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Book Details
Abstract
Implementing biocatalytic strategies in an industrial setting at a commercial scale is a challenging task, necessitating a balance between industrial need against economic viability. With invited contributions from small and large-scale chemical and pharmaceutical companies, this book bridges the gap between academia and industry. Contributors discuss current processes, types of biocatalysts and improvements, industrial motivation and key aspects to economically succeed. With its focus on industry related issues, this book will be a useful tool for future research by both practitioners and academics.
Table of Contents
| Section Title | Page | Action | Price |
|---|---|---|---|
| Cover | Cover | ||
| Biocatalysis: An Industrial Perspective | i | ||
| Preface | vii | ||
| Contents | ix | ||
| Part I - Context and Challenges for Industrial Biocatalysis | 1 | ||
| Chapter 1 - An Appreciation of Biocatalysis in the Swiss Manufacturing Environment | 3 | ||
| 1.1 Introduction | 3 | ||
| 1.1.1 Biocatalysis in the Swiss Manufacturing Environment | 7 | ||
| 1.1.2 Current Status | 7 | ||
| 1.1.3 Patent Analysis | 14 | ||
| 1.2 Selected Enzyme Classes Used in the Swiss Manufacturing Environment | 16 | ||
| 1.2.1 Oxidoreductases EC1 | 17 | ||
| 1.2.2 Transferases EC2 | 22 | ||
| 1.3 Challenges | 25 | ||
| 1.3.1 Regulation | 25 | ||
| 1.3.1.1 Technical Enzymes | 26 | ||
| 1.3.1.2 Food Processing Enzymes | 26 | ||
| 1.3.1.3 Feed Enzymes | 28 | ||
| 1.3.1.4 Enzymes in Cosmetics | 28 | ||
| 1.3.1.5 Enzymes for the Manufacture of APIs | 29 | ||
| 1.3.2 Development Time | 30 | ||
| 1.3.3 Technological Lock-in | 32 | ||
| 1.3.4 Public Perception | 32 | ||
| 1.3.5 Education | 33 | ||
| 1.4 Opportunities | 35 | ||
| 1.4.1 Starting Materials | 35 | ||
| 1.4.2 Sustainability and Greenness | 36 | ||
| 1.4.3 Swiss Industrial Biocatalysis Consortium | 36 | ||
| 1.4.4 New Business Ideas | 37 | ||
| 1.5 Future Directions | 37 | ||
| Acknowledgements | 39 | ||
| References | 39 | ||
| Chapter 2 - Biocatalysis – A Greener Alternative in Synthetic Chemistry | 44 | ||
| 2.1 Introduction | 44 | ||
| 2.2 Motivation for Industry to Use/Research on Biocatalysis | 47 | ||
| 2.3 Challenges Faced by Biocatalysis in Industry2 | 49 | ||
| 2.4 Prospects2,79 | 52 | ||
| 2.5 Overview of Current Enzyme-based Processes Implemented/In-progress at Industrial, Commercial Scale | 52 | ||
| 2.6 Our Experience in Some Chemoenzymatic Projects | 56 | ||
| 2.6.1 Protease-mediated Synthesis of Valganciclovir Intermediate135 | 58 | ||
| 2.6.2 Chemoenzymatic Synthesis of Optically Pure Rivastigmine Intermediate Using ADH from Baker’s Yeast and KRED142,143 | 58 | ||
| 2.6.3 Preparation of Deoxynojirimycin, Key Intermediate of an Anti-diabetic Drug | 60 | ||
| 2.7 Potential Safety Aspects | 66 | ||
| 2.8 Conclusions | 67 | ||
| Abbreviations | 68 | ||
| Glossary | 68 | ||
| References | 70 | ||
| Chapter 3 - Biocatalytic Synthesis of Small Molecules – Past, Present and Future | 77 | ||
| 3.1 Introduction | 77 | ||
| 3.2 Biocatalytic Conversions of Racemates | 78 | ||
| 3.2.1 Biocatalytic Resolution of Racemates | 79 | ||
| 3.2.2 Biocatalytic Deracemizations | 79 | ||
| 3.3 Biocatalytic Desymmetrizations | 80 | ||
| 3.4 Biocatalytic Asymmetric Oxidations and Reductions | 81 | ||
| 3.4.1 Biocatalytic Asymmetric Oxidations | 81 | ||
| 3.4.2 Biocatalytic Asymmetric Reductions | 83 | ||
| 3.5 Biocatalytic Asymmetric Hydrolysis and Acylation Reactions | 84 | ||
| 3.5.1 Biocatalytic Asymmetric Hydrolysis Reactions | 85 | ||
| 3.5.2 Biocatalytic Asymmetric Acylation Reactions | 86 | ||
| 3.6 Biocatalytic Asymmetric Transfer Reactions | 86 | ||
| 3.7 Biocatalytic Asymmetric Addition and Elimination Reactions | 88 | ||
| 3.8 Summary and Outlook | 89 | ||
| References | 90 | ||
| Chapter 4 - EntreChem: Building a Sustainable Business Case in Biotechnology: From Biocatalysis to Synthetic Biology | 98 | ||
| 4.1 Introduction | 98 | ||
| 4.2 Biocatalysis | 99 | ||
| 4.2.1 Enantiopure Chiral Building Blocks | 99 | ||
| 4.2.2 Cascade Processes Taking Advantage of Biocatalysis | 100 | ||
| 4.3 Drug Development | 105 | ||
| 4.3.1 Natural Products in Drug Discovery | 105 | ||
| 4.3.2 EntreChem’s Approach to Natural Products Drug Discovery | 107 | ||
| 4.3.3 Aureolic Acids: The Quest for Clinically Viable “Mithralogs” | 109 | ||
| 4.3.4 Collismycin Analogs as Immunosuppressive and Neuroprotective Drugs | 112 | ||
| 4.3.5 Glycosylated Indolocarbazoles as Potent and Selective Kinase Inhibitors | 115 | ||
| 4.4 Business Models in Biocatalysis and Natural Products Drug Discovery | 117 | ||
| References | 121 | ||
| Part II - Biocatalysis: from Pharmaceuticals to Bulk Chemistry | 125 | ||
| Chapter 5 - Bristol-Myers Squibb: Preparation of Chiral Intermediates for the Development of Drugs and APIs | 127 | ||
| 5.1 Introduction | 127 | ||
| 5.2 Anti-Alzheimer's Drug. Enzymatic Preparation of (R)-5,5,5-Trifluoronorvaline | 128 | ||
| 5.3 Cholesterol Lowering Agents | 130 | ||
| 5.3.1 Enantioselective Enzymatic Acylation of Racemic Alcohol | 130 | ||
| 5.3.2 Enzymatic Synthesis of (3S,5R)-Dihydroxy-6-(benzyloxy)hexanoic Acid, Ethyl Ester | 131 | ||
| 5.4 Calcitonin Gene-related Peptide Receptors Antagonists (Migraine Treatment): Enzymatic Preparation of (R)-2-Amino-3-(7-methyl-... | 132 | ||
| 5.5 Antidiabetic Drugs | 134 | ||
| 5.5.1 Saxagliptin: Enzymatic Synthesis of (S)-N-Boc-3-hydroxyadamantylglycine | 134 | ||
| 5.5.2 Saxagliptin: Enzymatic Synthesis of N-Cbz-4,5-dehydro-L-prolineamide and N-Boc-4,5-dehydro-L-prolineamide | 136 | ||
| 5.5.3 Saxagliptin: Enzymatic Ammonolysis of (5S)-4,5-Dihydro-1H-pyrrole-1,5-dicarboxylic Acid, 1-(1,1-Dimethylethyl)-5-ethyl Este... | 137 | ||
| 5.5.4 GLP-1 Receptor Agonists: Enzymatic Preparation of (S)-Amino-3-[3-{6-(2-methylphenyl)}pyridyl]-propionic Acid | 138 | ||
| 5.6 Antihypertensive Drugs | 140 | ||
| 5.6.1 Enzymatic Synthesis of (S)-6-Hydroxynorleucine | 140 | ||
| 5.6.2 Vanlev: Enzymatic Synthesis of Allysine Ethylene Acetal | 141 | ||
| 5.6.3 Vanlev: Enzymatic Synthesis of Thiazepine | 142 | ||
| 5.6.4 Captopril: Enzymatic Preparation of (S)-3-Benzoylthio-2-methylpropanoic Acid | 143 | ||
| 5.7 Antiviral Drugs. Case Study: Atazanavir | 144 | ||
| 5.7.1 Atazanavir: Enzymatic Synthesis of (S)-Tertiary-leucine | 144 | ||
| 5.7.2 Atazanavir: Enzymatic Preparation of (1S,2R)-[3-Chloro-2-hydroxy-1-(phenylmethyl)propyl]carbamic Acid, 1,1-Dimethyl-ethyl E... | 146 | ||
| 5.8 Antianxiety Drug. Buspirones: Enzymatic Preparation of 6-Hydroxybuspirone | 147 | ||
| 5.9 Antiviral Drugs. Hepatitis B Viral (HBV) Inhibitor: Enzymatic Asymmetric Hydrolysis and Acetylation | 149 | ||
| 5.10 Chemokine Receptor Modulators: Enzymatic Desymmetrization of Dimethyl Ester | 150 | ||
| 5.11 Anticancer Drugs | 151 | ||
| 5.11.1 Paclitaxel Semisynthetic Process | 151 | ||
| 5.11.2 Water-soluble Taxane Derivatives | 154 | ||
| 5.11.3 Epothilones: Epothilone B and Epothilone F | 155 | ||
| 5.11.4 IGF-1 Receptor Inhibitor: Enzymatic Preparation of (S)-2-Chloro-1-(3-chlorophenyl)ethanol | 157 | ||
| 5.11.5 Retinoic Acid Receptor Agonist: Enzymatic Preparation of 2-(R)-Hydroxy-2-(1′,2′,3′,4′-tetrahydro-1′,1′,4′,4′-tetramethyl-6... | 158 | ||
| 5.12 Microbial Hydroxylation of Mutilin and Pleuromutilin | 158 | ||
| 5.13 Conclusions | 160 | ||
| Acknowledgements | 161 | ||
| References | 161 | ||
| Chapter 6 - Johnson Matthey: A Technology Provider Perspective to Biocatalysis in the Fine Chemicals Industry | 168 | ||
| 6.1 Introduction | 168 | ||
| 6.2 Commercial Considerations | 170 | ||
| 6.2.1 Technology Value | 170 | ||
| 6.2.2 Manufacturing | 172 | ||
| 6.2.3 Market Analysis | 172 | ||
| 6.2.4 Catalyst Portfolio | 173 | ||
| 6.3 Technical Considerations | 174 | ||
| 6.3.1 Enzyme Recruitment | 175 | ||
| 6.3.2 Enzyme Engineering | 179 | ||
| 6.3.3 Process Improvement | 182 | ||
| 6.4 Conclusions | 186 | ||
| Acknowledgements | 188 | ||
| References | 188 | ||
| Chapter 7 - EnzymeWorks: Recent Advances in Enzyme Engineering for Chemical Synthesis | 190 | ||
| 7.1 Introduction to EnzymeWorks | 190 | ||
| 7.1.1 Current Status of Biocatalyst Development | 191 | ||
| 7.2 Biocatalysis in the Food and Beverage Industry | 192 | ||
| 7.2.1 Introduction of Stevia Development | 193 | ||
| 7.2.2 Plant Family 1 UDP-glycosyltransferase Applications | 194 | ||
| 7.2.3 Chemoenzymatic Synthesis of Rebaudioside M | 199 | ||
| 7.2.4 Enzyme Immobilization and Whole Cell Biosynthesis Development | 201 | ||
| 7.2.5 Future Perspectives on Biocatalysis in the Food and Beverage Industry | 202 | ||
| 7.3 Ketoreductase (KRED) Applications | 202 | ||
| 7.3.1 Ibrutinib Development | 205 | ||
| 7.3.2 Future Perspectives on Ketoreductase (KRED) Biocatalysis | 208 | ||
| 7.4 Biocatalysis in the Antibiotic Industry | 208 | ||
| 7.4.1 Introduction to Cephalosporin C Acylase (CCA) | 210 | ||
| 7.4.2 Gene Expression, Structure and Catalytic Mechanism of Acylases | 212 | ||
| 7.4.3 Recent Advances in Cephalosporin C Acylase (CCA) Development | 216 | ||
| 7.4.4 Future Perspectives on Acylase Biocatalysis | 217 | ||
| 7.4.5 Introduction to Deacetoxycephalosporin C Synthase | 217 | ||
| 7.4.6 Deacetoxycephalosporin C Synthase Structure and Mechanism | 219 | ||
| 7.4.7 Recent Advances in Deacetoxycephalosporin C Synthase Development | 220 | ||
| 7.4.8 Future Perspectives of Antibiotic Biocatalysis | 222 | ||
| 7.5 Future Perspectives of Biocatalyst Development | 222 | ||
| References | 223 | ||
| Chapter 8 - Almac: An Industrial Perspective of Ene Reductase (ERED) Biocatalysis | 229 | ||
| 8.1 Introduction | 229 | ||
| 8.1.1 Almac Group | 229 | ||
| 8.1.2 Biocatalysis at Almac | 230 | ||
| 8.1.3 The Rise of Biocatalysis | 230 | ||
| 8.2 Introduction to Alkene Reduction | 231 | ||
| 8.3 An Introduction to Ene Reductases and How They Work | 232 | ||
| 8.4 Examples of Ene Reductase Reactions Reported in the Literature | 233 | ||
| 8.4.1 Ene Reductases as Part of a Reaction Sequence | 234 | ||
| 8.4.2 Ene Reductases and Solvents | 239 | ||
| 8.4.3 Challenges of Co-factor Recycle | 240 | ||
| 8.4.4 Avoiding the Use of Nicotinamide Co-factors | 241 | ||
| 8.4.5 Impact of Synthetic Biology | 245 | ||
| 8.4.6 Ene Reductases in Reverse: Oxidation | 247 | ||
| 8.4.7 Thermophilic Ene-reductases | 248 | ||
| 8.4.8 Alternative Screening Methods | 248 | ||
| 8.5 Example of Utilisation of an ERED at Industrial Scale | 249 | ||
| 8.6 Transition of Ene Reductases to Mainstream Biocatalytic Use | 251 | ||
| 8.7 Conclusions | 252 | ||
| Acknowledgements | 253 | ||
| References | 253 | ||
| Chapter 9 - GSK: Biocatalyst Discovery and Optimisation | 257 | ||
| 9.1 Introduction | 257 | ||
| 9.2 Biocatalyst Discovery | 260 | ||
| 9.2.1 Design of Enzyme Panels | 260 | ||
| 9.2.2 Imine Reductase Panel – Importance and Applicability | 260 | ||
| 9.2.2.1 In silico Identification of Novel IREDs | 262 | ||
| 9.2.2.2 Panel Composition and Enzyme Production | 263 | ||
| 9.2.2.3 Activity Screening for Functional IREDs | 265 | ||
| 9.3 Biocatalyst Optimisation | 268 | ||
| 9.3.1 Nelarabine Case Study | 269 | ||
| 9.3.1.1 Library Design | 270 | ||
| 9.3.1.2 Activity Assay | 270 | ||
| 9.3.1.3 Results from Mutant Libraries | 272 | ||
| 9.4 Conclusions | 272 | ||
| Acknowledgements | 273 | ||
| References | 273 | ||
| Chapter 10 - PETROBRAS: Efforts on Biocatalysis for Fuels and Chemicals Production | 276 | ||
| 10.1 PETROBRAS Overview | 276 | ||
| 10.2 Hydrolysis of Lignocellulosic and Starchy Biomass | 277 | ||
| 10.3 Synthesis of Solvents | 280 | ||
| 10.3.1 Glycerol Carbonate | 280 | ||
| 10.3.2 Butyl Acetate | 281 | ||
| 10.4 Synthesis and Degradation of Polymers | 282 | ||
| 10.4.1 Synthesis of Polyesters | 282 | ||
| 10.4.2 Depolymerization of Poly(ethylene terephthalate) | 284 | ||
| 10.5 Synthesis of Biolubricants | 285 | ||
| 10.6 Synthesis of Biodiesel | 289 | ||
| 10.7 Concluding Remarks | 292 | ||
| References | 292 | ||
| Chapter 11 - MetGen: Value from Wood – Enzymatic Solutions | 298 | ||
| 11.1 Introduction | 298 | ||
| 11.1.1 METGEN – Masters of Enzyme Technology and Genetic Engineering | 298 | ||
| 11.1.2 Biocatalysis of Wood – Motivation and Challenges | 300 | ||
| 11.2 Enzymes in Pulp and Paper | 301 | ||
| 11.2.1 Enzymes in Pulp & Paper Industry Sector – Business Aspect | 301 | ||
| 11.2.2 Major Enzyme Components for Wood Applications | 302 | ||
| 11.2.3 Enzyme Development – from Laboratory to Industry | 304 | ||
| 11.2.4 MetZyme® LIGNO™ | 305 | ||
| 11.2.5 MetZyme® BRILA™ | 309 | ||
| 11.2.6 Concluding Remarks on Enzymes in Pulp and Paper | 313 | ||
| 11.3 Biorefinery Enzymes | 313 | ||
| 11.3.1 Renewable Chemical Industry Segment – Business Aspect | 313 | ||
| 11.3.2 Wood Biorefinery Concept | 314 | ||
| 11.3.3 Biomass Hydrolysis – Chemicals and Enzymes | 315 | ||
| 11.3.4 Biomass Is Not Oil; It Is More Like Soup of the Day | 316 | ||
| 11.3.5 Beyond Sugars | 317 | ||
| 11.3.6 Biorefinery Enzymes – Concluding Remarks | 320 | ||
| 11.3.7 Wood in Pulp and Paper and Biorefinery – Common Problems or Window for Opportunity | 320 | ||
| Abbreviations | 320 | ||
| References | 320 | ||
| Part III - Biocatalyst Optimization with Industrial Perspectives | 323 | ||
| Chapter 12 - LentiKat’s: Industrial Biotechnology, Experiences and Visions | 325 | ||
| 12.1 Introduction | 325 | ||
| 12.2 Lentikats Biotechnology | 326 | ||
| 12.2.1 Potential of Lentikats Biotechnology | 327 | ||
| 12.2.2 Properties of Lentikats Biotechnology | 329 | ||
| 12.2.2.1 Advantages of Lentikats Biocatalyst & Lentikats Biotechnology | 329 | ||
| 12.2.2.2 Specific Advantages of Lentikats Biocatalysts with Immobilized Whole-cells | 330 | ||
| 12.2.2.3 Disadvantages of Lentikats Biocatalyst & Lentikats Biotechnology | 330 | ||
| 12.2.3 Production of Lentikats Biocatalyst | 330 | ||
| 12.3 Experiences in Wastewater Treatment | 331 | ||
| 12.3.1 Municipal Wastewater Treatment | 331 | ||
| 12.3.2 Industrial Wastewater Treatment | 332 | ||
| 12.3.3 Special Applications | 332 | ||
| 12.3.4 Advantages of Lentikats Biotechnology in Wastewater Treatment | 332 | ||
| 12.3.5 Product Lines | 333 | ||
| 12.3.5.1 Nitrification | 333 | ||
| 12.3.5.2 Nitritation | 333 | ||
| 12.3.5.3 Denitrification | 333 | ||
| 12.3.5.4 Deammonification | 334 | ||
| 12.3.5.5 Biological Oxygen Demand (BOD) Removal | 334 | ||
| 12.3.5.6 Selective Biodegradations | 334 | ||
| 12.3.6 Wastewater Treatment Applications | 334 | ||
| 12.3.6.1 Pilot-scale Applications | 334 | ||
| 12.3.6.2 Industrial Applications | 336 | ||
| 12.4 Experiences in the Pharmaceutical & Food Industry | 338 | ||
| 12.4.1 Food Technology Industry | 338 | ||
| 12.4.2 Pharmaceutical Industry | 338 | ||
| 12.4.3 Bio-based Chemicals Industry | 339 | ||
| 12.4.4 Advantages of Lentikats Biotechnology in the Pharmaceutical & Food Industry | 339 | ||
| 12.4.5 Application Examples in the Pharmaceutical & Food Industry | 339 | ||
| 12.4.5.1 Penicillin G Acylase | 339 | ||
| 12.4.5.2 Whole-cell Catalysts | 340 | ||
| 12.4.5.3 Monoamine Oxidase | 340 | ||
| 12.4.5.4 Baeyer–Villiger Monooxygenase (BVMO) | 340 | ||
| 12.4.5.5 Spores | 340 | ||
| 12.4.5.6 Oxynitrilase | 341 | ||
| 12.4.5.7 β-Galactosidase | 341 | ||
| 12.4.5.8 ω-Transaminase | 341 | ||
| 12.4.6 Pharmaceutical & Food Applications | 342 | ||
| 12.4.6.1 Main Laboratory and Pilot-scale Applications | 343 | ||
| 12.4.6.2 Ongoing Projects and Projects in Preparation | 343 | ||
| 12.5 Vision | 343 | ||
| References | 344 | ||
| Chapter 13 - EziG: A Universal Platform for Enzyme Immobilisation | 345 | ||
| 13.1 Introduction | 345 | ||
| 13.2 A General Methodology for Enzyme Reuse | 348 | ||
| 13.2.1 The Potential of Biocatalysis by Far Exceeds Its Current Exploitation | 348 | ||
| 13.2.2 Unlocking the Potential of Enzymes | 349 | ||
| 13.2.3 Immobilised Enzymes for the Pharmaceutical Industry | 350 | ||
| 13.2.4 The Reusable Enzyme Utopia – Enzymes Anchored in Space | 350 | ||
| 13.2.5 The EziG Technology | 351 | ||
| 13.2.6 Standardised Procedure for Immobilisation | 354 | ||
| 13.2.7 Lower Cost Materials versus High Performance | 354 | ||
| 13.3 Case Studies27 | 355 | ||
| 13.3.1 In-reactor Enzyme Immobilisation | 355 | ||
| 13.3.2 Two-phase System in Flow for in situ Product Removal | 356 | ||
| 13.3.3 Candida antarctica Lipase B (CalB) | 357 | ||
| 13.3.4 Co-immobilisation for Cascade Reactions | 358 | ||
| 13.4 Prospects | 359 | ||
| 13.4.1 Stability versus Activity – Replacing Low Cost Catalysts | 359 | ||
| 13.4.2 Biocatalysis in Flow – Towards Manufacturing Processes in Continuous Mode | 360 | ||
| 13.5 Conclusions | 360 | ||
| Acknowledgements | 361 | ||
| References | 361 | ||
| Chapter 14 - Cross-linked Enzyme Aggregates (CLEAs): From Concept to Industrial Biocatalyst | 363 | ||
| 14.1 Introduction: Biocatalysis is Green and Sustainable | 363 | ||
| 14.2 Immobilisation of Enzymes | 364 | ||
| 14.3 The CLEA Technology | 365 | ||
| 14.3.1 The Concept | 365 | ||
| 14.3.2 Preparation of CLEAs | 366 | ||
| 14.3.2.1 Aggregation | 367 | ||
| 14.3.2.2 Cross-linking | 367 | ||
| 14.3.2.3 Effect of Additives | 368 | ||
| 14.3.2.4 Key Factors Influencing the Cost-effectiveness of CLEAs | 368 | ||
| 14.3.2.5 CLEA-polymer Composites | 369 | ||
| 14.3.3 Physical Properties of CLEAs | 369 | ||
| 14.3.4 Advantages and Limitations of CLEAs | 370 | ||
| 14.3.5 Reactor Design | 371 | ||
| 14.4 Scope of the CLEA Technology | 373 | ||
| 14.4.1 Hydrolase CLEAs | 373 | ||
| 14.4.2 Oxidoreductase and Lyase CLEAs | 376 | ||
| 14.5 Multi- and Combi-CLEAs | 378 | ||
| 14.6 Magnetic CLEAs: The New Frontier | 381 | ||
| 14.7 Applications of CLEAs, Combi-CLEAs and mCLEAs | 384 | ||
| 14.7.1 1G and 2G Biofuels Production | 385 | ||
| 14.7.2 Food and Beverages Processing | 387 | ||
| 14.7.3 Synthesis of Semi-synthetic Penicillin and Cephalosporin Antibiotics | 388 | ||
| 14.7.4 Removal of Dyes, Pharma Residues and Endocrine Disruptors from Waste Water | 389 | ||
| 14.7.5 Other Potential Applications | 389 | ||
| 14.8 Conclusions and Future Prospects | 390 | ||
| References | 390 | ||
| Chapter 15 - SynBiocat: Protein Purification, Immobilization and Continuous-flow Processes | 397 | ||
| 15.1 Introduction | 397 | ||
| 15.2 SynBiocat – From Protein Purification to Continuous-flow Processes | 398 | ||
| 15.2.1 Enzyme Production and Purification | 400 | ||
| 15.2.1.1 Enzymes at SynBiocat and Fermentia | 400 | ||
| 15.2.1.2 Hydrophobic Adsorption-based Protein Separation | 400 | ||
| 15.2.1.3 Metal Ion Affinity Based Protein Purification | 402 | ||
| 15.2.2 Enzyme Immobilization | 405 | ||
| 15.2.2.1 Enzyme Entrapment in Nanostructured Systems | 406 | ||
| 15.2.2.1.1\rEnzyme Entrapment in Sol–Gel Matrices.Sol–gel encapsulation of enzymes, which involves the formation of a silica matrix with the... | 406 | ||
| 15.2.2.1.2\rEnzyme Entrapment Within Electrospun Nanofibers.Recent developments in nanotechnology have provided a wealth of diverse nano-sca... | 408 | ||
| 15.2.2.2 Carrier-free Enzyme Immobilization by Enzyme–Enzyme Cross-linking | 410 | ||
| 15.2.2.3 Enzyme Immobilization onto Solid Nano- or Micro-sized Supports | 413 | ||
| 15.2.2.3.1\rEnzyme Immobilization on Surface-grafted Silica Supports by Adsorption.Among the many available carrier-based immobilization met... | 414 | ||
| 15.2.2.3.2\rEnzyme Immobilization onto Solid Supports by Covalent Bonds.As stated before, when applied under aqueous conditions, enzymes imm... | 414 | ||
| 15.2.2.4 Hybrid Immobilization | 417 | ||
| 15.2.3 Desktop Bioreactor Applications | 418 | ||
| 15.2.3.1 Biotransformations in Packed-bed Minireactors | 419 | ||
| 15.2.3.2 Biotransformations in Magnetic Chip Reactors | 421 | ||
| 15.3 Conclusion | 423 | ||
| List of Abbreviations | 424 | ||
| Acknowledgements | 425 | ||
| References | 425 | ||
| Part IV - Emerging Industrial Biocatalysis | 431 | ||
| Chapter 16 - Microvi: MicroNiche Engineering™ for Biocatalysis in the Water and Chemical Industries | 433 | ||
| 16.1 Introduction to Microvi | 433 | ||
| 16.2 Microvi’s MicroNiche Engineering™ Platform | 436 | ||
| 16.3 Case Study: MicroNiche Biocatalysts for Water Purification | 443 | ||
| 16.4 Producing Case Study: MicroNiche Biocatalysts for Biobased Chemicals | 449 | ||
| 16.5 Conclusions | 454 | ||
| References | 455 | ||
| Chapter 17 - Nofima: Peptide Recovery and Commercialization by Enzymatic Hydrolysis of Marine Biomass | 459 | ||
| 17.1 Nofima: The Company | 459 | ||
| 17.2 Hydrolysis of Marine Biomass | 461 | ||
| 17.2.1 Chemical Hydrolysis of Marine Biomass | 461 | ||
| 17.2.2 Enzymatic Hydrolysis of Marine Biomass | 462 | ||
| 17.3 Enzymes Used for Bioconversion | 464 | ||
| 17.4 Quality and Classification of Marine Biomass | 465 | ||
| 17.5 Functional Properties and Bioactivities of Hydrolyzed Marine Biomass | 466 | ||
| 17.6 Commercialization of Products from Marine Biomass | 471 | ||
| 17.7 Conclusions | 472 | ||
| 17.8 Case Examples | 472 | ||
| 17.8.1 Marealis – Producing a Nutraceutical from Shrimp Peels | 472 | ||
| 17.8.2 Polybait AS – Producing Fishing Bait from Fisheries By-products | 473 | ||
| References | 473 | ||
| Chapter 18 - CO2 Solutions: A Biomimetic Approach to Mitigate CO2 Emissions – The Use of Carbonic Anhydrase in an “Industrial Lung” | 477 | ||
| 18.1 Introduction | 477 | ||
| 18.2 Conventional Post-combustion CO2 Capture Technologies | 478 | ||
| 18.3 CSI’ Technology: An Industrial Lung | 481 | ||
| 18.4 Selection and Development of a Robust CA | 484 | ||
| 18.4.1 Elevated Ionic Strength | 485 | ||
| 18.4.2 High pH | 486 | ||
| 18.4.3 Temperatures Above 60 °C | 486 | ||
| 18.4.4 Effect of High Surface Volume Ratio | 486 | ||
| 18.4.5 Effect of High Shear Stress | 487 | ||
| 18.4.6 Effect of Contaminants | 487 | ||
| 18.4.7 Effect of Solid–Liquid Interface | 488 | ||
| 18.4.8 Carbonic Anhydrase Development | 488 | ||
| 18.5 Technology Validation/Demonstration at Pilot Scale | 491 | ||
| 18.6 Conclusions | 494 | ||
| Acknowledgements | 494 | ||
| References | 495 | ||
| Subject Index | 497 |