| Part 1 Novel reaction conditions for biotransformation 1 |
| CHAPTER 1 Biotransformation in ionic liquid Toshiyuki Itoh 3 |
| 1. Introduction 3 |
| 2. Ionic Liquids as a Reaction Medium for Biotransformation 3 |
| 3. Lipase-Catalyzed Reaction in an Ionic Liquid Solvent System 7 |
| 4. Activation of Lipase by an Ionic Liquid 10 |
| 5. Various Biotransformations in an Ionic Liquid Solvent System 15 |
| 6. Concluding Remarks 18 |
| References 18 |
| CHAPTER 2 Temperanture control of the enantioselectivity in the lipase-catalyzed resolutions Takashi Sakai 21 |
| 1. Introduction 21 |
| 2. Finding of the "Low-Temperature Method" in the Lipase-Catalyzed Kinetic Resolution 22 |
| 3. Theory of Temperature Effect on the Enantioselectivity 23 |
| 4. General Applicability of the "Low-Temperature Method" Examined 28 |
| 4.1. Application to solketal and other primary and secondary alcohols 28 |
| 4.2. Resolution of (±)-2-hydroxy-2-(pentafluorophenyl)acetonitrile 30 |
| 4.3. Immobilization of lipase on porous ceramic support (Toyonite) for acceleration 31 |
| 4.4. Structural optimization of organic bridges on Toyonite 32 |
| 4.5. Practical resolution of azirine 1 by the " low-temperature method" combined with Toyonite-immobilized lipase and optimized acylating agent 33 |
| 4.6. Resolution of (2R*,3S*)- and (2R*,3R*)-3-methyl-3-phenyl-2-aziridinemethanols 34 |
| 4.7. Resolution of 5-(hydroxymethyl)-3-phenyl-2-isoxazoline 36 |
| 4.8. Application of temperature control to asymmetric protonation 37 |
| 4.9. Lipase-catalyzed resolutions at high temperatures up to 120℃ 37 |
| 5. Low-Temperature Reactions in Literatures 37 |
| 6. Lipase-Catalyzed Resolution of Primary Alcohols: Promising Candidates for the "Low-Temperature Method" 40 |
| 7. Conclusion 45 |
| References 45 |
| CHAPTER 3 Future directions in photosynthetic organisms-catalyzed reactions Kaoru Nakamura 51 |
| 1. Introduction 51 |
| 2. Reduction Reaction 51 |
| 3. Oxidation and Hydroxylation 55 |
| 4. Removal of Organic and Inorganic Substances in Wastewater 56 |
| 5. Conclusion 57 |
| References 57 |
| CHAPTER 4 Catalysis by enzyme-metal combinations Mahn-Joo Kim, Jaiwook Park, Yangsoo Ahn, Palakodety R. Krishna 59 |
| 1. Introduction 59 |
| 2. Dynamic Kinetic Resolutions by Enzyme-Metal Combinations 60 |
| 2.1. DKR of secondary alcohols 60 |
| 3. Asymmetric Transformations by Enzyme-Metal Combinations 73 |
| 3.1. Asymmetric transformation of ketone 73 |
| 3.2. Asymmetric transformation of enol ester 75 |
| 3.3. Asymmetric transformation of ketoxime 76 |
| 4. Conclusion 78 |
| Acknowledgements 78 |
| References 79 |
| Part 2 Uncommon kind of biocatalytic reaction 81 |
| CHAPTER 5 Biological Kolbe-Schmitt carboxylation Possible use of enzymes for the direct carboxylation of organic substrates Toyokazu Yoshida, Toru Nagasawa 83 |
| 1. Introduction 83 |
| 2. Enzymes Catalyzing the Carboxylation of Phenolic Compounds 84 |
| 2.1. 4-Hydroxybenzoate decarboxylase (EC 4.1.1.61) 85 |
| 2.2. 3,4-Dihydroxybenzoate decarboxylase (EC 4.1.1.63) 87 |
| 2.3. Phenolphosphate carboxylase (EC 4.1.1.-) in Thauera aromatica 88 |
| 2.4. 2,6-Dihydroxybenzoate decarboxylase 91 |
| 2.5. 2,3-Dihydroxybenzoate decarboxylase 95 |
| 3. Enzymes Catalyzing the Direct Carboxylation of Heterocyclic Compounds 95 |
| 3.1. Pyrrole-2- carboxylate decarboxylase 96 |
| 3.2. Indole-3-carboxylate decarboxylase 99 |
| 4. Structure Analysis of Decarboxylases Catalyzing CO2 Fixation 101 |
| 4.1. Class Ⅰ decarboxylases 102 |
| 4.2. Class Ⅱ decarboxylases 103 |
| 4.3. Phenylphosphate carboxylase 103 |
| 5. Conclusion 103 |
| References 104 |
| CHAPTER 6 Discovery, redesign and applications of Baeyer-Villiger monooxygenases Daniel E. Torres Pazmino, Marco W. Fraaije 107 |
| 1. Introduction 107 |
| 2. Biocatalytic Properties of Recombinant Available BVMOs 110 |
| 2.1. Discovery of novel BVMOs 112 |
| 2.2. Exploring sequenced (meta)genomes for novel BVMOs 114 |
| 2.3. Screening the metagenome for novel BVMOs 118 |
| 2.4. Redesign of BVMOs 119 |
| 3. Conclusions: Future Directions 122 |
| References 125 |
| CHAPTER 7 Enzymes in aldoxime-nitrile pathway: versatile tools in biocatalysis Yasuhisa Asano 129 |
| 1. Introduction 129 |
| 2. Screening for New Microbial Enzymes by Enrichment and Acclimation Culture Techniques 129 |
| 3. Development of Nitrile-Degrading Enzymes 131 |
| 4. Screening for Heat-Stable NHase 131 |
| 5. Screening for NHase with PCR 132 |
| 6. Nitrile Synthesis Using a New Enzyme, Aldoxime Dehydratase 133 |
| 6.1. Aldoxime-converting enzymes 133 |
| 6.2. Isolation of microorganisms having aldoxime dehydratase activity 134 |
| 6.3. Purification, characterization and primary structure determination of aldoxime dehydratase 134 |
| 6.4. Synthesis of nitriles from aldoxime with aldoxime dehydratase 135 |
| 6.5. Distribution of aldoxime dehydratase 136 |
| 6.6. Molecular screening for "aldoxime-nitrile pathway" 136 |
| 7. Conclusion 137 |
| Acknowledgements 137 |
| References 137 |
| CHAPTER 8 Addition of hydrocyanic acid to carbonyl compounds Franz Effenberger, Anja Bohrer, Siegfried Forster 141 |
| 1. Introduction 141 |
| 2. Optimize Reaction Conditions for the HNL-Catalyzed Formation of Chiral Cyanohydrins 143 |
| 3. Synthetic Potential of Chiral Cyanohydrins in Stereoselective synthesis 145 |
| 3.1. Chiral 2-hydroxy carboxylic acids 145 |
| 3.2. Optically active 1,2-amino alcohols 147 |
| 3.3. Stereoselective substitution of the hydroxyl group in chiral cyanohydrins 148 |
| 3.4. Stereoselective synthesis of substituted cyclohexanone cyanohydrins 149 |
| 4. Crystal Structures of Hydroxynitrile Lyases and Mechanism of Cyanogenesis 149 |
| 4.1. Crystal structures of HNL5 151 |
| 4.2. Reaction mechanism of cyanogenesis 151 |
| 4.3. Changing substrate specificity and stereoselectivity applying Trp128 mutants of wt-MehNL 152 |
| 5. Conclusion 153 |
| References 154 |
| Part 3 Novel compounds synthesized by biotransformations 157 |
| CHAPTER 9 Chiral heteroatom-containing compounds Piotr Kietbasinski, Marian Mikolajezyk 159 |
| 1. Introduction 159 |
| 2. Organosulfur Compounds 160 |
| 2.1. C-chiral hydroxy sulfides and derivatives 160 |
| 2.2 C-chiral hydroxyalkyl sulfones 163 |
| 2.3. C-chiral alkyl sulfates 165 |
| 2.4. Other C-chiral organosulfur compounds 166 |
| 2.5. S-chiral sulfinylcarboxylates 166 |
| 2.6. S-chiral hydroxy sulfoxides 168 |
| 2.7. S-chiral sulfinamides 169 |
| 2.8. S-chiral sulfoximines 171 |
| 3. Organophosphorus Compounds 172 |
| 3.1. C-chiral hydroxy phosphorus derivatives 172 |
| 3.2. C-chiral amino phosphorus compounds 180 |
| 3.3. P-chiral phosphoro-acetates 183 |
| 3.4. P-chiral hydroxy phosphoryl compounds 186 |
| 3.5. P-chiral hydroxy phosphorus P-boranes 191 |
| 3.6. Stereocontrolled transformations of organophosphorus acid esters 192 |
| 4. Organosilanes 196 |
| 5. Organogermanes 197 |
| 6. Future Perspectives 197 |
| References 199 |
| CHAPTER 10 Enzymatic polymerization Hiroshi Uyama 205 |
| 1. Introduction 205 |
| 2. Enzymatic Synthesis of Polyesters 206 |
| 2.1. Ring-opening polymerization to polyesters 207 |
| 2.2. Polycondensation of dicarboxylic acid derivatives and glycols to polyesters 212 |
| 2.3. Enzymatic synthesis of functional polyesters 219 |
| 3. Enzymatic Synthesis of Phenolic Polymers 228 |
| 3.1. Enzymatic oxidative polymerization of phenols 228 |
| 3.2. Enzymatic synthesis of functional phenolic polymers 233 |
| 3.3. Artifical urushi 238 |
| 3.4. Enzymatic synthesis and biological properties of flavonoid polymers 240 |
| 4. Concluding remarks 244 |
| References 245 |
| CHAPTER 11 Synthesis of naturally occurring β-D-glucopyranosides based on enzymatic β-glucosidation using β-glucosidase from almond Hiroyuki Akita 253 |
| 1. Introduction 253 |
| 2. Synthesis of β-D-Glucopyranoside Under Kinetically Controlled Condition 255 |
| 2.1. Synthesis of naturally occurring β-D-glucopyranoside 259 |
| 3. Synthesis of β-D-Glucopyranoside Under Equilibrium-Controlled Condition 262 |
| 3.1. Immobilization of β-D-glucosidase using prepolymer 263 |
| 3.2. Enzymatic transglucosidation 263 |
| 3.3. Synthesis of naturally occurring benzyl β-D-glucopyranoside 267 |
| 3.4. Synthesis of phenethyl β-D-glucopyranoside 270 |
| 3.5. Synthesis of (3Z)-hexenyl β-D-glucoyranoside 272 |
| 3.6. Synatesis of geranyl β-D-glucopyranoside 275 |
| 3.7. Synthesis of Sacranosides A (89) annd B (90) 277 |
| 3.8. Synthesis of naturally occurring n-octyl β-D-glucoyranosides 278 |
| 3.9. Synthesis of naturally occurring hexyl β-D-glucoyranoside 280 |
| 3.10. Synthesis of naturally occurring phenylpropenoid β-D-glucoyranoside 282 |
| 4. Future Aspect 287 |
| 5. Conclusion 289 |
| References 289 |
| Part 4 Use of molecular biology technique to find novel biocatalyst 291 |
| CHAPTER 12 Future directions in alcohol dehydrogenase-catalyzed reactions Jon D. Stewart 293 |
| 1. Introduction 293 |
| 2. Future Progress in the Discovery Phase of Dehydrogenases 295 |
| 2.1. Accurately predicting dehydrogenase structures 295 |
| 2.2. Predicting dehydrogenase substrate acceptance and stereoselectivities 296 |
| 2.3. Rapid screening of novel dehydrogenases 296 |
| 2.4. Dehydrogenases for large substrates 299 |
| 2.5. Dehydrogenase modules within larger assemblies as monofunctional catalysts 299 |
| 2.6. Dehydrogenase catalysis of other 1,2-carbonyl additions 300 |
| 3. Future Progress in Dehydrogenase Process Development 300 |
| 3.1. Improving the kinetic properties of dehydrogenases 301 |
| 3.2. Reductions of highly hydrophobic substrates 301 |
| 3.3. Cofactorless dehydrogenases? 302 |
| 4. Conclusions 302 |
| Acknowledgements 303 |
| References 303 |
| CHAPTER 13 Enzymatic decarboxylation of synthetic compounds Kenji Miyamoto, Hiromichi Ohta 305 |
| 1. Introduction 305 |
| 2. Arylmalonate Decarboxylase 309 |
| 2.1. Discovery of arylmalonate decarboxylase and its substrate specificity 310 |
| 2.2 Purification of the enzyme and cloning of the gene 311 |
| 2.3. Reaction mechanism 312 |
| 2.4. Inversion of enationselectivity based on the reaction mechanism and homology 317 |
| 2.5. Addition of racemase activity 319 |
| 3. Transketolase-Catalyzed Reaction 321 |
| 3.1. Substrate specificity and stereochemical source of TKase-catalyzed reaction 322 |
| 3.2. Application of TKase-catalyzed reaction in organic syntheses 322 |
| 3.3. Tertiary structure and mutagenesis studies 329 |
| 4. Future Trends of this Area 331 |
| 4.1. Application of decarboxylation reaction to dialkylmalonates 331 |
| 4.2. Decarboxylation of various carboxylic acids 332 |
| 4.3. Oxidative decarboxylation of β-hydroxycarboxylic acids 333 |
| 4.4. Carboxylation 336 |
| 4.5. Development of biotransformation via enolate 337 |
| 4.6. Utilization of database and informatics 339 |
| 5. Conclusion 339 |
| References 340 |
| Index 345 |
| Part 1 Novel reaction conditions for biotransformation 1 |
| CHAPTER 1 Biotransformation in ionic liquid Toshiyuki Itoh 3 |
| 1. Introduction 3 |
| 2. Ionic Liquids as a Reaction Medium for Biotransformation 3 |
| 3. Lipase-Catalyzed Reaction in an Ionic Liquid Solvent System 7 |
| 4. Activation of Lipase by an Ionic Liquid 10 |
