Torres / Ayala Biocatalysis Based on Heme Peroxidases

Peroxidases as Potential Industrial Biocatalysts
1. Auflage 2010
ISBN: 978-3-642-12627-7
Verlag: Springer
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)

E-Book, Englisch, 358 Seiten

The last systematic description of heme peroxidases was published in 1999 by Brian Dunford, from the University of Alberta in Canada. The book Heme per- idases covers discussion on three-dimensional structure, reaction mechanism, kinetics, and spectral properties of representative enzymes from bacterial, plant, fungal, and animal origin. Since 1999, vast information on basic but also applied aspects of heme peroxidases has been generated. We believe fusion of these two aspects will bene?t research of those dedicated to development of biocatalytic process. The aim of this book is to present recent advances on basic aspects such as evolution, structure–function relation, and catalytic mechanism, as well as applied aspects, such as bioreactor and protein engineering, in order to provide the tools for rational design of enhanced biocatalysts and biocatalytic processes. The book does not include an exhaustive listing of references but rather a selected collection to enrich discussion and to allow envisioning future directions for research. This book is organized in three parts. In Part I, current knowledge of structure and mechanism of peroxidases is covered. From the molecular phylogeny, going through the in?uence of structural factors over oxidative ability to the molecular mechanism of catalysis, the authors intend to provide an understanding of per- idases at the molecular level. The understanding of the fundamental behavior of peroxidases will allow further adequation, design, and/or optimization of pero- dase-based catalysis to a particular process. In Part II, research on potential applications of peroxidases in several ?elds is presented and discussed.

Autoren/Hrsg.

Torres, Eduardo

Ayala, Marcela

Inhaltsverzeichnis

1;Preface;6
2;Contents;8
3;Contributors;10
4;Chapter 1: Introduction;14
4.1;References;17
5;Chapter 2: Molecular Phylogeny of Heme Peroxidases;19
5.1;2.1 Systematic Classification of Peroxidases;20
5.2;2.2 The Peroxidase-Cyclooxygenase Superfamily;21
5.2.1;2.2.1 Bacterial Members: Peroxicins, Peroxidockerins, Primordial Peroxidases;22
5.2.2;2.2.2 Bacterial, Fungal, and Animal Cyclooxygenases;24
5.2.3;2.2.3 Ecdysozoan and Echinozoan Peroxinectins;24
5.2.4;2.2.4 Ecdysozoan and Deuterostomian Peroxidasins;24
5.2.5;2.2.5 Chordata Peroxidases;28
5.3;2.3 The Peroxidase-Catalase Superfamily;29
5.3.1;2.3.1 Class I: Peroxidases;31
5.3.1.1;2.3.1.1 Catalase-Peroxidases (KatGs);31
5.3.1.2;2.3.1.2 Ascorbate Peroxidases, Cytochrome c Peroxidases, and Their Putative Hybrid Types;33
5.3.2;2.3.2 Class II: Manganese, Lignin Peroxidases, and Versatile Peroxidases;35
5.3.3;2.3.3 Class III: Plant Secretory Peroxidases;35
5.4;2.4 Di-Heme Peroxidase Family;38
5.5;2.5 Dyp-Type Heme Peroxidase Family;38
5.6;2.6 Haloperoxidase Family;42
5.7;2.7 Conclusions;44
5.8;References;44
6;Chapter 3: Structural and Functional Features of Peroxidases with a Potential as Industrial Biocatalysts;48
6.1;3.1 General Structural Characteristics of Heme Peroxidases;49
6.1.1;3.1.1 Superfamily of Plant, Fungal, and Bacterial Peroxidases;49
6.1.2;3.1.2 Superfamily of Mammalian and Other Animal Peroxidases;50
6.1.3;3.1.3 Other Heme Peroxidase (super)Families;53
6.2;3.2 Basidiomycete Peroxidases;54
6.2.1;3.2.1 White-Rot Fungal Peroxidases: Biotechnological Interest;54
6.2.2;3.2.2 Evolutionary Relationships of Basidiomycete Peroxidases;55
6.3;3.3 Ligninolytic Peroxidases;57
6.3.1;3.3.1 Heme Environment;58
6.3.2;3.3.2 Manganese Oxidation Site;58
6.3.3;3.3.3 LRET Substrate Oxidation at an Exposed Tryptophan;60
6.3.4;3.3.4 Influence of the Catalytic Tryptophan Environment;61
6.4;3.4 Heme-Thiolate Peroxidases;62
6.4.1;3.4.1 Heme Environment;63
6.4.2;3.4.2 Substrate Oxidation Sites;64
6.5;3.5 Dye-Decolorizing Peroxidases;64
6.6;3.6 Conclusions;65
6.7;References;66
7;Chapter 4: Redox Potential of Peroxidases;71
7.1;4.1 Introduction;71
7.2;4.2 Redox Potential of the Fe(III)/Fe(II) Couple in Heme Proteins;72
7.2.1;4.2.1 Thermodynamics of Ferric Heme Reduction;72
7.2.2;4.2.2 Influence of the Primary Coordination Sphere on Redox Potential;74
7.2.3;4.2.3 Influence of the Protein Matrix on Redox Potential;75
7.3;4.3 Redox Potential of Heme Peroxidases;76
7.3.1;4.3.1 Redox Potential of the Catalytic Species;77
7.3.2;4.3.2 Modulation of Redox Potential;78
7.4;4.4 Methods to Measure or Estimate Redox Potential of Heme Peroxidases;81
7.5;4.5 Conclusions;82
7.6;References;83
8;Chapter 5: Catalytic Mechanisms of Heme Peroxidases;88
8.1;5.1 Introduction;89
8.2;5.2 Peroxidase Catalytic Cycle;89
8.2.1;5.2.1 Ferric Peroxidase;91
8.2.2;5.2.2 Compound 0;92
8.2.3;5.2.3 Compound I: Porphyrin Radical;92
8.2.4;5.2.4 Compound I: Protein Radical;93
8.2.5;5.2.5 Compound II;94
8.2.6;5.2.6 Compound III;94
8.3;5.3 Self-Processing of Peroxidases;95
8.3.1;5.3.1 Protein Modifications;95
8.3.2;5.3.2 Heme-Protein Crosslinking;97
8.3.3;5.3.3 Heme Modification by Metabolites;98
8.4;5.4 Substrate Oxidations;102
8.4.1;5.4.1 Oxidative Properties;102
8.4.2;5.4.2 One-Electron Oxidations;103
8.4.2.1;5.4.2.1 Phenols;103
8.4.2.2;5.4.2.2 Aromatic Amines;105
8.4.2.3;5.4.2.3 Carbon Oxidation;106
8.4.2.4;5.4.2.4 Electron Transfer Relay;106
8.4.3;5.4.3 Two-Electron Oxidations;107
8.4.3.1;5.4.3.1 Halogenation;107
8.4.3.2;5.4.3.2 Oxygen Transfer;109
8.4.3.3;5.4.3.3 Sequential One-Electron Oxidations;109
8.5;5.5 Conclusions;110
8.6;References;111
9;Chapter 6: Potential Applications of Peroxidases in the Fine Chemical Industries;118
9.1;6.1 Selective Oxidations Catalyzed by Peroxidases;118
9.1.1;6.1.1 Introduction;118
9.1.2;6.1.2 Reactions Driven by Radical Mechanisms;121
9.1.2.1;6.1.2.1 Oxidation of Phenols (oxidative dehydrogenation of phenols);122
9.1.2.2;6.1.2.2 Oxidation of Amines;127
9.1.2.3;6.1.2.3 Oxidation of Catechols;128
9.1.2.4;6.1.2.4 Nitration of Phenols;128
9.1.3;6.1.3 Insertion of Oxygen Atoms into Substrate Molecules;130
9.1.3.1;6.1.3.1 Epoxidation;130
9.1.3.2;6.1.3.2 N-Oxidation;131
9.1.3.3;6.1.3.3 Aromatic Hydroxylation;132
9.1.3.4;6.1.3.4 Aliphatic Hydrocarbon Hydroxylation;132
9.1.3.5;6.1.3.5 Indole Oxidation;133
9.1.3.6;6.1.3.6 Alcohol Oxidation;133
9.1.3.7;6.1.3.7 Sulfoxidation;133
9.1.4;6.1.4 Activation of Halogens;136
9.1.5;6.1.5 Activation of Nitrite;137
9.2;6.2 Analytical Applications of Peroxidases;139
9.2.1;6.2.1 ELISA;139
9.2.2;6.2.2 Biosensors;140
9.3;6.3 Prospective Applications of Peroxidases in the Fine Chemical and Pharmaceutical Industries;142
9.3.1;6.3.1 Native and Modified Peroxidases;142
9.3.2;6.3.2 Proteins with Pseudoperoxidase Activity;143
9.3.3;6.3.3 Heme-Peptide Complexes;146
9.4;References;150
10;Chapter 7: Grafting of Functional Molecules: Insights into Peroxidase-Derived Materials;161
10.1;7.1 Introduction;162
10.2;7.2 Production of Functional Polymers;163
10.2.1;7.2.1 Phenolic Resins;163
10.2.2;7.2.2 Cardanol;166
10.2.3;7.2.3 Poly(methyl methacrylate) ;167
10.2.4;7.2.4 Acrylamide;167
10.2.5;7.2.5 Polystryrene;168
10.2.6;7.2.6 Conducting Polymers;168
10.2.7;7.2.7 Fluorescent Naphthol-Based Polymers;170
10.3;7.3 Surface Modification of Complex Polymers;171
10.3.1;7.3.1 Bonding Wood Fibers;171
10.3.2;7.3.2 Manufacturing of Medium Density Fiber boards;172
10.3.3;7.3.3 Modification of Thermomechanical Pulp;172
10.3.4;7.3.4 Textile Fibers;174
10.3.5;7.3.5 Hair Dyeing;175
10.3.6;7.3.6 Surface Modification of Polyphenylene-2,6-Benzobisthiazole Fibers;176
10.3.7;7.3.7 Biopolymer Cross-linking;177
10.4;7.4 Conclusions;178
10.5;References;178
11;Chapter 8: Applications and Prospective of Peroxidase Biocatalysis in the Environmental Field;184
11.1;8.1 Introduction;185
11.2;8.2 Phenols;187
11.3;8.3 Halogenated Phenols;189
11.4;8.4 Chloroanilines;190
11.5;8.5 Polycyclic Aromatic Hydrocarbons;192
11.6;8.6 Endocrine Disruptive Chemicals;193
11.7;8.7 Pesticides;196
11.8;8.8 Dioxins;198
11.9;8.9 Polychlorinated Biphenyls (PCBs);200
11.10;8.10 Dyes;201
11.11;8.11 Challenges for the Industrial Applications of Peroxidase for Environmental Purposes;203
11.12;References;205
12;Chapter 9: Enzyme Technology of Peroxidases: Immobilization, Chemical and Genetic Modification;213
12.1;9.1 Introduction;214
12.2;9.2 Immobilization;223
12.2.1;9.2.1 Immobilization on Inorganic Supports;224
12.2.2;9.2.2 Immobilization on Organic Supports;228
12.3;9.3 Chemical Modification;231
12.3.1;9.3.1 Chemical Modification of Superficial Amino Acids;232
12.3.2;9.3.2 Heme Modification;235
12.4;9.4 Genetic Engineering of Peroxidases;237
12.5;9.5 Conclusions;241
12.6;References;241
13;Chapter 10: Reactor Engineering;248
13.1;10.1 Characteristics of Peroxidative Reactions Influencing Reactor Design;249
13.1.1;10.1.1 Enzyme;249
13.1.2;10.1.2 Oxidizing Agent;250
13.1.3;10.1.3 Mediators;251
13.1.4;10.1.4 Additives;251
13.1.5;10.1.5 Oxygen;252
13.1.6;10.1.6 Temperature and pH;252
13.1.7;10.1.7 Agitation;253
13.1.8;10.1.8 Immobilization;254
13.1.9;10.1.9 Presence of Organic Solvents;254
13.2;10.2 Reactor Configuration;255
13.2.1;10.2.1 Discontinuous Stirred Tank Reactor;256
13.2.2;10.2.2 Continuous Stirred Tank Reactor;260
13.2.3;10.2.3 Membrane Reactor;262
13.2.4;10.2.4 Plug Flow Reactor;265
13.2.4.1;10.2.4.1 Fixed Bed Reactor;266
13.2.4.2;10.2.4.2 Fluidized Bed Reactor;266
13.2.4.3;10.2.4.3 Two-Stage Reactor;267
13.2.5;10.2.5 Electrochemical Reactor;268
13.3;10.3 Enzymatic Membrane Reactor;269
13.3.1;10.3.1 Dye Decolorization in a One-Stage Enzymatic Membrane Reactor;269
13.3.1.1;10.3.1.1 Reactor Selection;270
13.3.1.2;10.3.1.2 Selection of the Ultrafiltration Membrane;270
13.3.1.3;10.3.1.3 Reactor Configuration;271
13.3.1.4;10.3.1.4 Reactor Operation;271
13.3.1.5;10.3.1.5 Control Systems;274
13.3.2;10.3.2 Other Applications of One-Stage Enzymatic Membrane Reactors;276
13.3.2.1;10.3.2.1 Treatment of Phenolic Effluents;276
13.3.2.2;10.3.2.2 Oxidation of Indole to Oxindole;278
13.3.3;10.3.3 Two-Stage Enzymatic Membrane Reactor;278
13.4;10.4 Biphasic Reactors;282
13.4.1;10.4.1 Solvent Selection;282
13.4.2;10.4.2 Effect of Substrates and Cosubstrates of VP;283
13.4.3;10.4.3 Selection of a Surfactant;284
13.4.4;10.4.4 Enhancement of Mass Transfer and Enzyme Stability;284
13.4.5;10.4.5 Degradation of Anthracene in TPPB;286
13.5;References;287
14;Chapter 11: Deactivation of Hemeperoxidases by Hydrogen Peroxide: Focus on Compound III;294
14.1;11.1 Molecular Bases of the H2O2-Dependent Deactivation of Peroxidases;294
14.1.1;11.1.1 Compound III Formation Pathways;295
14.1.2;11.1.2 Compound III Decay Pathways;299
14.2;11.2 Structure and Electronic Configuration of Compound III;301
14.2.1;11.2.1 Optical Spectrum of Compound III in the Visible Region;301
14.2.2;11.2.2 Circular Dichroism Spectrum of Compound III;302
14.2.3;11.2.3 Magnetic Circular Dichroism Spectrum of Compound III;303
14.2.4;11.2.4 Electron Paramagnetic Resonance Spectrum of Compound III;304
14.2.5;11.2.5 Resonance Raman Spectrum of Compound III;305
14.2.6;11.2.6 Theoretical Study of Compound III Model Systems;307
14.2.7;11.2.7 Mössbauer Spectroscopy of Compound III;308
14.2.8;11.2.8 X-ray Diffraction Crystallography of Compound III;308
14.3;11.3 Conclusions;310
14.4;References;311
15;Chapter 12: Heterologous Expression of Peroxidases;318
15.1;12.1 Production of Peroxidases in E. coli;319
15.2;12.2 Production of Peroxidases in Saccharomyces cerevisiae and Pichia spp.;320
15.3;12.3 Production of Peroxidases in Baculovirus;321
15.4;12.4 Production of Peroxidases in White-Rot Fungi;322
15.5;12.5 Production of Peroxidases in Filamentous Fungi;323
15.6;12.6 Production of Heme-Peroxidases in Aspergillus;324
15.6.1;12.6.1 Expression Systems and Detection;324
15.6.2;12.6.2 Large-Scale Production with Bioreactors;326
15.7;12.7 Bottlenecks for Heterologous Protein Expression in Filamentous Fungi;327
15.7.1;12.7.1 The Secretory Pathway of Aspergillus;328
15.7.2;12.7.2 Limitations to Protein Production;329
15.7.2.1;12.7.2.1 Glycosylation and Proteolysis;329
15.7.2.2;12.7.2.2 Protein Folding and Maturation;330
15.7.2.3;12.7.2.3 Cofactor Incorporation;331
15.8;12.8 Conclusions;332
15.9;References;332
16;Chapter 13: A Compendium of Bio-Physical-Chemical Properties of Peroxidases;337
16.1;References;351
17;Index;355