High Value Fermentation Products, Volume 1

Name: High Value Fermentation Products, Volume 1 | Human Health
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Human Health

Saurabh Saran Vikash Babu Asha Chaubey(Herausgeber*in)

Wiley (Verlag)

1. Auflage

Erschienen am 12. März 2019

480 Seiten

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Inhalt

Cover
Title Page
Copyright Page
Contents
Foreword
About the Editors
List of Contributors
Preface
Acknowledgement
1 Introduction, Scope and Significance of Fermentation Technology
1.1 Introduction
1.2 Background of Fermentation Technology
1.3 Market of Fermentation Products
1.4 Types of Fermentation
1.4.1 Solid State Fermentation (SSF)
1.4.2 Submerged Fermentation (SmF)
1.4.3 Solid State (SSF) vs. Submerged (SmF) Fermentation
1.5 Classification of Fermentation
1.6 Design and Parts of Fermentors
1.7 Types of Fermentor
1.7.1 Stirred Tank Fermentor
1.7.2 Airlift Fermentor
1.7.3 Bubble Column Fermentor
1.7.4 Fluidized Bed Fermentor
1.7.5 Packed Bed Fermentor
1.7.6 Photo Bioreactor
1.8 Industrial Applications of Fermentation Technology
1.9 Scope and Global Market of Fermentation Technology
1.10 Conclusions
References
2 Extraction of Bioactive Molecules through Fermentation and Enzymatic Assisted Technologies
2.1 Introduction
2.2 Definition of Bioactives Compounds
2.2.1 Polyphenols and Polypeptides
2.2.2 Importance and Applications of Bioactive Compounds
2.2.3 Bioactive Peptides
2.3 Traditional Processes for Obtaining Bioactive Compounds
2.3.1 Soxhlet Extraction
2.3.2 Liquid-Liquid and Solid-Liquid Extraction
2.3.3 Maceration Extraction
2.4 Fermentation and Enzymatic Technologies for Obtaining Bioactive Compounds
2.4.1 Soft Chemistry in Bioactive Compounds
2.4.2 Biotransformation of Bioactive Compounds
2.4.3 Enzymatic and Fermentation Technologies
2.4.3.1 Enzymatic Technology
2.4.3.2 Fermentation Technology
2.5 Use of Agroindustrial Waste in the Fermentation Process
2.5.1 Cereal Wastes
2.5.2 Fruit and Plant Waste
2.6 General Parameters in the Optimization of Fermentation Processes
2.6.1 Response Surface Methodology
2.6.2 First-Order Model
2.6.3 Second-Order Model
2.7 Final Comments
Acknowledgements
References
3 Antibiotics Against Gram Positive Bacteria
3.1 Introduction
3.2 Target of Antibiotics Against Gram Positive Bacteria
3.2.1 Cell Wall Synthesis Inhibition
3.2.1.1 Penicillin
3.2.1.2 Cephalosporins
3.2.1.3 Vancomycin
3.2.1.4 Teicoplanin
3.2.1.5 Oritavancin
3.2.2 Protein Synthesis Inhibition
3.2.2.1 Erythromycin
3.2.2.2 Clarithromycin
3.2.2.3 Tetracyclines
3.2.3 DNA Synthesis Inhibition
3.3 Antibiotics Production Processes
3.4 Conclusion
References
4 Antibiotic Against Gram-Negative Bacteria
4.1 Introduction
4.2 Gram-Negative Bacteria and Antibiotics
4.2.1 ß-Lactam Drugs
4.2.1.1 Cephalosporins
4.2.1.2 Penicillin
4.2.1.3 Carbapenems
4.2.1.4 Monobactam
4.2.2 Macrolide
4.2.3 Aminoglycosides
4.2.4 Fluoroquinolones
4.3 Production of Antibiotics
4.3.1 Strain Development
4.3.1.1 Mutagenesis
4.3.1.2 Protoplast Fusion
4.3.1.3 Recombinant DNA
4.3.2 Media Formulation and Optimization
4.3.3 Fermentation
4.3.4 Downstream Processing and Purification
4.3.5 Quality Control
4.4 Conclusion
References
5 Role of Antifungal Drugs in Combating Invasive Fungal Diseases
5.1 Introduction
5.2 Antifungal Agents
5.2.1 Azoles
5.2.2 Polyenes
5.2.3 Allylamine/Thiocarbonates
5.2.4 Other Antifungal Agents
5.3 Targets of Antifungal Agents
5.3.1 Cell Wall Biosynthesis Inhibitors
5.3.2 Sphingolipid Synthesis Inhibitors
5.3.3 Ergosterol Synthesis Inhibitors
5.3.4 Protein Synthesis Inhibitors
5.3.5 Novel Targets
5.4 Development of Resistance towards Antifungal Agents
5.4.1 Minimum Inhibitory Concentration
5.4.2 Antifungal-Drug-Resistance Mechanisms
5.5 Market and Drug Development
5.6 Conclusions
Acknowledgement
References
6 Current Update on Rapamycin Production and its Potential Clinical Implications
6.1 Introduction
6.2 Biosynthesis of Rapamycin
6.2.1 Microbial Strain
6.2.2 Optimization of Carbon, Nitrogen Sources and Salts
6.2.3 Strain Manipulation to Improve Rapamycin Production
6.2.3.1 Random Mutagenesis
6.2.3.2 Chemical Mutagenesis
6.2.3.3 Metabolic Engineering Combined with Genetic Engineering to Improve Rapamycin Production
6.2.3.4 Protoplasts Fusion
6.2.3.5 Optimization of Fermentation Methods
6.3 Organic Synthesis of Rapamycin
6.4 Extraction and Quantification of Rapamycin
6.5 Physiological Factors Affecting Rapamycin Biosynthesis
6.5.1 Effect of Media Components
6.5.2 Effect of pH on Rapamycin Production
6.5.3 Effect of Physical Gravity
6.5.4 Effect of Morphological Changes
6.5.5 Effect of Dissolved Oxygen (DO) and Carbon Dioxide (DCO2)
6.6 Production of Rapamycin Analogs
6.7 Mechanism of Action of Rapamycin
6.8 Use of Rapamycin in Medicine
6.8.1 Anti-Fungal Agent
6.8.2 Immunosuppression
6.8.3 Anti-Cancer Agent
6.8.4 Anti-Aging Agent
6.8.5 Role in HIV Treatment
6.8.6 Rheumatoid Arthritis
6.9 Side Effects of Long-Term Use of Rapamycin
6.10 Conclusions
Acknowledgements
References
7 Advances in Production of Therapeutic Monoclonal Antibodies
7.1 Introduction
7.2 Discovery and Clinical Development
7.3 Structure and Classification
7.4 Nomenclature of Monoclonal Antibodies
7.5 Production of Monoclonal Antibodies
7.5.1 Hybridoma Technology
7.5.2 Epstein-Barr Virus Technology
7.5.3 Phage Display Technology
7.5.4 Cell Line Based Production Techniques
7.5.4.1 Cell Lines
7.5.4.2 Production Media
7.5.4.3 Production Conditions
7.5.4.4 Production Strategies
7.5.4.5 Production Vessel
7.5.4.6 Microbial Production
7.5.4.7 Plant-Based Production
7.5.5 Chemical Modifications of Monoclonal Antibodies
7.5.6 Advances in Antibody Technology
7.5.6.1 Antibody-Drug Conjugates (ADCs)
7.5.6.2 Antibody Fusion Proteins
7.5.6.3 Payloads
7.6 Conclusions
References
8 Antimicrobial Peptides from Bacterial Origin: Potential Alternative to Conventional Antibiotics
8.1 Introduction
8.2 Classification of Bacteriocins
8.2.1 Bacteriocins from Gram-Negative Bacteria
8.2.2 Bacteriocins from Gram-Positive Bacteria
8.3 Mode of Action
8.3.1 Pore-Forming Bacteriocins
8.3.2 Non-Pore-Forming Bacteriocins: Intracellular Targets
8.4 Applications
8.4.1 Food Bio Preservative
8.4.2 Food Packaging (In Packaging Films)
8.4.3 Hurdle Technology to Enhance Food Safety
8.4.4 Therapeutic Potential
8.4.5 Effect of Bacteriocins on Biofilms
8.5 Conclusions
Acknowledgments
Abbreviations
References
9 Non-Ribosomal Peptide Synthetases: Nature's Indispensable Drug Factories
9.1 Introduction
9.1.1 Non-Ribosomal Peptides as Natural Products
9.1.2 Non-Ribosomal Peptides as Drugs
9.2 NRPS Machinery
9.3 Catalytic Domains of NRPSs
9.3.1 Adenylation (A) Domains
9.3.2 Thiolation (T) or PCP Domains
9.3.3 Condensation (C) Domains
9.3.4 Thioesterase (Te) Domains
9.4 Types of NRPS
9.4.1 Type A (Linear NRPS)
9.4.2 Type B (Iterative NRPS)
9.4.3 Type C (Non-linear NRPS)
9.5 Working of NRPSs
9.5.1 Priming Thiolation Domain of NRPS
9.5.2 Substrate Recognition and Activation
9.5.3 Peptide Bond Formation between NRP Monomers
9.5.4 Chain Termination of NRP Synthesis
9.5.5 NRP Tailoring
9.6 Sources of NRPs
9.7 Production of Non-Ribosomal Peptides
9.8 Future Scope
Acknowledgements
References
10 Enzymes as Therapeutic Agents in Human Disease Management
10.1 Introduction
10.2 Pancreatic Enzymes
10.2.1 Trypsin (EC 3.4.21.4)
10.2.2 Pancreatic Lipase (EC 3.1.1.3)
10.2.3 Amylases (EC 3.2.1.1)
10.3 Oncolytic Enzymes
10.3.1 L-Asparaginase (EC 3.5.1.1)
10.3.2 L-Glutaminase (EC 3.5.1.2)
10.3.3 Arginine Deiminase (ADI) (EC 3.5.3.6)
10.4 Antidiabetic Enzymes
10.4.1 Glucokinase (EC2.7.1.1)
10.5 Liver Enzymes
10.5.1 Superoxide Dismutase (SOD) (EC 1.15.1.1)
10.5.2 Alkaline Phosphatase (ALP) (EC 3.1.3.1)
10.6 Kidney Disorder
10.6.1 Uricase (EC 1.7.3.3)
10.6.2 Urease (EC 3.5.1.5)
10.7 DNAand RNA-Based Enzymes
10.7.1 Dornase
10.7.2 Adenosine Deaminase
10.7.3 Ribonuclease
10.8 Enzymes for the Treatment of Cardiovascular Disorders
10.8.1 The Hemostatic System
10.8.1.1 Primary Hemostasis
10.8.1.2 Secondary Hemostasis
10.8.1.3 Tertiary Hemostasis
10.8.2 Enzymes of the Hemostatic System
10.8.2.1 Clotting Enzymes
10.8.2.2 Thrombolytic Enzymes
10.9 Lysosomal Storage Disorders
10.9.1 a-Galactosidase A (EC 3.2.1.22)
10.9.2 Glucocerebrosidase (EC 3.2.1.45)
10.9.3 Acid Alpha-Glucosidase (GAA) (EC 3.2.1.20)
10.9.4 a-L-iduronidase (Laronidase) (EC 3.2.1.76)
10.10 Miscellaneous Enzymes
10.10.1 Phenylalanine Hydroxylase (EC 1.14.16.1)
10.10.2 Collagenase (EC 3.4.24.3)
10.10.3 Hyaluronidase
10.10.4 Bromelain
10.11 Conclusions
References
11 Erythritol: A Sugar Substitute
11.1 Introduction
11.1.1 Background of Erythritol
11.1.2 History of Erythritol
11.1.3 Occurrence of Erythritol
11.1.4 General Characteristics
11.2 Chemical and Physical Properties of Erythritol
11.3 Estimation of Erythritol
11.3.1 Thin Layer Chromatography (TLC)
11.3.2 Colorimetric Assay for Detection of Polyols
11.3.3 High-Performance Liquid Chromatography (HPLC)
11.3.4 Capillary Electrophoresis (CE)
11.4 Production Methods for Erythritol
11.4.1 Chemical Methods for Erythritol Production
11.4.2 Fermentative Methods for Erythritol Production
11.4.2.1 Erythritol Production in Bacteria
11.4.2.2 Erythritol Production in Yeasts
11.5 Optimization of Erythritol Production
11.5.1 One Factor at a Time
11.5.2 Statistical Design Approaches
11.6 Toxicology of Erythritol
11.7 Applications of Erythritol
11.7.1 Confectioneries
11.7.2 Bakery
11.7.3 Pharmaceuticals
11.7.4 Cosmetics
11.7.5 Beverages
11.8 Precautions for Erythritol Usage
11.9 Global Market for Erythritol
11.10 Conclusions
References
12 Sugar and Sugar Alcohols: Xylitol
12.1 Introduction
12.1.1 Lignocellulosic Biomass
12.1.2 Properties of Xylitol
12.1.3 Occurrence and Production of Xylitol
12.2 Biomass Conversion Process
12.2.1 Pretreatment Methodologies
12.2.1.1 Physical Pretreatment
12.2.1.2 Physico-Chemical and Chemical Pretreatment
12.2.1.3 Microbial Pretreatment
12.2.2 Enzymatic Hydrolysis
12.2.3 Detoxification Techniques
12.2.3.1 Chemical Methods
12.2.3.2 Physical Method
12.2.3.3 Biological Method
12.3 Utilization of Xylose
12.3.1 Microorganisms Utilizing Xylose
12.3.2 Metabolism of Xylose
12.3.2.1 Transport of Xylose
12.3.2.2 Metabolic Pathways
12.4 Process Variables
12.4.1 Temperature and pH
12.4.2 Substrate Concentration
12.4.3 Aeration
References
13 Trehalose: An Anonymity Turns Into Necessity
13.1 Introduction
13.2 Trehalose Metabolism Pathways
13.3 Physicochemical Properties and its Biological Significance
13.4 Trehalose Production
13.4.1 Enzymatic Conversion to Trehalose
13.4.2 Microbe Mediated Fermentation
13.4.2.1 Propionibacteria Mediated Conversion
13.4.2.2 Micrococcus Mediated Conversion
13.4.2.3 Brevibacterium Mediated Conversion
13.4.2.4 Fungal Strain Mediated Fermentation
13.4.2.5 Recombinant Strains in Trehalose Production
13.4.3 Purification and Detection of Trehalose in Fermentation Process
13.5 Application of Trehalose
13.5.1 Role of Trehalose in Food Industries
13.5.2 Role of Trehalose in Cosmetics and Pharmaceutics
13.6 Conclusions
References
14 Production of Yeast Derived Microsomal Human CYP450 Enzymes (Sacchrosomes) in High Yields, and Activities Superior to Commercially Available Microsomal Enzymes
14.1 Introduction
14.1.1 Cytochrome P450 (CYP) Enzymes in Humans
14.1.2 Human Cytochrome P450 Enzymes and their Role in Drug Metabolism
14.1.3 Requirement of Activating Proteins to Form Functional Human CYP Enzymes
14.1.4 Use of Yeast Biased Codons for the Syntheses of Human Cytochrome P450 Genes
14.1.5 Expression of Human CYP Genes in Baker's Yeast from an Episomal Plasmid
14.1.6 Expression of Human CYP Genes in Baker's Yeast from Integrative Plasmids
14.1.7 The ADH2 Promoter for Production of Human CYP Enzymes in Baker's Yeast
14.1.8 Growth of Yeast Cells Containing Integrated Copies of CYP Gene Expression Cassettes, Driven by the ADH2 Promoter, for Production of CYP Enzymes
14.2 Amounts of Microsomal CYP Enzyme Isolated from Yeast Strains Containing Chromosomally Integrated CYP Gene Expression Cassettes are far Higher than Strains Harbouring an Episomal Expression Plasmid Encoding a CYP Gene
14.2.1 Preparation of Microsomal CYP Enzymes
14.2.2 Measurement of the Amounts of Functional CYPs in Microsomes Isolated from Baker's Yeast
14.2.3 Production of Functional Human CYP1A2 Microsomal Enzyme from Baker's Yeast
14.2.4 Production of Functional Human CYP3A4 Microsomal Enzyme from Baker's Yeast
14.2.5 Production of Functional Human CYP2D6 Microsomal Enzyme from Baker's Yeast
14.2.6 Production of Functional Human CYP2C19 Microsomal Enzyme from Baker's Yeast
14.2.7 Production of Functional Human CYP2C9 Microsomal Enzyme from Baker's Yeast
14.2.8 Production of Functional Human CYP2E1 Microsomal Enzyme from Baker's Yeast
14.2.9 Comments on the Production of Human CYP Enzymes from Baker's Yeast
14.3 Comparison of CYP Enzyme Activity of Yeast-Derived Microsomes (Sacchrosomes) with Commercially Available Microsomes Isolate from Insect and Bacterial Cells
14.3.1 Fluorescence-based Assays for Determining CYP Enzyme Activities in Isolated Microsomes
14.3.2 Comparison of Enzyme Activity of CYP1A2 Sacchrosomes with Commercially Available CYP1A2 Microsomes Isolated from Insect and Bacterial Cells
14.3.3 Comparison of Enzyme Activity of CYP2C9 Sacchrosomes with Those of Commercially Available CYP2C9 Microsomes from Insect and Bacterial Cells
14.3.4 Comparison of Enzyme Activity of CYP2C19 Sacchrosomes with Those of Commercially Available CYP2C19 Microsomes from Insect and Bacterial Cells
14.3.5 Comparison of Enzyme Activity of CYP2D6 Sacchrosomes with Those of Commercially Available CYP2D6 Microsomes from Insect and Bacterial Cells
14.3.6 Comparison of Enzyme Activity of CYP3A4 Sacchrosomes with Those of Commercially Available CYP3A4 Microsomes from Insect and Bacterial Cells
14.3.7 Comparison of Enzyme Activity of CYP2E1 Sacchrosomes with One of the Commercial CYP2E1 Microsomes Available from Insect Cells
14.4 IC50 Values of Known CYP Inhibitors Using Sacchrosomes, Commercial Enzymes and HLMs
14.5 Stabilisation of Sacchrosomes through Freeze-drying
14.6 Conclusions
References
15 Artemisinin: A Potent Antimalarial Drug
15.1 Introduction
15.2 Biosynthesis of Artemisinin in Artemisia annua and Pathways Involved
15.3 Yield Enhancement Strategies in A.annua
15.4 Artemisinin Production Using Heterologous Hosts
15.4.1 Microbial Engineering
15.4.2 Plant Metabolic Engineering
15.5 Spread of Artemisinin Resistance
15.6 Challenges in Large-Scale Production
15.7 Future Prospects
References
16 Microbial Production of Flavonoids: Engineering Strategies for Improved Production
16.1 Introduction
16.2 Flavonoids
16.3 Flavonoid Chemistry and Classes
16.4 Health Benefits of Flavonoids
16.5 Flavonoid Biosynthesis in Microorganism
16.6 Engineering of Flavonoid Biosynthesis Pathway
16.7 Metabolic Engineering Strategies
16.8 Applications of Synthetic Biology in Flavonoid Production
16.9 Post-modification of Flavonoids
16.10 Purification of Flavonoids
16.11 Conclusion
Acknowledgements
References
17 Astaxanthin: Current Advances in Metabolic Engineering of the Carotenoid
17.1 Introduction
17.1.1 Structure of Astaxanthin
17.1.2 Natural vs. Synthetic Astaxanthin
17.1.3 Uses and Market of Astaxanthin
17.2 Pathway of Astaxanthin
17.2.1 Bacteria
17.2.2 Algae
17.2.3 Yeast
17.2.4 Plants
17.3 Challenges/Current State of the Art in Fermentation/ Commercial Production
17.4 Metabolic Engineering for Astaxanthin
17.4.1 Bacteria
17.4.2 Plants
17.4.3 Synechocystis
17.4.4 Algae
17.4.5 Yeast
17.5 Future Prospects
References
18 Exploitation of Fungal Endophytes as Bio-Factories for Production of Functional Metabolites through Metabolic Engineering
Emphasizing on Taxol Production
18.1 Introduction
18.2 Taxol: History and Clinical Impact
18.3 Endophytes
18.3.1 Biodiversity of Endophytes
18.3.2 Endophyte vs. Host Plant: the Relationship
18.4 The Plausibility of Horizontal Gene Transfer (HGT) Hypothesis
18.5 Endophytes as Biological Factories of Functional Metabolites
18.6 Taxol Producing Endophytic Fungi
18.7 Molecular Basis of Taxol Production by Plants (Taxol Biosynthetic Pathway)
18.8 Metabolic Engineering for Synthesis of Taxol: Next Generation Tool
18.8.1 Plant Cell Culture
18.8.2 Microbial Metabolic Engineering for Synthesis of Taxol and Its Precursors
18.8.3 Metabolic Engineering in Heterologous Plant for Synthesis of Taxol and Its Precursors
18.9 Future Perspectives
Acknowledgements
References
Index
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