Biocatalysts and Enzyme Technology. (2012)

• Record Type: Book
• Other Names: Buchholz, Klaus; Kasche, Volker; Bornscheuer, U. T; ProQuest (Firm)
• Contents: Biocatalysts and Enzyme Technology -- Contents -- Preface to the Second Edition -- Preface to the First German Edition -- Preface to the First English Edition -- 1 Introduction to Enzyme Technology -- 1.1 Introduction -- 1.1.1 What are Biocatalysts? -- 1.1.2 Bio- and Chemocatalysts -- Similarities and Differences -- 1.2 Goals and Potential of Biotechnological Production Processes -- 1.3 Historical Highlights of Enzyme Technology/Applied Biocatalysis -- 1.3.1 Early Developments -- 1.3.2 Scientific Progress Since 1890: The Biochemical Paradigm -- Growing Success in Application -- 1.3.3 Developments Since 1950 -- 1.4 Biotechnological Processes: The Use of Isolated or Intracellular Enzymes as Biocatalysts -- 1.5 Advantages and Disadvantages of Enzyme-Based Production Processes -- 1.6 Goals and Essential System Properties for New or Improved Enzyme Processes -- 1.6.1 Goals -- 1.6.2 Essential System Properties for Rational Design of an Enzyme Process -- 1.6.3 Current Use and Potential of Enzyme Technology -- Exercises -- Literature -- References -- 2 Basics of Enzymes as Biocatalysts -- 2.1 Introduction -- 2.2 Enzyme Classification -- 2.3 Enzyme Synthesis and Structure -- 2.4 Enzyme Function and Its General Mechanism -- 2.5 Free Energy Changes and the Specificity of Enzyme-Catalyzed Reactions -- 2.6 Equilibrium- and Kinetically Controlled Reactions Catalyzed by Enzymes -- 2.7 Kinetics of Enzyme-Catalyzed Reactions -- 2.7.1 Quantitative Relations for Kinetic Characteristics and Selectivities of Enzyme-Catalyzed Reactions -- 2.7.1.1 Turnover Number (kcat) and Michaelis-Menten Constant (Km) -- 2.7.1.2 Stereoselectivities for Equilibrium- and Kinetically Controlled Reactions -- 2.7.2 Dependence of kcat, Km, and Selectivities on pH, Temperature, Inhibitors, Activators, and Ionic Strength in Aqueous Solutions -- 2.7.2.1 pH Dependence. 2.7.2.2 Temperature Dependence -- 2.7.2.3 Binding of Activator and Inhibitor Molecules -- 2.7.2.4 Influence of Ionic Strength -- 2.8 End Points of Enzyme Processes and Amount of Enzyme Required to Reach the End Point in a Given Time -- 2.8.1 Temperature Dependence of the Product Yield -- 2.8.2 pH Dependence of the Yield at the End Point -- 2.8.3 End Points for Kinetic Resolutions of Racemates -- 2.9 Enzyme-Catalyzed Processes with Slightly Soluble Products and Substrates -- 2.9.1 Enzyme-Catalyzed Processes in Aqueous Suspensions -- 2.9.1.1 Changes in Rates, kcat, Km, and Selectivities in These Systems Compared with Homogeneous Aqueous Solutions -- 2.9.2 Enzyme-Catalyzed Processes in Nonconventional Solvents Where Products and Substrates Are Dissolved (and the Enzyme Suspended) -- 2.9.2.1 Changes in Rates, kcat, Km, and Selectivities in These Systems Compared with Homogeneous Aqueous Solutions -- 2.10 Stability, Denaturation, and Renaturation of Enzymes -- 2.11 Better Enzymes by Natural Evolution, In Vitro Evolution, or Rational Enzyme Engineering -- 2.11.1 Changes in Enzyme Properties by Natural Evolution -- 2.11.1.1 kcat and Km -- 2.11.1.2 Enzyme Stability -- 2.11.1.3 Stereoselectivity -- 2.11.1.4 Selectivity in Kinetically Controlled Synthesis of Condensation Products -- Exercises -- Literature -- References -- 3 Enzyme Discovery and Protein Engineering -- 3.1 Enzyme Discovery -- 3.2 Strategies for Protein Engineering -- 3.2.1 Rational Protein Design -- 3.2.2 Directed (Molecular) Evolution -- 3.2.2.1 Methods to Create Mutant Libraries -- 3.2.2.2 Assay Systems -- 3.2.2.3 Examples -- 3.2.3 Focused Directed Evolution -- 3.3 Computational Design of Enzymes -- Exercises -- References -- 4 Enzymes in Organic Chemistry -- 4.1 Introduction -- 4.1.1 Kinetic Resolution or Asymmetric Synthesis -- 4.2 Examples -- 4.2.1 Oxidoreductases (EC 1). 4.2.1.1 Dehydrogenases (EC 1.1.1.-, EC 1.2.1.-, EC 1.4.1.-) -- 4.2.1.2 Oxygenases -- 4.2.1.3 Peroxidases (EC 1.11.1.10) -- 4.2.1.4 Enoate Reductases (EC 1.4.1.31) -- 4.2.1.5 Monoamine Oxidases -- 4.2.2 Transaminases -- 4.2.3 Hydrolases (EC 3.1) -- 4.2.3.1 Lipases (EC 3.1.1.3) -- 4.2.3.2 Esterases (EC 3.1.1.1) -- 4.2.3.3 Peptidases, Acylases, and Amidases -- 4.2.3.4 Epoxide Hydrolases (EC 3.3.2.3) -- 4.2.3.5 Dehalogenases (EC 3.8.1.5) -- 4.2.3.6 Nitrilases (EC 3.5.5.1) and Nitrile Hydratases (EC 4.2.1.84) -- 4.2.3.7 Hydantoinases (EC 3.5.2.-) -- 4.2.4 Lyases (EC 4) -- 4.2.4.1 Hydroxynitrile Lyases (EC 4.1.2.-) -- 4.2.4.2 Aldolases (EC 4.1.2.-, EC 4.1.3.-) -- 4.2.5 Isomerases (EC 5) -- Exercises -- Literature -- References -- 5 Cells Designed by Metabolic Engineering as Biocatalysts for Multienzyme Biotransformations -- 5.1 Introduction -- 5.2 A Short Introduction to Metabolic Engineering -- 5.3 Examples -- 5.3.1 1, 3-Propanediol -- 5.3.2 Synthesis of "Biodiesel" and Other Fatty Acid Derivatives -- 5.3.3 Conversion of Cellulosics to Ethanol -- 5.3.4 Conversion of D-Fructose to D-Mannitol -- 5.3.5 Synthesis of L-Ascorbic Acid -- 5.3.6 Other Examples -- Exercises -- Literature -- References -- 6 Enzyme Production and Purification -- 6.1 Introduction -- 6.2 Enzyme Sources -- 6.2.1 Animal and Plant Tissues -- 6.2.2 Wild-Type Microorganisms -- 6.2.3 Recombinant Microorganisms -- 6.3 Improving Enzyme Yield -- 6.3.1 Processes that Influence the Enzyme Yield -- 6.4 Increasing the Yield of Periplasmic and Extracellular Enzymes -- 6.4.1 Penicillin Amidase -- 6.4.2 Lipase -- 6.5 Downstream Processing of Enzymes -- 6.5.1 Static and Dynamic Properties of Chromatographic Adsorbents that Must Be Known for a Rational Design of Chromatographic Protein Purification -- 6.5.1.1 Static Properties -- 6.5.1.2 Dynamic Properties. 6.5.2 Chromatographic Puri.cation of Enzymes: Problems and Procedures -- 6.5.2.1 Problems -- 6.5.2.2 Procedures -- 6.5.3 Chromatographic Purification and Conditioning of Technical and Therapeutic Enzymes -- 6.5.3.1 Technical Enzymes -- 6.5.3.2 Enzymes for Therapy and Diagnostics -- 6.6 Regulations Based on Risk Assessments/Safety Criteria that Influence the Production of Enzymes and Their Use for Analytical, Pharmaceutical, Scientific, and Technical Purposes -- 6.6.1 Regulations Governing the Use of Genetically Modified Microorganisms for the Production of Enzymes in Laboratories and Production Facilities -- 6.6.2 Regulations Governing the Use of Enzymes Produced in Wild-Type or Recombinant Organisms -- Exercises -- Literature -- References -- 7 Application of Enzymes in Solution: Soluble Enzymes and Enzyme Systems -- 7.1 Introduction and Areas of Application -- 7.1.1 The Impact of Genetic Engineering -- 7.1.2 Medium Design -- 7.1.3 Safety Aspects -- 7.2 Space-Time Yield and Productivity -- 7.3 Examples for the Application of Enzymes in Solution -- 7.3.1 Survey -- 7.3.1.1 Food Applications -- 7.3.1.2 Other Industrial Applications -- 7.3.2 Starch Processing -- 7.3.3 Detergents -- 7.4 Membrane Systems and Processes -- Exercises -- Literature -- References -- 8 Immobilization of Enzymes (Including Applications) -- 8.1 Principles -- 8.1.1 Parameters of Immobilization -- 8.2 Carriers -- 8.2.1 Inorganic Carriers -- 8.2.2 Polysaccharides -- 8.2.3 Synthetic Polymers -- 8.3 Binding Methods -- 8.3.1 Adsorption -- 8.3.2 Covalent Binding -- 8.4 Examples: Application of Immobilized Enzymes -- 8.4.1 Hydrolysis and Biotransformation of Carbohydrates -- 8.4.2 Hydrolysis and Synthesis of Penicillins and Cephalosporins -- 8.4.3 Further Processes -- 8.4.3.1 Amino Acid, Peptide, and Amide Synthesis -- 8.4.3.2 Application of Lipases -- Exercises -- Literature.
• Edition: 2nd ed
• Publisher Details: Weinheim Somerset : Wiley-Blackwell John Wiley & Sons, Incorporated
• Publication Date: 2012
• Copyright Date: 2011
• Extent: 1 online resource (674 pages)
• Subjects: 660.634; Biotechnology; Catalysis; Enzymes; Enzymes -- Industrial applications; Enzymes -- Biotechnology; Biotechnology; Catalysis; Enzymes; Enzymes -- Biotechnology; Enzymes -- Industrial applications; Electronic books
• Languages: English
• ISBNs: 9783527672004; 3527672001
• Related ISBNs: 9783527329892
• Notes: Note: Includes bibliographical references and index.; Note: References -- 9 Immobilization of Microorganisms and Cells -- 9.1 Introduction -- 9.2 Fundamental Aspects -- 9.3 Immobilization by Aggregation/Flocculation -- 9.4 Immobilization by Entrapment -- 9.4.1 Entrapment in Polymeric Networks -- 9.4.2 Entrapment in Ionotropic Gels -- 9.4.2.1 Principle -- 9.4.2.2 Examples -- 9.5 Adsorption -- 9.6 Adhesion -- 9.6.1 Basic Considerations -- 9.6.2 Applications -- 9.6.2.1 Adherent Mammalian Cells for Biopharmaceuticals Production -- 9.6.2.2 Anaerobic Wastewater Treatment -- 9.6.2.3 Nitrogen Elimination (Nitrification and Denitrification) -- 9.6.2.4 Exhaust Gas Purification -- 9.7 Perspectives -- 9.7.1 Biofilm Catalysis -- 9.7.2 Microbial Fuel Cells -- Exercises -- References -- 10 Characterization of Immobilized Biocatalysts -- 10.1 Introduction -- 10.2 Factors Influencing the Space-Time Yield of Immobilized Biocatalysts -- 10.3 Effectiveness Factors for Immobilized Biocatalysts -- 10.4 Mass Transfer and Reaction -- 10.4.1 Maximal Reaction Rate of Immobilized Biocatalysts as a Function of Particle Radius -- 10.4.2 Calculation of Effectiveness Factors and Concentration Profiles Inside and Outside the Particles -- 10.5 Space-Time Yields and Effectiveness Factors for Different Reactors -- 10.5.1 Continuous Stirred Tank Reactor -- 10.5.2 Packed Bed Reactor or Stirred Batch Reactor -- 10.5.3 Comparison of CST and PB Reactors -- 10.6 Determination of Essential Properties of Immobilized Biocatalysts -- 10.6.1 Physicochemical Properties -- 10.6.1.1 Immobilized Biocatalyst Distribution and Conformation -- 10.6.1.2 Stationary Charge Density in the Support -- 10.6.2 Kinetic Characterization of Immobilized Biocatalysts: Influence of Support Properties on the Nano- and Micrometer Level in Aqueous and Other Systems -- 10.6.2.1 Determination of V 0max, k0cat, Substrate/Product Concentration, and pH Gradients.; Note: Description based on publisher supplied metadata and other sources.
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