.

0 (hodnocen0 x )

EB

EB

Boca Raton, FL : Pan Stanford, an imprint of Taylor and Francis, 2016.

1 online zdroj

ISBN 9781315185392 (e-book : PDF)

ISBN 9789814669795 (e-book)

ISBN 9789814669788 (vázáno)

Pan Stanford series on biocatalysis

Tištěná verze : ISBN 9789814669788

1 Basics in Carbohydrate Chemistry / Heinrich H hnerfuss -- 1.1 Introduction -- 1 1.2 Classification of Carbohydrates -- 1.2.1 Monosaccharides -- 2 1.2.1.1 Configuration and nomenclature -- 1.2.1.2 Ring structures of carbohydrates -- 5 1.2.2 Disaccharides -- 1.2.3 Oligosaccharides -- 12 1.2.4 Polysaccharides -- 1.3 Reactions of carbohydrates -- 16 1.3.1 Oxidation of carbohydrates -- 1.3.2 Reduction of Carbohydrates -- 1.3.3 Nucleophilic Reactions -- 1.3.4 Acylation and Alkylation of Monosaccharides -- 1.3.5 Formation of O-Glycosides and N-Glycosides -- 1.4 Glycoproteins -- 2 Glycoconjugates: A Brief Overview / Peter Grunwald -- 2.1 Introduction -- 2.2 Glycoconjugates: General Features and Glycosylation -- 2.3 Glycoproteins -- 2.3.1 Recombinant Glycoproteins -- 2.4 N-Glycosylation of Proteins -- 2.4.1 Quality Control and ER-Associated Degradation -- 2.4.2 Cytosolic Degradation -- 2.5 Mucins --

2.6 Glycosaminoglycans and Proteoglycans -- 2.6.1 Heparin -- 2.6.2 Heparan Sulfate -- 2.6.3 Chondroitin and Dermatan Sulfate -- 2.6.4 Keratan Sulfate -- 2.7 Peptidoglycans -- 2.8 Glycolipids, Lipopolysaccharides, and Toxins -- 2.8.1 Lipopolysaccharides -- 2.8.2 Toxins -- 2.9 Carbohydrates and Antibiotics -- 91 2.10 Antibiotics and Resistance -- 2.11 Glycan Analysis Methods -- 104 2.12 Glyconanotechnology -- 2.13 Concluding Remarks -- 3 Oligosaccharides and Glycoconjugates in Recognition Processes / Thisbe K. Lindhorst -- 3.1 Introduction -- 3.2 The Lectins and Their Ligands -- 3.2.1 Classification of Lectins -- 3.2.2 Characteristics of Important Lectin Classes -- 3.2.2.1 The R- and L-type lectins -- 3.2.2.2 The P-type lectins -- 3.2.2.3 The C-type lectins -- 3.2.2.4 The collectins: A subgroup of C-typelectins -- 3.2.2.5 The selectins: A subgroup of C-type lectins -- 3.2.2.6 The I-type lectins -- 3.2.2.7 The S-type lectins --

3.3 Recognition of Carbohydrates -- 3.3.1 Formation of a Carbohydrate Lectin Complex -- 3.3.2 Networks of Stabilizing Interactions -- 3.3.3 Complexation via -- 3.3.4 Weak Interactions and the Role of Water -- 3.3.5 Hydrophobic Interactions with Carbohydrates -- 3.3.6 Binding to the Bacterial Lectin FimH -- 3.4 The Biological Role of Carbohydrate Lectin Interactions -- 3.4.1 Clearance of Glycoproteins by Interaction with ASGPR -- 3.4.2 Leukocyte Trafficking -- 3.4.3 Galectins in Signaling -- 3.4.4 Type 1 Fimbriae-Mediated Bacterial Adhesion -- 3.5 Multivalency of Carbohydrate Protein Interactions -- 3.6 Model Systems for the Investigation of Carbohydrate Protein Interactions -- 3.6.1 Multivalent Glycomimetics: Glycodendrimers and Successors -- 3.6.2 Self-Assembled Monolayers: Glyco-SAMs -- 3.6.3 Testing Bacterial Adhesion -- 3.6.4 Tailoring Carbohydrate Surfaces to Mimic Cellular Adhesion to the Glycocalyx -- 3.7 Conclusions and Outlook --

4 Glycoside Hydrolases / Motomitsu Kitaoka.

4.1 Introduction -- 4.2 Classification -- 4.2.1 Anomeric Configuration of the Substrate -- 4.2.2 Location of the Hydrolyzed Linkage -- 4.2.3 Anomeric Retention and Inversion -- 4.3 Mechanisms of Action -- 4.3.1 Retaining GHs -- 4.3.1.1 Typical retaining GHs -- 4.3.1.2 Substrate-assisted catalysis of retaining GHs -- 4.3.1.3 NAD+-dependent catalysis of retaining GHs -- 4.3.2 Inverting GHs -- 4.3.3 Hydrolysis and Transglycosylation -- 4.4 Chemoenzymatic Syntheses Using GHs with Engineered Substrates -- 4.5 Chemoenzymatic Syntheses Using Mutant GHs -- 4.6 Concluding Remarks -- 5 Disaccharide Phosphorylases: Mechanistic Diversity and Application in the Glycosciences / Christiane Luley-Goedl and Bernd Nidetzky -- 5.1 Introduction -- 5.2 Disaccharide Phosphorylases: Classification,Structure, and Function -- 5.3 Phosphorylase Mechanisms -- 5.3.1 Cellobiose and Chitobiose Phosphorylase -- 5.3.2 Sucrose Phosphorylase --

5.3.3 Retaining a,a-Trehalose Phosphorylase -- 5.4 Novel Application of Disaccharide Phosphorylases in Synthesis -- 5.4.1 Multi-Step Enzymatic Synthesis of Disaccharides and Other Glycosides -- 5.4.1.1 Coupling to sucrose conversion -- 5.4.1.2 Lacto-N-biose -- 5.4.1.3 Glucosylglycerol -- 5.4.2 Engineering of Cellobiose Phosphorylase for Altered Substrate Specificity -- 5.5 Conclusions -- 6 Dihydroxyacetone Phosphate-Dependent Aldolases: From Flask Reaction to Cell-Based Synthesis / Mohui Wei, Zijie Li, Baolin Wu, Yunpeng Liu, Tiehai Li,Liuqing Wen, Jing Li, Jiansong Cheng, Junqiang Fang,Xianwei Liu, and Peng George Wang -- 6.1 Introduction -- 6.2 Synthetic Applications -- 6.3 DHAP Generation -- 6.4 Overcoming DHAP Dependence -- 6.4.1 Substrate/Reaction Engineering -- 6.4.2 Discovery and Design of New Enzymes -- 6.4.3 Directed Evolution of Enzymes -- 6.5 Transforming DHAP-Dependent Aldolase-Mediated Reactions from Flask into Cell-Based Synthesis --

6.6 Conclusion -- 7 Enzymatic and Chemoenzymatic Synthesis of Nucleotide Sugars: Novel Enzymes, Novel Substrates, Novel Products, and Novel / Routes Leonie Engels and Lothar Elling -- 7.1 Introduction -- 7.2 Novel Enzymes -- 7.2.1 UDP-Nucleotidylyltransferases -- 7.2.2 dTDP-Nucleotidylyltransferases -- 7.2.3 Salvage Pathway Enzymes -- 7.2.4 Glycosyltransferases -- 7.3 Novel Substrates and Novel Products -- 7.3.1 Screening of Novel Substrates -- 7.3.2 Novel Substrates for Nucleotidylyltransferases -- 7.3.3 Novel Substrates for Salvage Pathway Enzymes -- 7.3.4 Nucleotide Furanose Sugars -- 7.3.5 Nucleotide Phosphono Sugars -- 7.3.6 Nucleotide Carba Sugars -- 7.4 Novel Routes -- 7.4.1 Combinatorial Biocatalysis for in situ (Re)Generation of Nucleotide Sugars -- 7.5 Conclusions -- 8 Iteratively Acting Glycosyl transferases / Songya Zhang and Andreas Bechthold -- 8.1 Introduction --

8.2 Iterative Acting GTs Involved in Polysaccharide Biosynthesis in Plants.

8.2.1 GTs Involved in Biosynthesis of Starch -- 8.2.2 GTs Involved in Hemicellulose Biosynthesis -- 8.2.3 GTs Involved in Cellulose Biosynthesis -- 8.3 Iteratively Acting GTs Involved in Natural Product Biosynthesis -- 8.3.1 GTs Involved in Natural Product Biosynthesis -- 8.3.2 GTs Involved in Biosynthesis of Aureolic Acid-Type Compounds -- 8.3.3 GTs Involved in Biosynthesis of Anthracyclines -- 8.3.4 GTs Involved in Biosynthesis of Angucyclines -- 8.3.5 GTs Involved in Biosynthesis of Macrocyclic Lactones -- 8.3.6 GTs Involved in Biosynthesis of Oligosaccharides -- 8.4 Concluding Remarks -- 9 Bacterial Glycosyltransferases Involved in Molecular Mimicry of Mammalian Glycans Warren Wakarchuk -- 9.1 Introduction -- 9.2 Sialyltransferases -- 9.2.1 GT-52 and GT-80 (GT-B Folds) -- 9.2.2 GT-42 (Modified GT-A Folds) -- 9.2.3 GT-38 and Other Polymerizing Glycosyltransferases -- 9.2.4 Microbial GAG Polymerases --

9.3 Galactosyltransferases and N-Acetylhexosamine Transferases -- 9.3.1 -1,3-Galactosyltransferases and -1,3/4-N- Acetylhexosamine Transferases of GT-2 and GT-82 375 9.3.2 -1,4-Galactosyltransferases of GT-2 and GT-25 -- 9.3.3 a-1,4-Galactosyltransferases of GT-8 -- 9.4 Fucosyltransferases of GT-10 and GT-11 -- 9.5 Concluding Remarks -- 10 Sulfotransferases and Sulfatases: Sulfate Modification of Carbohydrates -- Eli Chapman and Sarah R. Hanson -- 10.1 Introduction -- 10.2 Sulfotransferases and Sulfatases Modify the Sulfation State of Carbohydrates -- 10.3 Sulfotransferases -- 10.3.1 Carbohydrate-Modifying STs in Humans -- 10.3.1.1 Glycosaminoglycans -- 10.3.1.2 Mucins -- 10.3.1.3 Sulfolipids -- 10.3.1.4 HNK-1 carbohydrate -- 10.3.2 Carbohydrate-Modifying STs in Bacteria -- 10.3.3 Structure -- 10.3.4 Mechanism -- 10.4 Sulfatases -- 10.4.1 Carbohydrate-Modifying Sulfatases in Humans -- 10.4.1.1 Extracellular sulfatases --

10.4.1.2 Lysosomal sulfatases -- 10.4.1.3 Secretory sulfatases with unknown function -- 10.4.2 Carbohydrate Sulfatases in Bacteria -- 10.4.2.1 GAG-degrading sulfatases -- 10.4.2.2 Bacterial mucin sulfatases -- 10.4.3 Sulfatase Structure -- 10.4.4 Sulfatase Mechanism -- 10.5 Concluding Remarks -- 11 Glycosylation in Health and Disease / Peter Grunwald -- 11.1 Introduction -- 11.2 Glycosaminoglycan/Protein Interactions -- 11.2.1 Heparins: Anticoagulant and Antimetastatic Agents -- 11.2.2 Glycosaminoglycans and HIV -- 11.2.3 Neurodegenarative Diseases and GAGs.

11.3 Mucins and Cancer -- 11.4 Glycosphingolipids: General Aspects -- 11.4.1 Catabolism of GSLs and Storage Diseases -- 11.4.2 GSLs and Cancer -- 11.5 Inhibitors of Carbohydrate Modifying Enzymes and Chaperones -- 11.5.1 Sugar-Mimicking Inhibitors -- 11.5.2 Chaperon-Mediated Therapy (CMT) -- 11.6 Quality-Control Defects in the ER -- 11.7 Lipoteichoic Acids -- 11.8 GPI-Anchored Proteins -- 11.9 Recombinant Therapeutics -- 11.10 Concluding Remarks -- 12 Sialic Acid Derivatives, Analogs, and Mimetics as Biological Probes and Inhibitors of Sialic Acid Recognizing Proteins / Joe Tiralongo and Thomas Haselhorst -- 12.1 Introduction -- 12.2 Sialic Acid Biosynthesis in Mammals -- 12.3 Sialic Acid and Cancer -- 12.4 Sialyltransferase and CMP-CST Inhibitors Based on Donor Substrate Analogs and Transition State Mimetics -- 12.4.1 Sialyltransferase Inhibitors -- 12.4.2 CST Inhibitors -- 12.5 Glycomimetic Inhibitors of Selectin and Siglecs --

12.6 Exploring the Interaction of Substrate Derivatives, Analogs, and Mimetics with Sialic Acid Recognizing Proteins by STD NMR Spectroscopy -- 12.6.1 CMP-Sialic Acid Synthetase -- 12.6.2 CMP-Sialic Acid Transporter -- 12.6.3 Vibrio cholerae Sialidase -- 12.6.4 Rotavirus Haemagglutinin (VP8*) -- 12.7 Concluding Remarks -- 13 Enzymes of the Carbohydrate Metabolism and Catabolism for Chemoenzymatic Syntheses of Complex Oligosaccharides / Stephan B ttcher, Julian Thimm, and Joachim Thiem -- 13.1 Introduction -- 13.2 Glycosylation Employing Leloir and Non-Leloir Glycosyltransferases -- 13.2.1 Leloir Glycosyltransferases -- 13.2.1.1 b,1-4-galactosyltransferase -- 13.2.1.2 a,1-3/4-fucosyltransferase -- 13.2.1.3 a,2-3- and a,2-6-sialyltransferases -- 13.2.2 Non-Leloir Glycosyltransferases -- 13.2.2.1 Cyclodextrin-a,14-glucosyltransferase (CGT) -- 13.2.2.2 Potato phosphorylase -- 13.2.2.3 b,1-3-Galactosyl-N-acetylhexosamine Phosphorylase --

13.3 Glycosylation Employing Glycohydrolases and Glycosynthases -- 13.3.1 Exo-Glycosidases -- 13.3.1.1 b,1-3-Galactosidases -- 13.3.1.2,1-4-Galactosidases -- 13.3.1.3 a-Sialidases -- 13.3.2 Trans-Sialidase -- 13.3.3 Endo-Glycosidases -- 13.3.4 Glycosynthases -- 14 From Gene to Product: Tailor-Made Oligosaccharides and Polysaccharides by Enzyme and Substrate Engineering / Maria Elena Ortiz-Soto and J rgen Seibel -- 14.1 Introduction -- 14.2 Enzyme Engineering of Glucansucrases -- 14.3 Donor and Acceptor Substrate Engineering: A Chemo-Enzymatic Approach for the Synthesis of Designed Products -- 14.4 Enzyme Engineering of Fructansucrases -- 14.5 Sucrose Analogues as Donor Substrates -- 14.6 Outlook.

15 Synthesis and Modification of Carbohydrates via Metabolic Pathway Engineering in Microorganisms / Xian-wei Liu, Lei Li, Hai-tao Gao, Li-jun Dang, and Peng George Wang -- 15.1 Introduction 657 15.2 Oligosaccharide Synthesis by Metabolic Engineered Microorganisms -- 15.2.1 Coupled Metabolically Engineered Bacteria Technology -- 15.2.2 Superbug Technology with in situ Regeneration of UDP-Gal -- 15.2.3 Oligosaccharide Synthesis via Living Cell Factory -- 15.3 Polysaccharide Remodeling and Molecular Imaging via Metabolic Pathway Engineering -- 15.4 Glycodiversification of Small-Molecule Natural Products via Metabolic Pathway Engineering -- 15.5 Humanization of Protein N-Glycans via Metabolic Pathway Engineering in Yeast -- 15.6 Summary -- 16 Metabolic Pathway Engineering for Hyaluronic Acid Production -- Esteban Marcellin, Wendy Y. Chen, and Lars K. Nielsen -- 16.1 Introduction -- 16.2 HA Synthase -- 16.3 Streptococcal Hyaluronic Acid Production --

16.4 Streptococcal Strain Engineering -- 16.5 HA Production in Heterologous Hosts -- 16.6 Systems Biology and Future Perspect -- 17 Microbial Rhamnolipids / Marius Henkel, Markus M. M ller, Barbara H rmann, Christoph Syldatk, and Rudolf Hausmann -- 17.1 Introduction -- 17.2 Chemical Structure and Properties of Microbial Rhamnolipids -- 17.2.1 Rhamnolipid Structure -- 17.2.2 Surfactant Properties of Rhamnolipids -- 17.2.3 Physiological Role of Rhamnolipids -- 17.3 Rhamnolipid Production by Pseudomonas aeruginosa -- 17.3.1 Rhamnolipid Biosynthesis Pathway -- 17.3.2 Quorum Sensing Regulation of Rhamnolipid Biosynthesis -- 17.3.3 Characteristic Rhamnolipid Production Curves -- 17.3.3.1 Rhamnolipid production under growth-limiting conditions -- 17.3.3.2 Specific rhamnolipid production rate: interplay of growth and quorum sensing -- 17.3.3.3 Genetic regulation of rhamnolipid production under growth-limiting conditions --

17.3.4 Cultivation Strategies for Rhamnolipid Production -- 17.3.4.1 Batch and fed-batch strategies 711 17.3.4.2 Resting cells cultivations 711 -- 17.3.4.3 Semi-continuous cultivations -- 17.3.4.4 Continuous cultures -- 17.3.4.5 Type of carbon source -- 17.3.4.6 Influence of the growth-limiting component -- 17.3.4.7 Other factors influencing rhamnolipid production -- 17.3.4.8 Typical production media composition -- 17.3.5 Downstream Processing of Rhamnolipids -- 17.3.5.1 Production of rhamnolipid crude extracts -- 17.3.5.2 Further purification steps -- 17.3.5.3 In situ product removal -- 17.4 Rhamnolipid Production by Other Microorganisms -- 17.4.1 Recombinant Production of Rhamnolipids -- 17.5 Commercial Aspects of Rhamnolipids -- 17.5.1 Agriculture and Environment.

17.5.2 Cosmetics and Medicine -- 17.5.3 Food Technology -- 17.5.4 Cleaning Detergents -- 17.6 Needs and Future Trends in Rhamnolipid Production -- 17.6.1 Systems Biotechnology and Modeling Approaches for the Improvement of Rhamnolipid Production -- 17.6.2 Future Trends and Needs for Downstream Processing -- 17.6.3 Strain Improvement and Development -- 17.7 Outlook -- 18 Chitin-Converting Enzymes / Karin Mo, Susanne Zibek, Thomas Hirth, and Steffen Rupp -- 18.1 Introduction -- 18.2 Chitin -- 18.3 Organisms Acting on Chitin -- 18.4 Chitin-Modifying Enzymes -- 18.4.1 Classification by Catalyzed Reaction (NC-IUBMB) -- 18.4.2 Classification of Hydrolases by Amino Acid Sequence Homology -- 18.4.3 Distribution of Chitin Hydrolases within Different Domains -- 18.4.4 Three-Dimensional Structure of Hydrolases -- 18.4.5 Catalytic Mechanism and Involved Catalytic Sites of Chitin Hydrolases -- 18.4.6 General Characteristics of Chitinases --

18.4.7 Chitindeacetylases -- 18.5 Potential Applications of Chitinases and Chitin Conversion Products -- 18.5.1 Chitin Oligomers and N-Acetylglucosamine -- 18.5.2 Chitinases as Biopesticides -- 18.5.3 Chitosan -- 18.6 Conclusion -- 19 Linear and Cyclic Oligosaccharides / Hajime Taniguchi -- 19.1 Introduction -- 19.2 Linear Oligosaccharides -- 19.2.1 Trehalose (a-d-Glucopyranosyl-a-d- Glucopyranoside) -- 19.2.2 Palatinose (Isomaltulose) -- 19.2.3 Fructooligosaccharide -- 19.2.4 Lactosucrose -- 19.2.5 Galactooligosaccharides -- 19.2.6 Glycosylsucrose -- 19.3 Cyclic Oligosaccharides -- 19.3.1 Difructose Anhydrides (DFAIII) -- 19.3.2 Cyclic Nigerosylnigerose -- 19.3.3 Cyclic Maltosylmaltose -- 19.3.4 Isocyclomaltopentaose -- 19.3.5 Cyclic Pentasaccharide Containing 1-3, 1-4, and 1-6 Linkages -- 19.3.6 Cyclodextrin -- 19.3.7 Cycloamylose -- 19.3.8 Highly Branched Cyclic Dextrin --

19.3.9 Cycloisomaltooligosaccharide (CI, cyclodextran) -- 19.3.10 Cyclic b-Glucans -- 19.3.11 Cycloinulooligosaccharides -- 19.4 Conclusion -- 20 Fungal Degradation of Plant Oligo- and Polysaccharides / Ronald P. de Vries, Joost van den Brink, Kristiina S. Hild n, Miia R. M kel, and Henrik St lbrand -- 20.1 Introduction -- 20.2 Degradation of Cellulose and Xyloglucan -- 20.2.1 Endoglucanases -- 20.2.2 Exoglucanases/Cellobiohydrolases -- 20.2.3 b-Glucosidases -- 20.2.4 Lytic Polysaccharide Monooxygenases -- 20.2.5 Accessory Enzymes for Xyloglucan Degradation -- 20.2.6 Insights from Fungal Genomes -- 20.2.7 Industrial Applications of Cellulases -- 20.3 Degradation of Xylan -- 20.3.1 Endoxylanases -- 20.3.2 -Xylosidases -- 20.3.3 Accessory Enzymes for Xylan Degradation -- 20.3.4 Insights from Fungal Genomes.

20.3.5 Applications of Xylanases -- 20.4 Degradation of Galacto(gluco)Mannan -- 20.4.1 b-Mannanases and b-Mannosidases -- 20.4.2 Accessory Enzymes -- 20.4.3 Insights from Fungal Genomes -- 20.4.4 Industrial Applications of Enzymes Degrading Galacto(gluco)Mannan -- 20.5 Fungal Pectinolytic Enzymes -- 20.5.1 Hydrolases Acting on the Pectin Backbone -- 20.5.2 Lyases Actin on the Pectin Backbone -- 20.5.3 Acetyl and Methyl Esterases -- 20.5.4 Accessory Enzymes -- 20.5.5 Insights from Fungal Genomes -- 20.5.6 Pectinases as Virulence Factors -- 20.5.7 Applications of Pectinolytic Enzymes -- 20.6 Inulin and Sucrose Degradation -- 20.6.1 Enzymes Acting on Inulin and Sucrose -- 20.6.2 Conserved Domains of Inulinases -- 20.6.3 Production of Inulinases -- 20.6.4 Insights from Fungal Genomes -- 20.6.5 Application of Inulinases -- 20.7 Degradation and Modification of Lactose -- 20.8 Degradation of Plant Oligo- and Polysaccharides by Basidiomycetes -- 20.8.1 Cellulose and Xyloglucan Degrading Enzymes of Basidiomycetes -- 20.8.2 Xylan Degrading Enzymes of Basidiomycetes -- 20.8.3 Degradation of Galacto(gluco)Mannan by Basidiomycetes -- 20.8.4 Basidiomycete Pectinolytic Enzymes -- 20.8.5 Insights from Basidiomycete Genomes -- 20.9 Concluding Remarks and Prospects -- 21 Bacterial Strategies for Plant Cell Wall Degradation and Their Genomic Information / Yutaka Tamaru and Roy H. Doi -- 21.1 Introduction -- 21.2 The Components of Plant Cell Wall and their Bioconversion -- 21.3 Cellulolytic Bacteria and Fungi Isolated from Natural Biomass -- 21.4 The Full Circle: From Microbial Communities to Metagenomes -- 21.5 Searching for Lignocellulose Degrading Enzymes: The Impact of Different Omics -- 21.6 Enzyme Enzyme Synergy -- 21.7 Carbohydrate-Binding Module (CBM)-Mediated GH Enzymes -- 21.8 The Fibrobacteres-Model of Plant Cell Wall Hydrolysis.

21.9 Cellulosomal Complex Formation -- 21.10 The Clostridium Cellulovorans Cellulosome -- 21.11 Cellulosome-Producing Clostridial Genomes -- 21.12 Conclusion -- 22 Heterologous Expression of Cellulolytic Enzymes / Christian Eckert, Rainer Fischer, and Ulrich Commandeur -- 22.1 Introduction -- 22.2 Cellulose -- 22.3 Cellulolytic Enzymes: The Key to Cellulose Degradation 930 -- 22.3.1 Endoglucanases -- 22.3.2 Exoglucanases -- 22.3.3 Carbohydrate-Binding Domains -- 22.3.4 Linker -- 22.3.5 b-Glucosidases -- 22.3.6 Cellulosomes -- 22.3.7 Auxiliary Activity Enzymes -- 22.3.7.1 Cell wall loosening enzymes -- 22.3.7.2 Lytic polysaccharide monooxygenases -- 22.4 Sources for Cellulolytic Enzymes -- 22.4.1 Cellulases from Filamentous Fungi -- 22.4.2 Cellulases from Hyperthermophilic Bacteria and Archaea -- 22.4.3 Cellulases from Insects -- 22.5 Heterologous Expression of Cellulolytic Enzymes in Bacteria --

22.6 Heterologous Expression of Cellulolytic Enzymes in Yeasts -- 22.6.1 The Concept of Consolidated Bioprocessing -- 22.7 Heterologous Expression of Cellulolytic Enzymes in Plants -- 22.8 Conclusions and Outlook -- 23 Engineered Minicellulosomes for Consolidated Bioprocessing / Youyun Liang, Ee Lui Ang, and Huimin Zhao -- 23.1 Introduction -- 23.2 Brief Description of Naturally-Occurring Cellulosomes -- 23.3 Considerations in Design of Engineered Minicellulosomes -- 23.3.1 Cohesins and Dockerins Pairs -- 23.3.2 Cell Surface Anchorage -- 23.3.3 Substrate-Binding Domain -- 23.3.4 Catalytic Units -- 23.3.5 Configuration of Engineered Cellulosome -- 23.4 Engineered Cellulosomes in Different Host Organisms -- 23.4.1 Engineered Cellulosomes in Yeast -- 23.4.2 Engineered Cellulosomes in C. Acetobutylicum -- 23.4.3 Engineered Cellulosomes in B. Subtilis -- 23.4.4 Engineered Cellulosomes in Other Organisms -- 23.5 Concluding Remarks --

24 Design of Efficient Multienzymatic Reactions for Cellulosic Biomass Processing / Anne S. Meyer -- 24.1 Introduction -- 24.2 The Cellulosic Biomass Substrate -- 24.3 Goals, Options, and Tools for Enzymatic Biomass Decomposition -- 24.3.1 Goals of Enzymatic Biomass Degradation -- 24.3.2 T. reesei Cellulases and Options Available for Reducing Cellulase Production Costs -- 24.3.3 Options and Tools Available for Improving the Enzymatic Processing Step -- 24.4 The Minimal Enzyme Mixture Approach -- 24.5 Conclusions and Perspectives -- Index.

This book provides an actual overview of the structure, function, and application of carbohydrate-modifying biocatalysts. Carbohydrates have been disregarded for a long time by the scientific community, mainly due to their complex structure. Meanwhile, the situation changed with increasing knowledge about the key role carbohydrates play in biological processes such as recognition, signal transduction, immune responses, and others. An outcome of research activities in glycoscience is the development of several new pharmaceuticals against serious diseases such as malaria, cancer, and various storage diseases. Furthermore, the employment of carbohydrate-modifying biocatalysts enzymes as well as microorganisms will contribute significantly to the development of environmentally friendly processes boosting a shift of the chemical industry from petroleum- to bio-based production of chemicals from renewable resources. The updated content of the second edition of this book has been extended by discussing the current state of the art of using recombinantly expressed carbohydrate-modifying biocatalysts and the synthesis of minicellulosomes in connection with consolidated bioprocessing of lignocellulosic material. Furthermore, a synthetic biology approach for using DAHP-dependent aldolases to catalyze asymmetric aldol reactions is presented..

001638326

(OCoLC)964586563