Biocatalysis /

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Bibliographic Details
Author / Creator:	Bommarius, A. S. (Andreas Sebastian)
Imprint:	Weinheim ; Cambridge : Wiley-VCH, c2004.
Description:	xxiii, 611 p. ; ill. ; 25 cm.
Language:	English
Subject:	Enzymes -- Biotechnology. Biosynthesis. Catalysis. Biosynthesis. Catalysis. Enzymes -- Biotechnology.
Format:	Print Book
URL for this record:	http://pi.lib.uchicago.edu/1001/cat/bib/5131687

Hidden Bibliographic Details
Varying Form of Title:	Biocatalysis: fundamentals and applications
Other authors / contributors:	Riebel, B. R. (Bettina R.)
ISBN:	3527303448
Notes:	Includes bibliographical references (p.591-592) and index.

Table of Contents:

Preface
Acknowledgments
1. Introduction to Biocatalysis
1.1. Overview: The Status of Biocatalysis at the Turn of the 21st Century
1.1.1. State of Acceptance of Biocatalysis
1.1.2. Current Advantages and Drawbacks of Biocatalysis
1.2. Characteristics of Biocatalysis as a Technology
1.2.1. Contributing Disciplines and Areas of Application
1.2.2. Characteristics of Biocatalytic Transformations
1.2.3. Applications of Biocatalysis in Industry
1.3. Current Penetration of Biocatalysis
1.3.1. The Past: Historical Digest of Enzyme Catalysis
1.3.2. The Present: Status of Biocatalytic Processes
1.4. The Breadth of Biocatalysis
1.4.1. Nomenclature of Enzymes
1.4.2. Biocatalysis and Organic Chemistry, or "Do we Need to Forget our Organic Chemistry?"
2. Characterization of a (Bio-)catalyst
2.1. Characterization of Enzyme Catalysis
2.1.1. Basis of the Activity of Enzymes: What is Enzyme Catalysis?
2.1.2. Development of Enzyme Kinetics from Binding and Catalysis
2.2. Sources and Reasons for the Activity of Enzymes as Catalysts
2.2.1. Chronology of the Most Important Theories of Enzyme Activity
2.2.2. Origin of Enzymatic Activity: Derivation of the Kurz Equation
2.2.3. Consequences of the Kurz Equation
2.2.4. Efficiency of Enzyme Catalysis: Beyond Pauling's Postulate
2.3. Performance Criteria for Catalysts, Processes, and Process Routes
2.3.1. Basic Performance Criteria for a Catalyst: Activity, Selectivity and Stability of Enzymes
2.3.2. Performance Criteria for the Process
2.3.3. Links between Enzyme Reaction Performance Parameters
2.3.4. Performance Criteria for Process Schemes, Atom Economy, and Environmental Quotient
3. Isolation and Preparation of Microorganisms
3.1. Introduction
3.2. Screening of New Enzyme Activities
3.2.1. Growth Rates in Nature
3.2.2. Methods in Microbial Ecology
3.3. Strain Development
3.3.1. Range of Industrial Products from Microorganisms
3.3.2. Strain Improvement
3.4. Extremophiles
3.4.1. Extremophiles in Industry
3.5. Rapid Screening of Biocatalysts
4. Molecular Biology Tools for Biocatalysis
4.1. Molecular Biology Basics: DNA versus Protein Level
4.2. DNA Isolation and Purification
4.2.1. Quantification of DNA/RNA
4.3. Gene Isolation, Detection, and Verification
4.3.1. Polymerase Chain Reaction
4.3.2. Optimization of a PCR Reaction
4.3.3. Special PCR Techniques
4.3.4. Southern Blotting
4.3.5. DNA-Sequencing
4.4. Cloning Techniques
4.4.1. Restriction Mapping
4.4.2. Vectors
4.4.3. Ligation
4.5. (Over)expression of an Enzyme Function in a Host
4.5.1. Choice of an Expression System
4.5.2. Translation and Codon Usage in E. coli
4.5.3. Choice of Vector
4.5.4. Expression of Eukaryotic Genes in Yeasts
5. Enzyme Reaction Engineering
5.1. Kinetic Modeling: Rationale and Purpose
5.2. The Ideal World: Ideal Kinetics and Ideal Reactors
5.2.1. The Classic Case: Michaelis-Menten Equation
5.2.2. Design of Ideal Reactors
5.2.3. Integrated Michaelis-Menten Equation in Ideal Reactors
5.3. Enzymes with Unfavorable Binding: Inhibition
5.3.1. Types of Inhibitors
5.3.2. Integrated Michaelis-Menten Equation for Substrate and Product Inhibition
5.3.3. The KI -[I]50 Relationship: Another Useful Application of Mechanism Elucidation
5.4. Reactor Engineering
5.4.1. Configuration of Enzyme Reactors
5.4.2. Immobilized Enzyme Reactor (Fixed-Bed Reactor with Plug-Flow)
5.4.3. Enzyme Membrane Reactor (Continuous Stirred Tank Reactor, CSTR)
5.4.4. Rules for Choice of Reaction Parameters and Reactors
5.5. Enzyme Reactions with Incomplete Mass Transfer: Influence of Immobilization
5.5.1. External Diffusion (Film Diffusion)
5.5.2. Internal Diffusion (Pore Diffusion)
5.5.3. Methods of Testing for Mass Transfer Limitations
5.5.4. Influence of Mass Transfer on the Reaction Parameters
5.6. Enzymes with Incomplete Stability: Deactivation Kinetics
5.6.1. Resting Stability
5.6.2. Operational Stability
5.6.3. Comparison of Resting and Operational Stability
5.6.4. Strategy for the Addition of Fresh Enzyme to Deactiving Enzyme in Continuous Reactors
5.7. Enzymes with Incomplete Selectivity: E-Value and its Optimization
5.7.1. Derivation of the E-Value
5.7.2. Optimization of Separation of Racemates by Choice of Degree of Conversion
5.7.3. Optimization of Enantiomeric Ratio E by Choice of Temperature
6. Applications of Enzymes as Bulk Actives: Detergents, Textiles, Pulp and Paper, Animal Feed
6.1. Application of Enzymes in Laundry Detergents
6.1.1. Overview
6.1.2. Proteases against Blood and Egg Stains
6.1.3. Lipases against Grease Stains
6.1.4. Amylases against Grass and Starch Dirt
6.1.5. Cellulases
6.1.6. Bleach Enzymes
6.2. Enzymes in the Textile Industry: Stone-washed Denims, Shiny Cotton Surfaces
6.2.1. Build-up and Mode of Action of Enzymes for the Textile Industry
6.2.2. Cellulases: the Shinier Look
6.2.3. Stonewashing: Biostoning of Denim: the Worn Look
6.2.4. Peroxidases
6.3. Enzymes in the Pulp and Paper Industry: Bleaching of Pulp with Xylanases or Laccases
6.3.1. Introduction
6.3.2. Wood
6.3.3. Papermaking: Kraft Pulping Process
6.3.4. Research on Enzymes in the Pulp and Paper Industry
6.4. Phytase for Animal Feed: Utilization of Phosphorus
6.4.1. The Farm Animal Business and the Environment
6.4.2. Phytase
6.4.3. Efficacy of Phytase: Reduction of Phosphorus
6.4.4. Efficacy of Phytase: Effect on Other Nutrients
7. Application of Enzymes as Catalysts: Basic Chemicals, Fine Chemicals, Food, Crop Protection, Bulk Pharmaceuticals
7.1. Enzymes as Catalysts in Processes towards Basic Chemicals
7.1.1. Nitrile Hydratase: Acrylamide from Acrylonitrile, Nicotinamide from 3-Cyanopyridine, and 5-Cyanovaleramide from Adiponitrile
7.1.2. Nitrilase: 1,5-Dimethyl-2-piperidone from 2-Methylglutaronitrile
7.1.3. Toluene Dioxygenase: Indigo or Prostaglandins from Substituted Benzenes via cis-Dihydrodiols
7.1.4. Oxynitrilase (Hydroxy Nitrile Lyase, HNL): Cyanohydrins from Aldehydes
7.2. Enzymes as Catalysts in the Fine Chemicals Industry
7.2.1. Chirality, and the Cahn-Ingold-Prelog and Pfeiffer Rules
7.2.2. Enantiomerically Pure Amino Acids
7.2.3. Enantiomerically Pure Hydroxy Acids, Alcohols, and Amines
7.3. Enzymes as Catalysts in the Food Industry
7.3.1. HFCS with Glucose Isomerase (GI)
7.3.2. AspartameO, Artificial Sweetener through Enzymatic Peptide Synthesis
7.3.3. Lactose Hydrolysis
7.3.4. "Nutraceuticals": L-Carnitine as a Nutrient for Athletes and Convalescents (Lonza)
7.3.5. Decarboxylases for Improving the Taste of Beer
7.4. Enzymes as Catalysts towards Crop Protection Chemicals
7.4.1. Intermediate for Herbicides: (R)-2-(4-Hydroxyphenoxypropionic acid (BASF, Germany)
7.4.2. Applications of Transaminases towards Crop Protection Agents: L-Phosphinothricin and (S)-MOIPA
7.5. Enzymes for Large-Scale Pharma Intermediates
7.5.1. Penicillin G (or V) Amidase (PGA, PVA): [beta]-Lactam Precursors, Semi-synthetic [beta]-Lactams
7.5.2. Ephedrine
8. Biotechnological Processing Steps for Enzyme Manufacture
8.1. Introduction to Protein Isolation and Purification
8.2. Basics of Fermentation
8.2.1. Medium Requirements
8.2.2. Sterilization
8.2.3. Phases of a Fermentation
8.2.4. Modeling of a Fermentation
8.2.5. Growth Models
8.2.6. Fed-Batch Culture
8.3. Fermentation and its Main Challenge: Transfer of Oxygen
8.3.1. Determination of Required Oxygen Demand of the Cells
8.3.2. Calculation of Oxygen Transport in the Fermenter Solution
8.3.3. Determination of k[subscript L], a, and k[subscript L]a
8.4. Downstream Processing: Crude Purification of Proteins
8.4.1. Separation (Centrifugation)
8.4.2. Homogenization
8.4.3. Precipitation
8.4.4. Aqueous Two-Phase Extraction
8.5. Downstream Processing: Concentration and Purification of Proteins
8.5.1. Dialysis (Ultrafiltration) (adapted in part from Blanch, 1997)
8.5.2. Chromatography
8.5.3. Drying: Spray Drying, Lyophilization, Stabilization for Storage
8.6. Examples of Biocatalyst Purification
8.6.1. Example 1: Alcohol Dehydrogenase [(R)-ADH from L. brevis (Riebel, 1997)]
8.6.2. Example 2: l-Amino Acid Oxidase from Rhodococcus opacus (Geueke 2002a,b)
8.6.3. Example 3: Xylose Isomerase from Thermoanaerobium Strain JW/SL-YS 489
9. Methods for the Investigation of Proteins
9.1. Relevance of Enzyme Mechanism
9.2. Experimental Methods for the Investigation of an Enzyme Mechanism
9.2.1. Distribution of Products (Curtin-Hammett Principle)
9.2.2. Stationary Methods of Enzyme Kinetics
9.2.3. Linear Free Enthalpy Relationships (LFERs): Bronsted and Hammett Effects
9.2.4. Kinetic Isotope Effects
9.2.5. Non-stationary Methods of Enzyme Kinetics: Titration of Active Sites
9.2.6. Utility of the Elucidation of Mechanism: Transition-State Analog Inhibitors
9.3. Methods of Enzyme Determination
9.3.1. Quantification of Protein
9.3.2. Isoelectric Point Determination
9.3.3. Molecular Mass Determination of Protein Monomer: SDS-PAGE
9.3.4. Mass of an Oligomeric Protein: Size Exclusion Chromatography (SEC)
9.3.5. Mass Determination: Mass Spectrometry (MS) (after Kellner, Lottspeich, Meyer)
9.3.6. Determination of Amino Acid Sequence by Tryptic Degradation, or Acid, Chemical or Enzymatic Digestion
9.4. Enzymatic Mechanisms: General Acid-Base Catalysis
9.4.1. Carbonic Anhydrase II
9.4.2. Vanadium Haloperoxidase
9.5. Nucleophilic Catalysis
9.5.1. Serine Proteases
9.5.2. Cysteine in Nucleophilic Attack
9.5.3. Lipase, Another Catalytic Triad Mechanism
9.5.4. Metalloproteases
9.6. Electrophilic catalysis
9.6.1. Utilization of Metal Ions: ADH, a Different Catalytic Triad
9.6.2. Formation of a Schiff Base, Part I: Acetoacetate Decarboxylase, Aldolase
9.6.3. Formation of a Schiff Base with Pyridoxal Phosphate (PLP): Alanine Racemase, Amino Acid Transferase
9.6.4. Utilization of Thiamine Pyrophosphate (TPP): Transketolase
10. Protein Engineering
10.1. Introduction: Elements of Protein Engineering
10.2. Methods of Protein Engineering
10.2.1. Fusion PCR
10.2.2. Kunkel Method
10.2.3. Site-Specific Mutagenesis Using the QuikChange Kit from Stratagene
10.2.4. Combined Chain Reaction (CCR)
10.3. Glucose (Xylose) Isomerase (GI) and Glycoamylase: Enhancement of Thermostability
10.3.1. Enhancement of Thermostability in Glucose Isomerase (GI)
10.3.2. Resolving the Reaction Mechanism of Glucose Isomerase (GI): Diffusion-Limited Glucose Isomerase?
10.4. Enhancement of Stability of Proteases against Oxidation and Thermal Deactivation
10.4.1. Enhancement of Oxidation Stability of Subtilisin
10.4.2. Thermostability of Subtilisin
10.5. Creating New Enzymes with Protein Engineering
10.5.1. Redesign of a Lactate Dehydrogenase
10.5.2. Synthetic Peroxidases
10.6. Dehydrogenases, Changing Cofactor Specificity
10.7. Oxygenases
10.8. Change of Enantioselectivity with Site-Specific Mutagenesis
10.9. Techniques Bridging Different Protein Engineering Techniques
10.9.1. Chemically Modified Mutants, a Marriage of Chemical Modification and Protein Engineering
10.9.2. Expansion of Substrate Specificity with Protein Engineering and Directed Evolution
11. Applications of Recombinant DNA Technology: Directed Evolution
11.1. Background of Evolvability of Proteins
11.1.1. Purpose of Directed Evolution
11.1.2. Evolution and Probability
11.1.3. Evolution: Conservation of Essential Components of Structure
11.2. Process steps in Directed Evolution: Creating Diversity and Checking for Hits
11.2.1. Creation of Diversity in a DNA Library
11.2.2. Testing for Positive Hits: Screening or Selection
11.3. Experimental Protocols for Directed Evolution
11.3.1. Creating Diversity: Mutagenesis Methods
11.3.2. Creating Diversity: Recombination Methods
11.3.3. Checking for Hits: Screening Assays
11.3.4. Checking for Hits: Selection Procedures
11.3.5. Additional Techniques of Directed Evolution
11.4. Successful Examples of the Application of Directed Evolution
11.4.1. Application of Error-prone PCR: Activation of Subtilisin in DMF
11.4.2. Application of DNA Shuffling: Recombination of p-Nitrobenzyl Esterase Genes
11.4.3. Enhancement of Thermostability: p-Nitrophenyl Esterase
11.4.4. Selection instead of Screening: Creation of a Monomeric Chorismate Mutase
11.4.5. Improvement of Enantioselectivity: Pseudomonas aeruginosa Lipase
11.4.6. Inversion of Enantioselectivity: Hydantoinase
11.4.7. Redesign of an Enzyme's Active Site: KDPG Aldolase
11.5. Comparison of Directed Evolution Techniques
11.5.1. Comparison of Error-Prone PCR and DNA Shuffling: Increased Resistance against Antibiotics
11.5.2. Protein Engineering in Comparison with Directed Evolution: Aminotransferases
11.5.3. Directed Evolution of a Pathway: Carotenoids
12. Biocatalysis in Non-conventional Media
12.1. Enzymes in Organic Solvents
12.2. Evidence for the Perceived Advantages of Biocatalysts in Organic Media
12.2.1. Advantage 1: Enhancement of Solubility of Reactants
12.2.2. Advantage 2: Shift of Equilibria in Organic Media
12.2.3. Advantage 3: Easier Separation
12.2.4. Advantage 4: Enhanced Stability of Enzymes in Organic Solvents
12.2.5. Advantage 5: Altered Selectivity of Enzymes in Organic Solvents
12.3. State of Knowledge of Functioning of Enzymes in Solvents
12.3.1. Range of Enzymes, Reactions, and Solvents
12.3.2. The Importance of Water in Enzyme Reactions in Organic Solvents
12.3.3. Physical Organic Chemistry of Enzymes in Organic Solvents
12.3.4. Correlation of Enzyme Performance with Solvent Parameters
12.4. Optimal Handling of Enzymes in Organic Solvents
12.4.1. Enzyme Memory in Organic Solvents
12.4.2. Low Activity in Organic Solvents Compared to Water
12.4.3. Enhancement of Selectivity of Enzymes in Organic Solvents
12.5. Novel Reaction Media for Biocatalytic Transformations
12.5.1. Substrate as Solvent (Neat Substrates): Acrylamide from Acrylonitrile with Nitrile Hydratase
12.5.2. Supercritical Solvents
12.5.3. Ionic Liquids
12.5.4. Emulsions [Manufacture of Phosphatidylglycerol (PG)]
12.5.5. Microemulsions
12.5.6. Liquid Crystals
12.5.7. Ice-Water Mixtures
12.5.8. High-Density Eutectic Suspensions
12.5.9. High-Density Salt Suspensions
12.5.10. Solid-to-Solid Syntheses
12.6. Solvent as a Parameter for Reaction Optimization ("Medium Engineering")
12.6.1. Change of Substrate Specificity with Change of ReactionM: Specificity of Serine Proteases
12.6.2. Change of Regioselectivity by Organic Solvent Medium
12.6.3. Solvent Control of Enantiospecificity of Nifedipines
13. Pharmaceutical Applications of Biocatalysis
13.1. Enzyme Inhibition for the Fight against Disease
13.1.1. Introduction
13.1.2. Procedure for the Development of Pharmacologically Active Compounds
13.1.3. Process for the Registration of New Drugs
13.1.4. Chiral versus Non-chiral Drugs
13.2. Enzyme Cascades and Biology of Diseases
13.2.1. [beta]-Lactam Antibiotics
13.2.2. Inhibition of Cholesterol Biosynthesis (in part after Suckling, 1990)
13.2.3. Pulmonary Emphysema, Osteoarthritis: Human Leucocyte Elastase (HLE)
13.2.4. AIDS: Reverse Transcriptase and HIV Protease Inhibitors
13.3. Pharmaceutical Applications of Biocatalysis
13.3.1. Antiinfectives (see also Chapter 7, Section 7.5.1)
13.3.2. Anticholesterol Drugs
13.3.3. Anti-AIDS Drugs
13.3.4. High Blood Pressure Treatment
13.4. Applications of Specific Biocatalytic Reactions in Pharma
13.4.1. Reduction of Keto Compounds with Whole Cells
13.4.2. Applications of Pen G Acylase in Pharma
13.4.3. Applications of Lipases and Esterases in Pharma
14. Bioinformatics
14.1. Starting Point: from Consequence (Function) to Sequence
14.1.1. Conventional Path: from Function to Sequence
14.1.2. Novel Path: from Sequence to Consequence (Function)
14.2. Bioinformatics: What is it, Why do we Need it, and Why Now? (NCBI Homepage)
14.2.1. What is Bioinformatics?
14.2.2. Why do we Need Bioinformatics?
14.2.3. Why Bioinformatics Now?
14.3. Tools of Bioinformatics: Databases, Alignments, Structural Mapping
14.3.1. Available Databases
14.3.2. Protein Data Bank (PDB)
14.3.3. Protein Explorer
14.3.4. ExPASy Server: Roche Applied Science Biochemical Pathways
14.3.5. GenBank
14.3.6. SwissProt
14.3.7. Information on an Enzyme: the Example of dehydrogenases
14.4. Applied Bioinformatics Tools, with Examples
14.4.1. BLAST
14.4.2. Aligning Several Protein Sequences using ClustalW
14.4.3. Task: Whole Genome Analysis
14.4.4. Phylogenetic Tree
14.5. Bioinformatics for Structural Information on Enzymes
14.5.1. The Status of Predicting Protein Three-Dimensional Structure
14.6. Conclusion and Outlook
15. Systems Biology for Biocatalysis
15.1. Introduction to Systems Biology
15.1.1. Systems Approach versus Reductionism
15.1.2. Completion of Genomes: Man, Earthworm, and Others
15.2. Genomics, Proteomics, and other -omics
15.2.1. Genomics
15.2.2. Proteomics
15.3. Technologies for Systems Biology
15.3.1. Two-Dimensional Gel Electrophoresis (2D PAGE)
15.3.2. Mass Spectroscopy
15.3.3. DNA Microarrays
15.3.4. Protein Microarrays
15.3.5. Applications of Genomics and Proteomics in Biocatalysis
15.4. Metabolic Engineering
15.4.1. Concepts of Metabolic Engineering
15.4.2. Examples of Metabolic Engineering
16. Evolution of Biocatalytic Function
16.1. Introduction
16.1.2. Congruence of Sequence, Function, Structure, and Mechanism
16.2. Search Characteristics for Relatedness in Proteins
16.2.1. Classification of Relatedness of Proteins: the -log Family
16.2.2. Classification into Protein Families
16.2.3. Dominance of Different Mechanisms
16.3. Evolution of New Function in Nature
16.3.1. Dual-Functionality Proteins
16.3.2. Gene Duplication
16.3.3. Horizontal Gene Transfer (HGT)
16.3.4. Circular Permutation
16.4. [alpha]/[beta]-Barrel Proteins as a Model for the Investigation of Evolution
16.4.1. Why Study [alpha]/[beta]-Barrel Proteins?
16.4.2. Example of Gene Duplication: Mandelate and a-Ketoadipate Pathways
16.4.3. Exchange of Function in the Aromatic Biosynthesis Pathways: Trp and His Pathways
17. Stability of Proteins
17.1. Summary: Protein Folding, First-Order Decay, Arrhenius Law
17.1.1. The Protein Folding Problem
17.1.2. Why do Proteins Fold?
17.2. Two-State Model: Thermodynamic Stability of Proteins (Unfolding)
17.2.1. Protein Unfolding and Deactivation
17.2.2. Thermodynamics of Proteins
17.3. Three-State Model: Lumry-Eyring Equation
17.3.1. Enzyme Deactivation
17.3.2. Empirical Deactivation Model
17.4. Four-State Model: Protein Aggregation
17.4.1. Folding, Deactivation, and Aggregation
17.4.2. Model to Account for Competition between Folding and Inclusion Body Formation
17.5. Causes of Instability of Proteins: [Delta]G [less than sign] 0, [gamma](t), A
17.5.1. Thermal Inactivation
17.5.2. Deactivation under the Influence of Stirring
17.5.3. Deactivation under the Influence of Gas Bubbles
17.5.4. Deactivation under the Influence of Aqueous/Organic Interfaces
17.5.5. Deactivation under the Influence of Salts and Solvents
17.6. Biotechnological Relevance of Protein Folding: Inclusion Bodies
17.7. Summary: Stabilization of Proteins
17.7.1. Correlation between Stability and Structure
18. Artificial Enzymes
18.1. Catalytic Antibodies
18.1.1. Principle of Catalytic Antibodies: Connection between Chemistry and Immunology
18.1.2. Test Reaction Selection, Haptens, Mechanisms, Stabilization
18.1.3. Breadth of Reactions Catalyzed by Antibodies
18.2. Other Proteinaceous Catalysts: Ribozymes and Enzyme Mimics
18.2.1. Ribozymes: RNA World before Protein World?
18.2.2. Proteinaceous Enzyme Mimics
18.3. Design of Novel Enzyme Activity: Enzyme Models (Synzymes)
18.3.1. Introduction
18.3.2. Enzyme Models on the Basis of the Binding Step: Diels-Alder Reaction
18.3.3. Enzyme Models with Binding and Catalytic Effects
18.4. Heterogenized/Immobilized Chiral Chemical Catalysts
18.4.1. Overview of Different Approaches
18.4.2. Immobilization with Polyamino Acids as Chiral Polymer Catalysts
18.4.3. Immobilization on Resins or other Insoluble Carriers
18.4.4. Heterogenization with Dendrimers
18.4.5. Retention of Heterogenized Chiral Chemical Catalysts in a Membrane Reactor
18.4.6. Recovery of Organometallic Catalysts by Phase Change: Liquid-Liquid Extraction
18.5. Tandem Enzyme Organometallic Catalysts
19. Design of Biocatalytic Processes
19.1. Design of Enzyme Processes: High-Fructose Corn Syrup (HFCS)
19.1.1. Manufacture of HFCS from Glucose with Glucose Isomerase (GI): Process Details
19.1.2. Mathematical Model for the Description of the Enzyme Kinetics of Glucose Isomerase (GI)
19.1.3. Evaluation of the Model of the GI Reaction in the Fixed-Bed Reactor
19.1.4. Productivity of a Fixed-Bed Enzyme Reactor
19.2. Processing of Fine Chemicals or Pharmaceutical Intermediates in an Enzyme Membrane Reactor
19.2.1. Introduction
19.2.2. Determination of Process Parameters of a Membrane Reactor
19.2.3. Large-Scale Applications of Membrane Reactors
19.3. Production of Enantiomerically Pure Hydrophobic Alcohols: Comparison of Different Process Routes and Reactor Configurations
19.3.1. Isolated Enzyme Approach
19.3.2. Whole-Cell Approach
19.3.3. Organometallic Catalyst Approach
19.3.4. Comparison of Different Catalytic Reduction Strategies
20. Comparison of Biological and Chemical Catalysts for Novel Processes
20.1. Criteria for the Judgment of (Bio-)catalytic Processes
20.1.1. Discussion: Jacobsen's Five Criteria
20.1.2. Comment on Jabobsen's Five Criteria
20.2. Position of Biocatalysis in Comparison to Chemical Catalysts for Novel Processes
20.2.1. Conditions and Framework for Processes of the Future
20.2.2. Ibuprofen (Painkiller)
20.2.3. Indigo (Blue Dye)
20.2.4. Menthol (Peppermint Flavoring Agent)
20.2.5. Ascorbic Acid (Vitamin C)
20.3. Pathway Engineering through Metabolic Engineering
20.3.1. Pathway Engineering for Basic Chemicals: 1,3-Propanediol
20.3.2. Pathway Engineering for Pharmaceutical Intermediates: cis-Aminoindanol
Index

Biocatalysis /

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