Biotechnology of microbial enzymes : production, biocatalysis and industrial applications /

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Brahmachari, Goutam
Formato: Electrónico eBook
Idioma:Inglés
Publicado: London, UK : Academic Press : Elsevier, 2016.
Temas:
Microbial enzymes > Biotechnology.
Enzymes microbiennes > Biotechnologie.
SCIENCE > Chemistry > Industrial & Technical.
TECHNOLOGY & ENGINEERING > Chemical & Biochemical.
Microbial enzymes > Biotechnology
Acceso en línea:Texto completo
Tabla de Contenidos:
  • Front Cover
  • Biotechnology of Microbial Enzymes
  • Copyright Page
  • Dedication
  • Contents
  • List of Contributors
  • Preface
  • 1 Useful Microbial Enzymes-An Introduction
  • 1.1 The Enzymes: A Class of Useful Biochemicals
  • 1.2 Microbial Enzymes for Industry
  • 1.3 Improvement of Enzymes
  • 1.4 Discovery of New Enzymes
  • 1.5 Concluding Remarks
  • Acknowledgements
  • References
  • 2 Production, Purification, and Application of Microbial Enzymes
  • 2.1 Introduction
  • 2.2 Production of Microbial Enzymes
  • 2.2.1 Enzyme Production in Industries
  • 2.2.2 Industrial Enzyme Production Technology
  • 2.2.2.1 Submerged Fermentation
  • 2.2.2.2 Solid State Fermentation
  • 2.3 Strain Improvements
  • 2.3.1 Mutation
  • 2.3.2 Recombinant DNA (rDNA) Technology
  • 2.3.3 Protein Engineering
  • 2.4 Downstream Processing/Enzyme Purification
  • 2.5 Product Formulations
  • 2.6 Global Enzyme Market Scenarios
  • 2.7 Industrial Applications of Enzymes
  • 2.7.1 Food Industry
  • 2.7.1.1 Starch Industry
  • 2.7.1.2 Baking Industry
  • 2.7.1.3 Brewing Industry
  • 2.7.1.4 Fruit Juice Industry
  • 2.7.2 Textile Industry
  • 2.7.3 Detergent Industry
  • 2.7.4 Pulp and Paper Industry
  • 2.7.5 Animal Feed Industry
  • 2.7.6 Leather Industry
  • 2.7.7 Biofuel From Biomass
  • 2.7.8 Enzyme Applications in the Chemistry and Pharma Sectors
  • 2.7.8.1 Speciality Enzymes
  • 2.7.8.2 Enzymes in Personal Care Products
  • 2.7.8.3 Enzymes in DNA-Technology
  • 2.8 Concluding Remarks
  • References
  • 3 Solid State Fermentation for Production of Microbial Cellulases
  • 3.1 Introduction
  • 3.2 Solid State Fermentation (SSF)
  • 3.2.1 Comparative Aspects of Solid State and Submerged Fermentations
  • 3.2.2 Cellulase-Producing Microorganisms in SSF
  • 3.2.3 Extraction of Microbial Cellulase in SSF
  • 3.2.4 Measurement of Cellulase Activity in SSF
  • 3.2.4.1 Filter Paper Activity (FPase).
  • 3.2.4.2 Carboxymethyl Cellulase Activity (CMCase)
  • 3.2.4.3 Xylanase Activity
  • 3.2.4.4 �-Glucosidase Activity
  • 3.3 Lignocellulosic Residues/Wastes as Solid Substrates in SSF
  • 3.4 Pretreatment of Agricultural Residues
  • 3.4.1 Physical/Mechanical Pretreatments
  • 3.4.1.1 Mechanical Comminution
  • 3.4.1.2 Grinding/Milling/Chipping
  • 3.4.2 Physico-Chemical Pretreatments
  • 3.4.2.1 Steam Explosion (Autohydrolysis)
  • 3.4.3 Chemical Pretreatments
  • 3.4.4 Biological Pretreatment
  • 3.5 Environmental Factors Affecting Microbial Cellulase Production in SSF
  • 3.5.1 Water Activity/Moisture Content
  • 3.5.2 Temperature
  • 3.5.3 Mass Transfer Processes: Aeration and Nutrient Diffusion
  • 3.5.3.1 Gas Diffusion
  • 3.5.3.2 Nutrient Diffusion
  • 3.5.4 Substrate Particle Size
  • 3.5.5 Other Factors
  • 3.6 Strategies to Improve Production of Microbial Cellulase
  • 3.6.1 Metabolic Engineering and Strain Improvement
  • 3.6.2 Recombinant Strategy (Heterologous Cellulase Expression)
  • 3.6.2.1 Yeast Expression Systems
  • 3.6.2.2 Bacterial Expression Systems
  • 3.6.2.3 Plant Expression System
  • 3.6.3 Mixed-Culture (Coculture) Systems
  • 3.7 Fermenter (Bioreactor) Design for Cellulase Production in SSF
  • 3.7.1 Tray Type Bioreactor
  • 3.7.2 Rotary Drum Bioreactor
  • 3.7.3 Packed Bed Bioreactor
  • 3.7.4 Fluidized Bed Bioreactor
  • 3.8 Biomass Conversion and Application of Microbial Cellulases
  • 3.8.1 Textile Industry
  • 3.8.2 Laundry and Detergents
  • 3.8.3 Food and Animal Feed
  • 3.8.4 Pulp and Paper Industry
  • 3.8.5 Biofuels
  • 3.9 Concluding Remarks
  • Abbreviations
  • References
  • 4 Hyperthermophilic Subtilisin-Like Proteases From Thermococcus kodakarensis
  • 4.1 Introduction
  • 4.2 Two Subtilisin-Like Serine Proteases From Thermococcus kodakarensis KOD1
  • 4.3 Tk-Subtilisin
  • 4.3.1 Ca2+-Dependent Maturation of Tk-Subtilisin.
  • 4.3.2 Crystal Structures of Tk-Subtilisin
  • 4.3.3 Requirement of Ca2+-Binding Loop for Folding
  • 4.3.4 Ca2+ Ion Requirements for Hyperstability
  • 4.3.5 Role of Tkpro
  • 4.3.6 Role of the Insertion Sequences
  • 4.3.7 Cold-Adapted Maturation Through Tkpro Engineering
  • 4.3.8 Degradation of PrPSc by Tk-Subtilisin
  • 4.3.9 Tk-Subtilisin Pulse Proteolysis Experiments
  • 4.4 Tk-SP
  • 4.4.1 Maturation of Pro-Tk-SP
  • 4.4.2 Crystal Structure of Pro-S359A*
  • 4.4.3 Role of proN
  • 4.4.4 Role of the C-Domain
  • 4.4.5 PrPSc Degradation by Tk-SP
  • 4.5 Concluding Remarks
  • Acknowledgments
  • Abbreviations
  • References
  • 5 Enzymes from Basidiomycetes-Peculiar and Efficient Tools for Biotechnology
  • 5.1 Introduction
  • 5.2 Brown and White Rot Fungi
  • 5.3 Isolation and Laboratory Maintenance of Wood Rot Basidiomycetes
  • 5.4 Basidiomycetes as Producers of Enzymes Involved in Degradation of Lignocellulose Biomass
  • 5.4.1 Enzymes Involved in the Degradation of Cellulose and Hemicelluloses
  • 5.4.2 Enzymes Involved in Lignin Degradation
  • 5.5 Production of Ligninolytic Enzymes by Basidiomycetes: Screening and Production in Laboratory Scale
  • 5.6 General Characteristics of the Main Ligninolytic Enzymes with Potential Biotechnological Applications
  • 5.6.1 Laccases
  • 5.6.2 Peroxidases
  • 5.7 Industrial and Biotechnological Applications of Ligninolytic Enzymes from Basidiomycetes
  • 5.7.1 Application of Ligninolytic Enzymes in Delignification of Vegetal Biomass and Biological Detoxification for Biofuel P ...
  • 5.7.2 Application of Ligninolytic Enzymes in the Degradation of Xenobiotic Compounds
  • 5.7.3 Application of Ligninolytic Enzymes in the Degradation of Textile Dyes
  • 5.7.4 Application of Ligninolytic Enzymes in Pulp and Paper Industry
  • 5.8 Concluding Remarks
  • Acknowledgments
  • References.
  • 6 Microbial Production and Molecular Engineering of Industrial Enzymes: Challenges and Strategies
  • 6.1 Introduction
  • 6.2 Strategies for Achieving High-Level Expression of Industrial Enzymes in Microorganisms
  • 6.2.1 Strategies for High-Level Expression of Microbial Enzymes in E. coli
  • 6.2.1.1 High-Level Expression of Enzymes by Transcriptional Regulation in E. coli
  • 6.2.1.2 High-Level Expression of Enzymes by Translational Regulation in E. coli
  • 6.2.1.3 Enhancement of the Expression of Enzymes by Different Protein Formations in E. coli
  • 6.2.1.4 Improving Enzyme Production Yield by Fusion Proteins or Molecular Chaperones in E. coli
  • 6.2.1.5 High-Level Expression of Enzymes by Codon Optimization in E. coli
  • 6.2.1.6 Fermentation Optimization of Enzyme Production in E. coli
  • 6.2.2 High-Level Expression of Microbial Enzymes in Bacilli
  • 6.2.3 High-Level Expression of Microbial Enzymes in Lactic Acid Bacteria
  • 6.2.4 High-Level Expression of Microbial Enzymes in Yeasts
  • 6.2.4.1 High-Level Expression of Microbial Enzymes in P. pastoris
  • 6.2.4.2 High-Level Expression of Microbial Enzymes in S. cerevisiae
  • 6.2.4.3 High-Level Expression of Microbial Enzymes in Other Yeast Hosts
  • 6.2.5 High-Level Expression of Microbial Enzymes in Filamentous Fungi
  • 6.2.5.1 High-Level Expression of Microbial Enzymes in Aspergillus Species
  • 6.2.5.2 High-Level Expression of Microbial Enzymes in Trichoderma Species
  • 6.2.5.3 High-Level Expression of Microbial Enzymes in Other Filamentous Fungi Species
  • 6.3 Molecular Engineering Strategies
  • 6.3.1 Directed Evolution
  • 6.3.2 Site-Directed Mutagenesis
  • 6.3.3 Saturation Mutagenesis
  • 6.3.4 Truncation
  • 6.3.5 Fusion
  • 6.4 Concluding Remarks
  • References
  • 7 Metagenomics and the Search for Industrial Enzymes
  • 7.1 Introduction
  • 7.2 The Dilemma Between Known, Engineered, or Novel Enzymes.
  • 7.3 Metagenomics and Its Application to Enzyme Research
  • 7.4 Success Stories of Na�ive and Direct Sequencing Screens for New Enzymes
  • 7.5 Success Stories for Introducing Environmental Enzymes into the Market
  • 7.6 Enzyme Search: Limitations of Metagenomics and Solutions
  • 7.7 Concluding Remarks
  • Acknowledgments
  • References
  • 8 The Pocket Manual of Directed Evolution: Tips and Tricks
  • 8.1 Introduction
  • 8.2 Methods to Generate DNA Diversity
  • 8.2.1 Mutagenic Methods
  • 8.2.1.1 Random Mutagenesis
  • 8.2.1.2 Saturation Mutagenesis
  • 8.2.2 DNA Recombination Methods
  • 8.2.2.1 In Vitro Methods
  • 8.2.2.1.1 Homology-Dependent Recombination Methods
  • 8.2.2.1.2 Homology-Independent Recombination Methods
  • 8.2.2.2 In Vivo Methods
  • 8.3 Computational Tools
  • 8.4 Functional Expression Systems
  • 8.5 Mutant Library Exploration
  • 8.5.1 Genetic Selection Methods
  • 8.5.2 High-Throughput Screening (HTS) Assays
  • 8.5.3 Ultrahigh-Throughput Screening Assays
  • 8.6 Forthcoming Trends in Directed Evolution
  • 8.7 Concluding Remarks
  • Acknowledgments
  • Abbreviations
  • References
  • 9 Insights into the Structure and Molecular Mechanisms of �-Lactam Synthesizing Enzymes in Fungi
  • 9.1 Introduction
  • 9.1.1 Penicillin and Cephalosporin Biosynthesis: A Brief Overview
  • 9.1.2 Genes Involved in Penicillin Biosynthesis
  • 9.2 ACV Synthetase
  • 9.2.1 The ACV Assembly Line
  • 9.2.2 The Cleavage Function of the Integrated Thioesterase Domain
  • 9.2.3 The Quality Control (Proofreading) Role of the Thioesterase Domain
  • 9.2.4 ACV Analog Dipeptides and Tripeptides Synthesized by the ACVS in Vitro
  • 9.3 Isopenicillin N Synthase
  • 9.3.1 Binding and Lack of Cyclization of the LLL-ACV
  • 9.3.2 The Iron-Containing Active Center
  • 9.3.3 The Crystal Structure of IPNS
  • 9.3.4 Oxidase and Oxygenase Activities of IPNS.

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