Current developments in biotechnology and bioengineering. Production, isolation and purification of industrial products / edited by Ashok Pandey, Sangeeta Negi, Carlos Ricardo Soccol.

Format:

Book

Author/Creator:

Pandey, Ashok.

Contributor:

Pandey, Ashok, editor.

Negi, Sangeeta, editor.

Soccol, Carlos Ricardo, editor.

Language:

English

Subjects (All):

Biological products--Separation.

Biological products.

Biotechnology--Technique.

Biotechnology.

Separation (Technology).

Bioengineering.

Medical Subjects:

Biotechnology.

Bioengineering.

Physical Description:

1 online resource (888 pages) : illustrations (some color)

Place of Publication:

Amsterdam : Elsevier, [2017]

Summary:

Current Developments in Biotechnology and Bioengineering: Production, Isolation and Purification of Industrial Products provides extensive coverage of new developments, state-of-the-art technologies, and potential future trends, focusing on industrial biotechnology and bioengineering practices for the production of industrial products, such as enzymes, organic acids, biopolymers, and biosurfactants, and the processes for isolating and purifying them from a production medium. During the last few years, the tools of molecular biology and genetic and metabolic engineering have rendered tremendous improvements in the production of industrial products by fermentation. Structured by industrial product classifications, this book provides an overview of the current practice, status, and future potential for the production of these agents, along with reviews of the industrial scenario relating to their production.

Contents:

Front Cover

Current Developments in Biotechnology and Bioengineering

Current Developments in Biotechnology and Bioengineering: Production, Isolation and Purification of Industrial Products

Copyright

Contents

List of Contributors

About the Editors

Preface

1 - Industrial and Therapeutic Enzymes

1 - α-Amylases

1.1 Introduction

1.1.1 Starch

1.1.2 Amylases

1.1.3 Classification of Amylases

1.2 Sources of α-Amylase

1.2.1 Plant α-Amylases

1.2.2 Bacterial α-Amylases

1.2.3 Fungal α-Amylases

1.3 Production of α-Amylase

1.3.1 Production Methods

1.3.2 Factors Influencing the Production of α-Amylase

1.3.2.1 Incubation Temperature

1.3.2.2 pH

1.3.2.3 Carbon Sources

1.3.2.4 Nitrogen Sources

1.3.2.5 Metal Ions

1.3.2.6 Surfactants

1.3.2.7 Agitation

1.4 Assay of α-Amylases

1.5 α-Amylase Inhibitors

1.6 Strain Improvement

1.7 Purification and Characterization of α-Amylases

1.8 Applications of α-Amylase

1.8.1 Detergent Applications

1.8.2 Textile Desizing

1.8.3 Medicinal and Clinical Chemistry

1.8.4 Paper Industry

1.8.5 Starch Liquefaction and Saccharification

1.8.6 Bread and Baking Industry

1.8.7 Alcohol Production

1.9 Conclusion and Perspectives

References

2 - Amylolytic Enzymes: Glucoamylases

2.1 Introduction

2.2 Sources of Glucoamylase

2.2.1 Microbial Sources

2.2.1.1 Fungal Sources

2.2.1.2 Bacterial Sources

2.2.1.3 Yeast Sources

2.2.2 Other Sources

2.3 Glucoamylase Production

2.3.1 Selection of Fermentation Process

2.3.2 Composition of Substrate

2.3.3 Optimization of Physical Parameters

2.4 Purification and Characterization

2.4.1 Purification Techniques

2.4.2 Characterization

2.5 Enzyme Assay

2.6 Strain Improvement

2.7 Commercially Available Glucoamylases

2.8 Conclusion and Perspective.

References

3 - Pectinolytic Enzymes

3.1 Introduction

3.2 Pectic Substances

3.3 Pectinase Classification

3.4 Pectinase Assays

3.5 Pectinase Production Processes

3.5.1 Raw Materials for Pectinase Production

3.5.2 Submerged Fermentation

3.5.3 Solid-State Fermentation

3.5.4 Bioreactors for Pectinase Production

3.6 Downstream and Purification Methods

3.6.1 Pectinase Enzyme Recovery

3.6.2 Isolation and Concentration Methods

3.6.3 Pectinase Purification

3.7 Technoeconomic Analysis of Pectinase Production

3.8 Conclusions and Perspectives

4 - Cellulases

4.1 Introduction

4.2 Sources

4.3 The Cellulase System

4.3.1 Noncomplex System

4.3.2 Complex Cellulases/Cellulosomes

4.4 Regulation of Cellulase Expression

4.5 Research on Bioprocesses for Improved Cellulase Production

4.5.1 Solid-State Fermentation

4.5.2 Submerged Fermentation

4.6 Strain Improvement

4.6.1 Mutagenesis and Selection

4.6.2 Genome Shuffling

4.6.3 Recombinant DNA/Gene Cloning

4.7 Cellulase Global Market

4.8 Protocol for Assay of Filter Paper Activity

4.8.1 Glucose Standard

4.8.2 Enzyme Assay

4.9 Challenges for Enzymatic Biomass Conversion

4.10 Future Perspectives

4.11 Conclusion

5 - Industrial Enzymes: β-Glucosidases

5.1 Introduction

5.2 Classification of β-Glucosidases

5.3 Mechanism of Action

5.3.1 Hydrolysis

5.3.2 Reverse Hydrolysis or Transglycosylation

5.4 Sources of β-Glucosidases

5.5 Production of β-Glucosidases

5.6 Assay of β-Glucosidases

5.6.1 β-Glucosidase Assay Using pNPG as Substrate

5.6.2 β-Glucosidase Assay Using Cellobiose as Substrate

5.7 Strain Improvement

5.7.1 Mutation

5.7.2 Genetic Manipulation

5.8 Applications of β-Glucosidases

5.8.1 Applications Based on Hydrolysis.

5.8.2 Applications Based on Transglycosylation

5.8.3 Role of BGL in Biomass Conversion

5.9 Conclusions and Perspectives

6 - Industrial Enzymes: Xylanases

6.1 Introduction

6.2 Sources of Xylanases

6.3 Production of Xylanases

6.4 Purification and Characterization of Xylanases

6.4.1 Ion-Exchange Chromatography

6.4.2 Size-Exclusion Chromatography

6.4.3 Affinity Chromatography

6.5 Xylanase Assays

6.5.1 3,5-Dinitrosalicylic Acid Assay

6.5.2 Congo Red Assay

6.5.3 Remazol Brilliant Blue Plate Assay

6.5.4 Somogyi Nelson Method

6.5.5 Zymogram Analysis

6.5.6 Detection Using Monoclonal Antibodies

6.5.7 High-Performance Anion Exchange Coupled With Pulsed Amperometric Detection

6.6 Strain Improvement

6.7 Conclusions and Perspectives

7 - Proteolytic Enzymes

7.1 Introduction

7.2 Sources of Proteolytic Enzymes

7.2.1 Proteolytic Enzymes from Plants

7.2.2 Proteolytic Enzymes from Animals

7.2.3 Proteolytic Enzymes from Microbial Sources

7.3 Production of Proteolytic Enzymes

7.3.1 Solid-State Fermentation

7.3.2 Submerged Fermentation

7.3.3 Immobilized Cell Technology

7.4 Industrial Production Scenario

7.5 Purification and Characterization of Proteolytic Enzymes

7.6 Assay of Proteolytic Enzymes

7.7 Properties of Proteolytic Enzymes

7.7.1 Optimum pH and Temperature for Proteolytic Activity and Enzyme Stability

7.7.2 Effects of Inhibitors and Metal Ions on Proteolytic Activity

7.7.3 Substrate Specificity and Determination of Kinetic Parameters

7.7.4 Influence of Detergents and Surfactants on Proteolytic Activity

7.8 Strain Improvement

7.8.1 Classical Strain Improvement

7.8.2 Recombinant DNA Technology for Strain Improvement

7.8.3 Improvement of Proteolytic Enzymes by Site-Directed Mutagenesis.

7.8.4 Improvement of Proteolytic Enzymes by Directed Evolution

7.8.5 High-Throughput Screening for Improved Proteases

7.9 Conclusions and Perspectives

8 - Lipolytic Enzymes

8.1 Introduction

8.1.1 Lipase Structure: Active-Site Lid and Interfacial Activation

8.1.2 Catalytic Mechanism

8.2 Microbial Sources of Enzymes

8.3 Production of Enzyme

8.3.1 Optimization of Fermentation Conditions

8.3.1.1 Carbon Source

8.3.1.2 Nitrogen Source

8.3.1.3 Metal Ion Requirement

8.3.1.4 pH and Temperature

8.3.1.5 Aeration and Agitation

8.3.1.6 Response Surface Methodology for Production Optimization

8.3.2 Cloning and Overexpression

8.4 Purification and Characterization of Lipases

8.4.1 Hydrophobic-Interaction Chromatography

8.4.2 Ion-Exchange Chromatography

8.4.3 Aqueous Two-Phase Systems

8.4.4 Reversed Micellar Extraction

8.4.5 Immunopurification

8.4.6 Affinity Chromatography

8.5 Studies on Pseudomonas aeruginosa Lipase Genes

8.6 Assay of Enzyme Lipolytic Activity

8.7 Conclusions and Perspectives

9 - Laccases

9.1 Introduction

9.2 Possible Substrates for Laccases

9.2.1 Textile Dyes

9.2.2 Toxic and Recalcitrant Compounds (Pesticides, Herbicides)

9.2.3 Degradation of Potential Environmental Contaminants in Soil

9.3 Laccase Action Mechanism

9.4 The Ideal Physicochemical Conditions for Laccases

9.5 Sources of Laccases

9.5.1 Natural Sources

9.5.2 Microbial Sources

9.5.2.1 Fungi

9.5.2.2 Bacteria

9.6 Laccase Applications

9.6.1 Soil Bioremediation

9.6.2 Wastewater Treatment

9.6.3 Microbial Biopulping

9.6.4 Enzymatic Biopulping

9.6.5 Cellulosic Pulp Bleaching

9.7 Future Trends in Uses and Applications

9.8 Conclusions and Perspectives

10 - Peroxidases

10.1 Introduction

10.2 Lignin Structure.

10.3 Peroxidases

10.4 Lignin Peroxidase

10.4.1 Reaction Pathway of Peroxidases

10.4.2 Manganese Peroxidase Pathway

10.5 Sources of Peroxidases

10.5.1 Bacterial Peroxidases

10.5.2 Fungal Peroxidases

10.5.3 Plant Peroxidases

10.6 Enzymes as Biocatalysts

10.7 Peroxidase Applications

10.7.1 Decolorization of Dyes

10.7.2 Removal of Phenolic Contaminants

10.8 Trends and Future of Peroxidases

10.9 Conclusions and Perspectives

11 - Therapeutic Enzymes: l-Glutaminase

11.1 Introduction

11.2 Isozymes of Glutaminase

11.3 Glutaminase as a Therapeutic Agent

11.4 Glutaminase in the Food Industry

11.5 Sources of l-Glutaminases

11.5.1 Microbial Sources of Enzymes

11.5.2 Microbial Sources of l-Glutaminase

11.5.2.1 l-Glutaminase From Marine Microorganisms

11.6 Production of l-Glutaminase

11.6.1 Submerged Fermentation

11.6.2 Solid-State Fermentation

11.6.2.1 Inert Supports in Solid-State Fermentation

11.6.2.2 Immobilized Cells

11.6.3 Commercial Production

11.7 Enzyme Characteristics

11.7.1 Recovery and Purification

11.7.2 Properties

11.8 Glutaminase Assay

11.9 Strain Improvement

11.10 Conclusion and Perspectives

12 - Therapeutic Enzymes: l-Asparaginases

12.1 Introduction

12.2 Sources of Asparaginases

12.2.1 Plant Sources

12.2.2 Bacterial Sources

12.2.3 Fungal and Yeast Sources

12.2.4 Actinomycetes

12.3 Production of l-Asparaginase

12.3.1 Recombinant Production

12.3.2 Industrial Production and Global Market

12.4 Purification and Characterization of l-Asparaginases

12.5 Assays for l-Asparaginase

12.6 Strain Improvement

12.6.1 Chemical Modification

12.6.2 Recombinant DNA Technology

12.6.3 Protoplast Fusion

12.6.4 Some Prominent Examples of Strain Improvement

12.6.4.1 Escherichia coli.

12.6.4.2 Erwinia.

Notes:

Includes bibliographical references and index.

Description based on online resource; title from PDF title page (ebrary, viewed October 5, 2016).

ISBN:

9780444636737

0444636730