK1\/NK2 Dual Antagonists: Enzymatic Desymmetrization of Diethyl 3][3′,4′]Dichlorophenyl] Glutarate 80\u003c\/p\u003e \u003cp\u003e4.13 Pregabalin: Enzymatic Synthesis of Ethyl (S)]3]Cyano]5]Methylhexanoate 81\u003c\/p\u003e \u003cp\u003e4.14 Chemokine Receptor Modulator: Enzymatic Synthesis of (1S,2R)]2](Methoxycarbonyl)-Cyclohex]4]ene]1]Carboxylic Acid 82\u003c\/p\u003e \u003cp\u003e4.15 Enzymatic Synthesis of (3S,5R)]3](Aminomethyl)]5]Methyloctanoic Acid 82\u003c\/p\u003e \u003cp\u003e4.16 Atorvastatin (Lipitor): Enzymatic Desymmetrization of 3]Hydroxyglutaronitrile 83\u003c\/p\u003e \u003cp\u003e4.17 Anticancer Drugs: Enzymatic Synthesis of Taxane Side Chain 84\u003c\/p\u003e \u003cp\u003e4.18 Antidiabetic and CNS Drugs: Enzymatic Hydrolysis of Dimethyl Bicyclo[2.2.1] Heptane]1,4]Dicarboxylate 85\u003c\/p\u003e \u003cp\u003e4.19 Clopidogrel (Plavix): Enzymatic Preparation of 2]Chloromandelic Acid Esters 85\u003c\/p\u003e \u003cp\u003e4.20 Antiviral Drug: Regioselective Enzymatic Acylation of Ribavirin 86\u003c\/p\u003e \u003cp\u003e4.21 Anticholesterol Drug: Enzymatic Acylation of Alcohol 87\u003c\/p\u003e \u003cp\u003e4.22 Saxagliptin: Enzymatic Synthesis of (5S)]4,5]Dihydro]1H]Pyrrole]1,5 Dicarboxylic Acid, 1](1,1]Dimethylethyl)]5]Ethyl Ester 88\u003c\/p\u003e \u003cp\u003e4.23 Montelukast: Synthesis of Intermediate for LTD4 Antagonists 89\u003c\/p\u003e \u003cp\u003e4.24 Atazanavir: Enzymatic Synthesis of (1S,2R)][3]Chloro]2]Hydroxy]1 (Phenylmethyl) Propyl]]Carbamic Acid,1,1]Dimethyl]Ethyl Ester 90\u003c\/p\u003e \u003cp\u003e4.25 Atorvastatin: Enzymatic Synthesis of (R)]4]Cyano]3]Hydroxybutyrate 91\u003c\/p\u003e \u003cp\u003e4.26 Antianxiety Drug: Enzymatic Synthesis of 6]Hydroxybuspirone 92\u003c\/p\u003e \u003cp\u003e4.27 Protease Inhibitor: Enzymatic Synthesis of (R)]3](4]Fluorophenyl)]2]Hydroxy Propionic Acid 93\u003c\/p\u003e \u003cp\u003e4.28 Dermatological and Anticancer Drugs: Enzymatic Synthesis of 2](R)]Hydroxy]2](1′,2′,3′, 4′]Tetrahydro]1′,1′,4′,4′]Tetramethyl]6′]Naphthalenyl) Acetate 94\u003c\/p\u003e \u003cp\u003e4.29 Antipsychotic Drug: Enzymatic Reduction of 1](4]Fluorophenyl)4][4](5]Fluoro]2]Pyrimidinyl)1]Piperazinyl]]1]Butanone 95\u003c\/p\u003e \u003cp\u003e4.30 Cholesterol]Lowering Agents: Enzymatic Synthesis of (3S,5R)]Dihydroxy]6](Benzyloxy) Hexanoic Acid, Ethyl Ester 95\u003c\/p\u003e \u003cp\u003e4.31 Antimigraine Drugs: Enzymatic Synthesis of (R)]2]Amino]3](7]Methyl]1H]Indazol]5]yl) Propanoic Acid 96\u003c\/p\u003e \u003cp\u003e4.32 Antidiabetic Drug (GLP]1 Mimics): Enzymatic Synthesis of (S)]Amino]3][3]{6](2]Methylphenyl)} Pyridyl]]Propionic Acid 97\u003c\/p\u003e \u003cp\u003e4.33 Ephedrine: Synthesis of (R)]Phenylacetylcarbinol 98\u003c\/p\u003e \u003cp\u003e4.34 Zanamivir: Enzymatic Synthesis of N]Acetylneuraminic Acid 99\u003c\/p\u003e \u003cp\u003e4.35 Epivir: Enzymatic Deamination Process for the Synthesis of (2′R]cis)]2′]Deoxy]3]Thiacytidine 100\u003c\/p\u003e \u003cp\u003e4.36 HMG]CoA Reductase Inhibitors: Aldolase]Catalyzed Synthesis of Chiral Lactol 101\u003c\/p\u003e \u003cp\u003e4.37 Boceprevir: Oxidation of 6,6]Dimethyl]3]Azabicyclo[3.1.0]Hexane by Monoamine Oxidase 102\u003c\/p\u003e \u003cp\u003e4.38 Crixivan: Enzymatic Synthesis of Indandiols 103\u003c\/p\u003e \u003cp\u003e4.39 Potassium Channel Opener: Preparation of Chiral Epoxide and trans]Diol 104\u003c\/p\u003e \u003cp\u003e4.40 Epothilones (Anticancer Drugs): Epothilone B and Epothilone F 105\u003c\/p\u003e \u003cp\u003e4.41 β]Adrenergic Blocking Agents: Synthesis of Intermediates for Propranolol and Denopamine 106\u003c\/p\u003e \u003cp\u003e4.42 Conclusion 106\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 5 Dynamic Kinetic Resolution of Alcohols, Amines, and Amino Acids 115\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJusuk Lee, Yoon Kyung Choi, Jaiwook Park, and Mahn]Joo Kim\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction 115\u003c\/p\u003e \u003cp\u003e5.2 Dynamic Kinetic Resolution of Secondary Alcohols 119\u003c\/p\u003e \u003cp\u003e5.3 Dynamic Kinetic Resolution of Amines and Amino Acids 133\u003c\/p\u003e \u003cp\u003e5.4 Applications of Dynamic Kinetic Resolution 139\u003c\/p\u003e \u003cp\u003e5.5 Summary 145\u003c\/p\u003e \u003cp\u003eAppendix: List of Abbreviations 145\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 6 Recent Developments in Flavin-Based Catalysis: Enzymatic Sulfoxidation 149\u003c\/b\u003e\u003cbr\u003e\u003ci\u003ePatricia B. Brondani, Marco W. Fraaije, and Gonzalo de Gonzalo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction 149\u003c\/p\u003e \u003cp\u003e6.2 Enzymatic Sulfoxidation Catalyzed by Flavoprotein Oxidases 150\u003c\/p\u003e \u003cp\u003e6.3 Use of Flavoprotein Monooxygenases for the Synthesis of Chiral Sulfoxides 151\u003c\/p\u003e \u003cp\u003e6.4 Asymmetric Sulfoxidation using Flavins as Catalysts 160\u003c\/p\u003e \u003cp\u003e6.5 Summary and Outlook 162\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 7 Development of Chemoenzymatic Processes: An Industrial Perspective 165\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRajesh Kumar, Carlos Martinez, Van Martin, and John Wong\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 165\u003c\/p\u003e \u003cp\u003e7.2 Synthetic Route Design and Integration of Biocatalysis 166\u003c\/p\u003e \u003cp\u003e7.3 Screening and Biocatalyst Selection 169\u003c\/p\u003e \u003cp\u003e7.4 Chemoenzymatic Process Development 169\u003c\/p\u003e \u003cp\u003e7.5 Conclusions 176\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 8 Epoxide Hydrolases and their Application in Organic Synthesis 179\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eAlain Archelas, Gilles Iacazio, and Michael Kotik\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 179\u003c\/p\u003e \u003cp\u003e8.2 Sources and Reaction Mechanism of EHs 181\u003c\/p\u003e \u003cp\u003e8.3 Directed Evolution and Genetic Engineering of EHs 183\u003c\/p\u003e \u003cp\u003e8.4 Immobilized EHs and Reactions in Nonaqueous Media 186\u003c\/p\u003e \u003cp\u003e8.5 Monofunctional Epoxides as Chiral Building Blocks for the Synthesis of Biologically Active Compounds 188\u003c\/p\u003e \u003cp\u003e8.6 Preparation of Valuable Chiral Building Blocks for the Synthesis of Biologically Active Compounds Starting from Bifunctional Epoxides 204\u003c\/p\u003e \u003cp\u003e8.7 Application to Natural Product Synthesis 210\u003c\/p\u003e \u003cp\u003e8.8 Bienzymatic Process Implying One Epoxide Hydrolase 216\u003c\/p\u003e \u003cp\u003e8.9 Conclusions 219\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 9 Enantioselective Acylation of Alcohol and Amine Reactions in Organic Synthesis 231\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eVicente Gotor]Fernández and Vicente Gotor\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction 231\u003c\/p\u003e \u003cp\u003e9.2 Enantioselective Acylation of Alcohols 234\u003c\/p\u003e \u003cp\u003e9.3 Acylation of Amines 248\u003c\/p\u003e \u003cp\u003e9.4 Conclusions 260\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 10 Recent Advances in Enzyme-Catalyzed Aldol Addition Reactions 267\u003c\/b\u003e\u003cbr\u003e\u003ci\u003ePere Clapés\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction 267\u003c\/p\u003e \u003cp\u003e10.2 Pyruvate-Dependent Aldolases 269\u003c\/p\u003e \u003cp\u003e10.3 Dihydroxyacetone Phosphate (DHAP)-Dependent Aldolases, d-Fructose-6-Phosphate Aldolase (FSA) and Transaldolases 276\u003c\/p\u003e \u003cp\u003e10.4 Threonine Aldolases 287\u003c\/p\u003e \u003cp\u003e10.5 Aldol Type Reactions Catalyzed by Non]Aldolases 293\u003c\/p\u003e \u003cp\u003e10.6 Computational De Novo Enzyme Design 294\u003c\/p\u003e \u003cp\u003e10.7 Conclusions and Perspectives 295\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 11 Enzymatic Asymmetric Reduction of Carbonyl Compounds 307\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eTomoko Matsuda, Rio Yamanaka, and Kaoru Nakamura\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 307\u003c\/p\u003e \u003cp\u003e11.2 Mechanisms 307\u003c\/p\u003e \u003cp\u003e11.3 Preparation of Biocatalysts 309\u003c\/p\u003e \u003cp\u003e11.4 Solvent Engineering 316\u003c\/p\u003e \u003cp\u003e11.5 Examples for Biocatalytic Asymmetric Reductions 317\u003c\/p\u003e \u003cp\u003e11.6 Conclusions 325\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 12 Nitrile]Converting Enzymes and their Synthetic Applications 331\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eLudmila Martínková\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction 331\u003c\/p\u003e \u003cp\u003e12.2 Screening Methodology 332\u003c\/p\u003e \u003cp\u003e12.3 Nitrilases 333\u003c\/p\u003e \u003cp\u003e12.4 Nitrile Hydratases 340\u003c\/p\u003e \u003cp\u003e12.5 Conclusions 343\u003c\/p\u003e \u003cp\u003eAcknowledgements 343\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 13 Biocatalytic Epoxidation for Green Synthesis 351\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eHui Lin, Meng]Yu Xu, Yan Liu, and Zhong]Liu Wu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction 351\u003c\/p\u003e \u003cp\u003e13.2 Enzymes for Asymmetric Epoxidation 352\u003c\/p\u003e \u003cp\u003e13.3 Application of Bioepoxidation in Organic Synthesis 354\u003c\/p\u003e \u003cp\u003e13.4 Protein Engineering for Biocatalytic Epoxidation Reaction 362\u003c\/p\u003e \u003cp\u003e13.5 Conclusions and Outlook 367\u003c\/p\u003e \u003cp\u003eAcknowledgments 368\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 14 Dynamic Kinetic Resolution via Hydrolase–Metal Combo Catalysis 373\u003c\/b\u003e\u003cbr\u003e\u003ci\u003ePilar Hoyos, Vittorio Pace, María J. Hernáiz, and Andrés R. Alcántara\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Introduction 373\u003c\/p\u003e \u003cp\u003e14.2 DKR of Secondary Alcohols 374\u003c\/p\u003e \u003cp\u003e14.3 DKR of Amines 386\u003c\/p\u003e \u003cp\u003e14.4 Conclusion 391\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 15 Discovery and Engineering of Enzymes for Peptide Synthesis and Activation 397\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eAna Toplak, Muhammad I. Arif, Bian Wu, and Dick B. Janssen\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Introduction 397\u003c\/p\u003e \u003cp\u003e15.2 Classification of Enzymes for Peptide Coupling 399\u003c\/p\u003e \u003cp\u003e15.3 Serine and Cysteine Proteases for Peptide Synthesis 402\u003c\/p\u003e \u003cp\u003e15.4 Protease Discovery 409\u003c\/p\u003e \u003cp\u003e15.5 Proteases Engineered for Improved Synthesis 410\u003c\/p\u003e \u003cp\u003e15.6 Enzymes for Peptide Terminal Modification 412\u003c\/p\u003e \u003cp\u003e15.7 Conclusions 415\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 16 Biocatalysis for Drug Discovery and Development 421\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eYouyun Liang, Mingzi M. Zhang, Ee Lui Ang, and Huimin Zhao\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Introduction 421\u003c\/p\u003e \u003cp\u003e16.2 Single Enzymatic Reactions 423\u003c\/p\u003e \u003cp\u003e16.3 Multienzyme Biocatalytic Reactions 437\u003c\/p\u003e \u003cp\u003e16.4 Future Perspective: Biocatalysts for the Pharmaceutical Industry 445\u003c\/p\u003e \u003cp\u003e16.5 Conclusion 448\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 17 Application of Aromatic Hydrocarbon Dioxygenases 457\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eWatumesa A. Tan and Rebecca E. Parales\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17.1 Introduction 457\u003c\/p\u003e \u003cp\u003e17.2 Challenges in Aromatic Hydrocarbon Dioxygenase Applications 457\u003c\/p\u003e \u003cp\u003e17.3 Protein Engineering to Improve Enzymatic Activity and Alter Substrate Specificity 459\u003c\/p\u003e \u003cp\u003e17.4 Protein Engineering for the Production of Specific Chemicals 464\u003c\/p\u003e \u003cp\u003e17.5 Strain Modification for the Development of New Biodegradation Pathways 467\u003c\/p\u003e \u003cp\u003e17.6 Phytoremediation: The Expression of Bacterial Dioxygenases in Plant Systems for Bioremediation Purposes 468\u003c\/p\u003e \u003cp\u003e17.7 Concluding Remarks 469\u003c\/p\u003e \u003cp\u003eAcknowledgments 469\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 18 Ene]reductases and their Applications 473\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eTanja Knaus, Helen S. Toogood, and Nigel S. Scrutton\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e18.1 Introduction 473\u003c\/p\u003e \u003cp\u003e18.2 Substrate Classes and Industrial Applications 474\u003c\/p\u003e \u003cp\u003e18.3 Multienzyme Reactions 478\u003c\/p\u003e \u003cp\u003e18.4 Alternative Hydride Sources 479\u003c\/p\u003e \u003cp\u003e18.5 Improvements of Productivity, Stereoselectivity, and\/or Conversion 482\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 19 Recent Developments in Aminopeptidases, Racemases, and Oxidases 489\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eYasuhisa Asano, Seiji Okazaki, and Kazuyuki Yasukawa\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e19.1 Aminopeptidase 489\u003c\/p\u003e \u003cp\u003e19.2 Racemase 492\u003c\/p\u003e \u003cp\u003e19.3 Amino Acid Oxidase 495\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 20 Biocatalytic Cascades for API Synthesis 503\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJohn M. Woodley\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e20.1 Introduction 503\u003c\/p\u003e \u003cp\u003e20.2 Multienzymatic Biocatalysis 504\u003c\/p\u003e \u003cp\u003e20.3 Process Aspects for Multistep Biocatalysis 506\u003c\/p\u003e \u003cp\u003e20.4 Process Development 511\u003c\/p\u003e \u003cp\u003e20.5 Biocatalytic Cascade Examples 512\u003c\/p\u003e \u003cp\u003e20.6 Future Outlook 515\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 21 Yeast-Mediated Stereoselective Synthesis 519\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRené Csuk\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e21.1 Introduction 519\u003c\/p\u003e \u003cp\u003e21.2 Reductions of Aldehydes and Ketones 521\u003c\/p\u003e \u003cp\u003e21.3 Reduction of Thiocarbonyls or Sulfur]Containing Compounds 524\u003c\/p\u003e \u003cp\u003e21.4 Reduction of Functionalized Carbonyl and Dicarbonyl Compounds 524\u003c\/p\u003e \u003cp\u003e21.5 Reduction of Keto Esters 527\u003c\/p\u003e \u003cp\u003e21.6 Hydrolysis of Esters 529\u003c\/p\u003e \u003cp\u003e21.7 Immobilized Baker’s Yeast 530\u003c\/p\u003e \u003cp\u003e21.8 Whole]Cell Biocatalysis in Ionic Liquids and Deep Eutectic Solvents 531\u003c\/p\u003e \u003cp\u003e21.9 C„ŸC Bond]Forming and Breaking Reactions 532\u003c\/p\u003e \u003cp\u003e21.10 Miscellaneous Reactions 533\u003c\/p\u003e \u003cp\u003e21.11 Conclusions 534\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 22 Biocatalytic Introduction of Chiral Hydroxy Groups using Oxygenases and Hydratases 545\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJun Ogawa, Makoto Hibi, and Shigenobu Kishino\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e22.1 Introduction 545\u003c\/p\u003e \u003cp\u003e22.2 Regio] and Stereoselective Hydroxylation of Propylbenzene and 3]Chlorostyrene by Cytochrome P450 BM]3 and its Mutant 546\u003c\/p\u003e \u003cp\u003e22.3 Regio] and Stereoselective Hydroxylation of Aliphatic Amino Acids by Fe(Ii)\/α]Ketoglutarate]Dependent Dioxygenases 547\u003c\/p\u003e \u003cp\u003e22.4 Regio] and Stereoselective Hydration of Unsaturated Fatty Acids by a Novel Fatty Acid Hydratase 551\u003c\/p\u003e \u003cp\u003e22.5 Conclusion 553\u003c\/p\u003e \u003cp\u003eAcknowledgment 553\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 23 Asymmetric Synthesis with Recombinant Whole]Cell Catalyst 557\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eHarald Gröger, Werner Hummel, and Severin Wedde\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e23.1 Introduction 557\u003c\/p\u003e \u003cp\u003e23.2 The Design\/Construction of Whole]Cell Catalysts 558\u003c\/p\u003e \u003cp\u003e23.3 Biotransformations with Whole]Cell Catalysts 561\u003c\/p\u003e \u003cp\u003e23.4 Conclusion 581\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 24 Lipases and Esterases as User-Friendly Biocatalysts in Natural Product Synthesis 587\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eKenji Mori\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e24.1 Introduction 587\u003c\/p\u003e \u003cp\u003e24.2 Desymmetrization of Prochiral or meso]Diols and Diacetates 587\u003c\/p\u003e \u003cp\u003e24.3 Kinetic Resolution of Racemic Alcohols 592\u003c\/p\u003e \u003cp\u003e24.4 Preparation of Enantiopure Intermediate(s) from a Mixture of Stereoisomers 599\u003c\/p\u003e \u003cp\u003e24.5 Conclusion 601\u003c\/p\u003e \u003cp\u003eAcknowledgments 601\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 25 Hydroxynitrile Lyases for Biocatalytic Synthesis of Chiral Cyanohydrins 603\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRomana Wiedner, Helmut Schwab, and Kerstin Steiner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e25.1 Introduction 603\u003c\/p\u003e \u003cp\u003e25.2 Discovery of Hydroxynitrile Lyases: Bioprospecting 604\u003c\/p\u003e \u003cp\u003e25.3 Applications of Hydroxynitrile Lyases 609\u003c\/p\u003e \u003cp\u003e25.4 Structural and Mechanistic Aspects 611\u003c\/p\u003e \u003cp\u003e25.5 Engineering of Hydroxynitrile Lyases 612\u003c\/p\u003e \u003cp\u003e25.6 Reaction Engineering and Reaction Systems 620\u003c\/p\u003e \u003cp\u003e25.7 Conclusion 623\u003c\/p\u003e \u003cp\u003eAcknowledgment 623\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 26 Biocatalysis: Nitrilases in Organic Synthesis 629\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJin]Song Gong, Jin]Song Shi, and Zheng]Hong Xu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e26.1 Introduction 629\u003c\/p\u003e \u003cp\u003e26.2 Nitrilase Discovery 630\u003c\/p\u003e \u003cp\u003e26.3 Nitrilase Improvement 631\u003c\/p\u003e \u003cp\u003e26.4 Applications in Organic Synthesis 635\u003c\/p\u003e \u003cp\u003e26.5 Conclusions and Future Prospects 638\u003c\/p\u003e \u003cp\u003eAcknowledgments 639\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 27 Biotechnology for the Production of Chemicals, Intermediates, and Pharmaceutical Ingredients 643\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eHans]Peter Meyer\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e27.1 Introduction 643\u003c\/p\u003e \u003cp\u003e27.2 Value Chains and Markets 645\u003c\/p\u003e \u003cp\u003e27.3 The Toolbox 661\u003c\/p\u003e \u003cp\u003e27.4 Sustainability, Green Premium Pricing, and Subsidies 665\u003c\/p\u003e \u003cp\u003e27.5 Regulatory Aspects and Public Perception 667\u003c\/p\u003e \u003cp\u003e27.6 Innovation (Not Only in the Laboratory!) 669\u003c\/p\u003e \u003cp\u003e27.7 Conclusions 670\u003c\/p\u003e \u003cp\u003eAcknowledgments 671\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 28 Microbial Transformations of Pentacyclic Triterpenes 675\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRobert Azerad\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e28.1 Introduction 675\u003c\/p\u003e \u003cp\u003e28.2 Typical Biotransformations in the Lupane Family 677\u003c\/p\u003e \u003cp\u003e28.3 Typical Biotransformations in the Oleane Family 680\u003c\/p\u003e \u003cp\u003e28.4 Typical Biotransformations in the Ursane Family 692\u003c\/p\u003e \u003cp\u003e28.5 Microbial Transformations of Other Pts 704\u003c\/p\u003e \u003cp\u003e28.6 Glycosylations and Deglycosylations 704\u003c\/p\u003e \u003cp\u003e28.7 Conclusion and Perspectives 710\u003c\/p\u003e \u003cp\u003e\u003cb\u003eChapter 29 Transaminases and their Applications 715\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eSarah-Marie Dold, Christoph Syldatk, and Jens Rudat\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e29.1 Introduction 715\u003c\/p\u003e \u003cp\u003e29.2 General Properties of Transaminases 715\u003c\/p\u003e \u003cp\u003e29.3 Synthesis Strategies with Transaminases 719\u003c\/p\u003e \u003cp\u003e29.4 Approaches to Optimize the Transaminase]Catalyzed Reactions 735\u003c\/p\u003e \u003cp\u003e29.5 Conclusion 743\u003c\/p\u003e \u003cp\u003eIndex 747\u003c\/p\u003e \u003cb\u003eRamesh N. Patel, Ph.D.\u003c\/b\u003e, 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. \u003cp\u003e\u003ci\u003eGreen Biocatalysis\u003c\/i\u003e 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.\u003c\/p\u003e \u003cp\u003eDrawing on the knowledge of over 70 internationally renowned experts in the field of biotechnology, \u003ci\u003eGreen Biocatalysis\u003c\/i\u003e discusses a variety of case studies with emphases on process R\u0026amp;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: \u003c\/p\u003e \u003cul\u003e \u003cli\u003eA 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\u003c\/li\u003e \u003cli\u003eDiscussion 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\u003c\/li\u003e \u003cli\u003eThe 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\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003e With over 3000 references and 800 figures, tables, equations, and drawings, \u003ci\u003eGreen Biocatalysis\u003c\/i\u003e is an excellent resource for biochemists, organic chemists, medicinal chemists, chemical engineers, microbiologists, pharmaceutical chemists, and undergraduate and graduate students in the aforementioned disciplines.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47989311406309,"sku":"NP9781118822296","price":252.95,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9781118822296.jpg?v=1761783623","url":"https:\/\/k12savings.com\/products\/green-biocatalysis-isbn-9781118822296","provider":"K12savings","version":"1.0","type":"link"}