Food Biotechnology, Second Edition

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ISBN: 9780824753290 | 0824753291
Cover: Hardcover
Copyright: 10/11/2005

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Revised and updated to reflect the latest research and advances available, Food Biotechnology, Second Edition demonstrates the effect that biotechnology has on food production and processing. It is an authoritative and exhaustive compilation that discusses the bioconversion of raw food materials to processed products, the improvement of food quality, the importance of food safety, the design of ingredients for functional foods, and the biochemical advances made in traditional fermentation. It also provides an international perspective on the discipline as a whole.The content of the book is divided into three sections for easy reference. The first section provides an overview of the basic principles and explains microbial applications. The next section explains plant tissue culture techniques, genetic engineering of plants and animals, functional food ingredients and their health benefits, probiotics, antibody production for oral vaccines, and topics on enzyme technologies. The final section discusses food safety issues and the various bio-processing and fermentation biotechnologies used throughout the world.Food Biotechnology, Second Edition is an indispensable guide for anyone who needs to understand the latest information on food production and processing from a biotechnology perspective.

SECTION 1 FOOD MICROBIOLOGY

(192)

Chapter 1.01 Food Microbiology

(16)

Robert E. Levin

1.1 Introduction

(1)

1.2 General Aspects

(1)

1.2.1 Applications of Microbiology to Foods

(1)

1.2.2 The Nature of Microorganisms

(1)

1.3 Fungi

(3)

1.3.1 Fungal Cell Walls

(1)

1.3.2 Yeasts

(1)

1.3.3 Molds

(2)

1.4 Microbial Taxonomy

(3)

1.4.1 General

(2)

1.4.2 Classification of Bacteria

(1)

1.4.3 Serotypes

(1)

1.4.4 Molecular Taxonomy

(1)

1.5 Metabolic Control for Enhanced Metabolite Production

(1)

1.6 Mutagenesis for Overproduction of Metabolites

(1)

1.7 Selective Cultivation

(2)

1.7.1 Selective Enrichment

(1)

1.7.2 Use of Incubation Temperature for Selective Isolation

(1)

1.7.3 The Use of Mineral Salts Media for the Isolation of Unique Carbon Sources Utilizing Microorganisms

(1)

1.7.4 Selective Isolation as a Result of Sequential Biochemical Activity

(1)

1.8 Electrostimulation of Metabolite Production

(1)

1.9 Aspects of Microbial Evolution

(1)

References

(3)

Chapter 1.02 Principles of Biochemistry and Molecular Biology

(14)

Patrick P. McCue and Kalidas Shetty

2.1 Preface

(1)

2.2 A Brief History of Classical Biochemistry

(2)

2.3 Experimental Techniques of Classical Biochemistry

(2)

2.3.1 Principles of Chromatography

(1)

2.3.1.1 Column Chromatography

(1)

2.3.1.2 Other Types of Chromatography

(1)

2.3.2 Principles of Spectrophotometry

(1)

2.4 A Brief History of Modern Biochemistry – Molecular Biology

(1)

2.5 Key Principles of Biochemistry and Molecular Biology

(4)

2.5.1 Basic Cellular Biology

(1)

2.5.2 Macromolecules and Basic Cellular Chemistry

(1)

2.5.3 Importance of Water, Ionization, and Buffers

(1)

2.5.4 Nucleic Acids

(1)

2.5.5 Proteins

(1)

2.6 Experimental Techniques of Modern Biochemistry and Molecular Biology

(2)

2.6.1 Detection of Proteins and Nucleic Acids

(1)

2.6.1.1 Principles of Electrophoresis

(1)

2.6.2 Southern, Western, and Northern Blotting

(1)

2.6.3 Mass Spectrometry

(1)

2.6.4 Other Important Molecular Techniques

(1)

2.6.4.1 The Polymerase Chain Reaction (PCR)

(1)

2.6.4.2 Real-Time PCR

(1)

2.6.4.3 Microarrays

(1)

References

(2)

Chapter 1.03 Fermentation Technology and Bioreactor Design

(54)

A. Eugene Raj and N. Ganesh Karanth

3.1 Historical Perspective

(1)

3.2 Fermentation in Food Biotechnology

(1)

3.3 Types of Fermentation

(1)

3.3.1 Submerged Fermentation

(1)

3.3.2 Solid-State Fermentation

(1)

3.4 Bioreactor Configurations

(8)

3.4.1 Submerged Fermentor Systems

(1)

3.4.1.1 Stirred Tank Bioreactor

(1)

3.4.1.2 Air Lift Bioreactor

(1)

3.4.1.3 Fluidized Bed Bioreactor

(1)

3.4.1.4 Microcarrier Bioreactor

(1)

3.4.1.5 Membrane Bioreactor

(1)

3.4.1.6 Photobioreactor

(1)

3.4.1.7 Innovative and Special Bioreactors

(2)

3.4.2 Solid-State Fermentor Systems

(1)

3.4.2.1 Laboratory Scale SSF Bioreactor

(1)

3.4.2.2 Industrial Scale SSF Bioreactor

(1)

3.5 Stages in a Fermentation Process

(14)

3.5.1 Upstream Processing

(1)

3.5.1.1 Fermentation Medium

(1)

3.5.1.2 Optimization of Fermentation Medium

(1)

3.5.1.3 Components of Industrial Fermentation Medium

(1)

3.5.1.4 Sterilization

(1)

3.5.1.5 Inoculation

(1)

3.5.2 Fermentation Process

(1)

3.5.2.1 Modes of Operation

(1)

3.5.2.2 Agitation

(1)

3.5.2.3 Aeration

(1)

3.5.2.4 Process Monitoring and Control

(3)

3.5.3 Downstream Processing

(1)

3.6 Fermentation Systems in Practice

(2)

3.6.1 Microbial Cultivation

(1)

3.6.2 Mammalian Cell Cultivation

(1)

3.6.3 Plant Cell Cultivation

(1)

3.7 Scale Up of Fermentation Processes

(1)

3.8 Asepsis in Fermentation Process

(2)

3.9 Bioreactor Design

(7)

3.9.1 Design Criteria

(1)

3.9.1.1 Mechanical Aspects

(1)

3.9.1.2 Process Aspects

(1)

3.9.2 Standard Dimensions

(1)

3.9.3 Jackets and Coils

(1)

3.9.4 Safety Codes

(1)

3.9.5 Material of Construction

(1)

3.9.6 Baffles

(1)

3.9.7 Sparger

(1)

3.9.8 Nozzles and Manways

(1)

3.9.9 Piping and Valves

(1)

3.9.10 Steam Locks

(1)

3.9.11 Welds and Joints

(1)

3.9.12 Surface Treatment and Finish

(1)

3.9.13 Cleanability

(1)

3.9.14 Sterility Aspects

(1)

3.10 Agitation System Design

(5)

3.10.1 Impeller Design

(1)

3.10.2 Drive Location

(1)

3.10.3 Seals

(3)

3.10.4 Power Requirement

(1)

3.11 Natural Bioreactors Using Transgenic Technology

(1)

3.11.1 Animal Bioreactors

(1)

3.11.2 Plant Bioreactors

(1)

3.11.3 Insect Cell Bioreactors

(1)

3.12 Conclusions and Future Perspective

(1)

References

(10)

Chapter 1.04 Process Developments in Solid-State Fermentation for Food Applications

(24)

Ashok Pandey and Sumitra Ramachandran

4.1 Introduction

(1)

4.2 Significance of SSF

(1)

4.3 SSF processes for Food Applications

(1)

4.3.1 Historical Developments

(1)

4.3.2 New Developments

(1)

4.4 SSF processes for Food Enzymes

(6)

4.4.1 Amylases

(2)

4.4.2 Lipases

(1)

4.4.3 Proteases

(1)

4.4.4 Pectinases

(1)

4.4.5 L-Glutaminase

(1)

4.4.6 Inulinase

(1)

4.4.7 Tannase

(1)

4.4.8 Recovery of Enzymes from Fermented Matter

(1)

4.5 SSF processes for Organic Acids

(1)

4.6 Production of Amino Acids

(1)

4.7 Mushroom Production

(1)

4.8 Production of Exopolysaccharides

(1)

4.9 Production of Pigments

(2)

4.10 Production of Aroma Compounds

101

(1)

4.11 Vitamins

101

(1)

4.12 Mycotoxins

102

(1)

References

102

(9)

Chapter 1.05 Metabolic Engineering of Bacteria for Food Ingredients

111

(20)

Ramon Gonzalez

5.1 Introduction

112

(1)

5.2 Amino Acids

113

(5)

5.2.1 Modification of Central Metabolic Pathways

113

(2)

5.2.2 Modification of Biosynthetic Pathways

115

(2)

5.2.3 Modification of Transport Systems

117

(1)

5.2.4 Use of Analytical Tools in the ME Toolbox

117

(1)

5.2.5 Use of LAB in the Production of Amino Acids

118

(1)

5.3 Multifunctional Organic Acids

118

(4)

5.3.1 Succinic Acid

118

(2)

5.3.2 Pyruvic Acid

120

(1)

5.3.3 Lactic Acid

121

(1)

5.3.4 Acetic Acid

121

(1)

5.4 Vitamins

122

(1)

5.4.1 Riboflavin (Vitamin B2)

123

(1)

5.4.2 Folate (Vitamin B11)

123

(1)

5.4.3 L-Ascorbic Acid (Vitamin C)

123

(1)

5.5 Carbohydrates

123

(1)

5.6 Bacteriocins

124

(1)

5.7 Low Calorie Sugars

125

(1)

5.8 Aroma Compounds

125

(1)

5.9 Future Trends and Potentials

126

(1)

References

127

(4)

Chapter 1.06 Technologies Used for Microbial Production of Food Ingredients

131

(12)

Anthony L. Pometto III and Ali Demirci

6.1 Introduction

131

(1)

6.2 Microorganism Selection and Development

132

(1)

6.3 Culture Media and Upstream Components

133

(2)

6.4 Bioreactor Monitoring Systems and Design

135

(3)

6.5 Fermentation Types Employed: The Actual Production Process

138

(1)

6.6 Novel Bioreactors Design

139

(1)

6.7 Future Research

140

(1)

References

141

(2)

Chapter 1.07 Production of Carotenoids by Gene Combination in Escherichia coli

143

(12)

Gerhard Sandmann

7.1 Carotenoids: Properties, Commercial Aspects, and Biological Function in Human Health

143

(2)

7.2 Escherichia coli as a Carotenoid Production System

145

(1)

7.3 Principles of Carotenoid Biosynthesis

146

(2)

7.4 Production of Carotenoids in Escherichia coli: Achievements and Perspectives

148

(4)

References

152

(3)

Chapter 1.08 Production of Amino Acids: Physiological and Genetic Approaches

155

(38)

Reinhard Krämer

8.1 Introduction

155

(3)

8.2 Physiological, Biochemical, and Genetic Background of Amino Acid Production

158

(6)

8.3 Physiological, Biochemical, and Genetic Tools used to Improve Amino Acid Production

164

(4)

8.4 Amino Acid Production: Technical Aspects

168

(1)

8.5 Selected Examples of Amino Acids

169

(10)

8.5.1 Glutamate

169

(5)

8.5.2 L-phenylalanine

174

(1)

8.5.3 L-tryptophan

175

(1)

8.5.4 L-lysine

175

(3)

8.5.5 Threonine

178

(1)

8.5.6 Other Amino Acids

179

(1)

8.6 Future Developments and Perspectives

179

(6)

References

185

(8)

Chapter 1.09 Biotechnology of Microbial Polysaccharides in Food

193

(118)

Ian W. Sutherland

9.1 Introduction

194

(1)

9.2 Natural Occurrence of Microbial Polysaccharides in Foods

194

(5)

9.2.1 Microbial Polysaccharides Present in Food as Products of Microbial Food Components

194

(4)

9.2.2 Physical Properties

198

(1)

9.2.3 Production and Synthesis

198

(1)

9.3 Microbial Polysaccharides Incorporated as Food Additives

199

(12)

9.3.1 Xanthan

199

(1)

9.3.1.1 Industrial Substrates

200

(1)

9.3.1.2 Biosynthesis of Xanthan

202

(1)

9.3.1.3 Physical Properties of Xanthan

204

(1)

9.3.1.4 Food Usage of Xanthan

205

(1)

9.3.1.5 Two Are Better Than One — Synergistic Gels Involving Xanthan

207

(1)

9.3.2 Gellan

207

(1)

9.3.2.1 Structure

208

(1)

9.3.2.2 Physical Properties

208

(1)

9.3.2.3 Food Applications

210

(1)

9.3.3 Curdlan

210

(1)

9.4 Exopolysaccharides as a Source of Flavor Components

211

(1)

9.5 Gazing Into the Crystal Ball: The Future for Microbial Polysaccharides in Food

212

(1)

9.6 Legislative Acceptability of Microbial Polysaccharides

213

(2)

References

215

(6)

Chapter 1.10 Genetics of Dairy Starter Cultures

221

(24)

Daniel J. O'Sullivan

10.1 Introduction

221

(1)

10.2 Taxonomy and Identification of Dairy Starter Cultures

222

(2)

10.3 Plasmid Biology of Dairy Starter Cultures

224

(6)

10.3.1 Role of Plasmids in L. Lactis

224

(2)

10.3.2 Role of Plasmids in Other Dairy Starter Cultures

226

(3)

10.3.3 Plasmid Replication in Dairy Cultures

229

(1)

10.4 Tools for Genetic Manipulation of Dairy Starter Cultures

230

(4)

10.4.1 Cloning Vectors

231

(1)

10.4.2 Expression Systems

231

(1)

10.4.3 Integrative Strategies

231

(3)

10.5 Genomics of Dairy Cultures

234

(1)

10.6 Conclusions

235

(1)

References

236

(9)

Chapter 1.11 Genetic Engineering of Baker's Yeast: Challenges and Outlook

245

(36)

Jose Antonio Prieto, Jaime Aguilera, and Francisca Randez-Gil

11.1 Introduction

246

(1)

11.2 Molecular Tools

247

(4)

11.2.1 Plasmids and Integrative Fragments

247

(1)

11.2.2 Dominant Selection Markers

248

(1)

11.2.3 Homologous Dominant Markers

249

(1)

11.2.4 Expression Level Promoters

250

(1)

11.3 Extension of Substrate Range

251

(10)

11.3.1 Melibiose

252

(2)

11.3.2 Lactose

254

(1)

11.3.3 Starch

255

(2)

11.3.4 Lignocellulose

257

(1)

11.3.4.1 Cellulose

257

(1)

11.3.4.2 Hemicellulose

258

(3)

11.4 Heterologous Enzyme Production

261

(2)

11.4.1 Amylases

261

(1)

11.4.2 Xylanases

261

(1)

11.4.3 Lipases

262

(1)

11.4.4 Phytases

262

(1)

11.4.5 Other Enzymes

263

(1)

11.5 Overproduction of Essential Nutrients

263

(4)

11.5.1 Amino Acids

263

(2)

11.5.2 Vitamins

265

(1)

11.5.3 Production of Novel Lipids

266

(1)

11.5.4 Prebiotics

266

(1)

11.6 Perspectives

267

(1)

References

268

(13)

Chapter 1.12 The Biotechnology of Wine Yeast

281

(30)

Linda F. Bisson

12.1 Introduction

282

(7)

12.1.1 The Winemaking Process

282

(2)

12.1.2 Genetic Characteristics of Saccharomyces

284

(1)

12.1.2.1 Laboratory, Native and Industrial Strains

285

(1)

12.1.2.2 Genomic Instability of Yeast Strains

287

(1)

12.1.3 Role of Indigenous Yeasts and Bacteria in Wine Production

287

(1)

12.1.4 Historical Aspects of Wine Yeast Biotechnology: Uses of Classical Breeding and Selection

288

(1)

12.2 Genetic Engineering Technology for Yeast

289

(6)

12.2.1 Molecular Genetic Tools

289

(1)

12.2.2 Selectable Markers

290

(3)

12.2.3 Strain Construction Strategies

293

(2)

12.3 Improvement of Oenological Traits of Yeast Strains

295

(6)

12.3.1 Fermentation Performance

297

(2)

12.3.2 Loss of Negative Characters

299

(1)

12.3.3 Enhanced Production of Positive Characters

299

(1)

12.3.4 Facilitation of Wine Processing and Enhancement of Wine Organoleptic Properties

300

(1)

12.4 Novel Traits

301

(2)

12.4.1 Flavor Production

302

(1)

12.4.2 Facilitation of the Production Process

302

(1)

12.4.3 Improved Healthfulness of Product

303

(1)

12.5 Future Perspective

303

(1)

References

304

(7)

Chapter 1.13 Stress Tolerance, Metabolism, and Development: The Many Flavors of Trehalose

311

(240)

Mike A. Singer, Tiago F. Outeiro, and Susan Lindquist

13.1 Introduction

311

(1)

13.2 Structure and Protective Mechanisms

312

(2)

13.3 Synthesis in S. cerevisiae

314

(1)

13.4 Degradation

315

(2)

13.5 Trehalose and Metabolism

317

(1)

13.6 Trehalose in Heat Shock

317

(2)

13.7 Trehalose in Plants and Drosophila

319

(2)

13.8 Applications in Biotechnology

321

(1)

13.9 Perspectives

321

(1)

References

322

(7)

Chapter 1.14 Production of Pectinases and Utilization in Food Processing

329

(20)

K.S. Venkatesh and S. Umesh-Kumar

14.1 Introduction

329

(1)

14.2 Production of Pectinases

330

(6)

14.2.1 Submerged Fermentation

333

(1)

14.2.2 Solid-State Fermentation

333

(3)

14.2.3 Strain Improvement

336

(1)

14.3 Genes of Pectin Degrading Enzymes

336

(1)

14.4 Pectinases of Aspergillus

337

(1)

14.5 Cloning and Expression of Pectinase Enzymes

338

(2)

14.6 Regulation of Pectinase Production in Aspergillus

340

(1)

14.7 Applications

340

(3)

14.8 Perspectives

343

(1)

References

344

(5)

Chapter 1.15 Biotechnology of Citric Acid Production

349

(58)

T Roukas

15.1 Introduction

350

(1)

15.2 Microorganisms Used for the Production of Citric Acid

351

(2)

15.2.1 Fungi

351

(1)

15.2.2 Yeasts

352

(1)

15.2.3 Bacteria

353

(1)

15.3 Biosynthesis of Citric Acid

353

(8)

15.4 Factors Affecting Citric Acid Production

361

(8)

15.4.1 Nutrients

361

(3)

15.4.2 Inhibitors and Stimulants

364

(2)

15.4.3 Inoculum

366

(1)

15.4.4 Fermentation Time

366

(1)

15.4.5 Temperature

366

(1)

15.4.6 pH

367

(1)

15.4.7 Aeration and Agitation

367

(2)

15.5 Morphology of Aspergillus niger and Rheological Properties of the Fermentation Broth During Citric Acid Production

369

(4)

15.6 Fermentation Processes for Citric Acid Production by Free and Immobilized Microbial Cells

373

(10)

15.6.1 Surface Fermentation

373

(1)

15.6.2 Submerged Fermentation

374

(1)

15.6.3 Comparison of Surface Fermentation and Submerged Fermentation

375

(1)

15.6.4 Continuous Culture

376

(1)

15.6.5 Fed Batch Culture

376

(1)

15.6.6 Solid-State Fermentation

377

(1)

15.6.7 Immobilized Cells

378

(5)

15.7 Substrates Used for the Productionof Citric Acid

383

(5)

15.7.1 Chemically Defined Media

383

(1)

15.7.2 Molasses

383

(1)

15.7.3 Cereal Constituents

384

(1)

15.7.4 Fruit Extracts

385

(1)

15.7.5 Hydrocarbons

386

(1)

15.7.6 Agricultural Wastes

387

(1)

15.8 Genetic Engineering of Microorganisms Used for the Production of Citric Acid

388

(4)

15.9 Recovery of Citric Acid

392

(2)

15.10 Conclusions

394

(1)

References

395

(12)

Chapter 1.16 Microbial Biotechnology of Food Flavor Production

407

(36)

G. Feron and Y. Waché

16.1 Introduction

408

(1)

16.2 Market of Flavor: Cost and Legacy Consideraton

408

(1)

16.3 Traditional Fermentations and de Novo Synthesis of Flavor

409

(8)

16.3.1 Metabolism

409

(1)

16.3.1.1 Carbon Metabolism

409

(1)

16.3.1.2 Lipid Metabolism

410

(1)

16.3.1.3 Amino Acid Metabolism

412

(1)

16.3.1.4 Cometabolism

414

(1)

16.3.1.5 Conclusion

414

(1)

16.3.2 De Novo Synthesis of Flavors

415

(2)

16.4 Bioconversion

417

(16)

16.4.1 Vanillin

418

(4)

16.4.2 Raspberry Ketone or Frambinone

422

(1)

16.4.3 Other Phenolic Compounds

422

(1)

16.4.3.1 Benzaldehyde

422

(1)

16.4.3.2 2-phenylethanol

424

(1)

16.4.4 Lactones and Methyl Ketones

424

(1)

16.4.5 Green Notes

425

(1)

16.4.6 Prospects

425

(1)

16.4.6.1 Genetic Engineering

426

(1)

16.4.6.2 Biocatalyst Environment

432

(1)

16.5 General Conclusion

433

(1)

References

434

(9)

Chapter 1.17 Microbial Production of Oils and Fats

443

(30)

James P. Wynn and Colin Ratledge

17.1 Introduction

443

(6)

17.1.1 The Concept of Single Cell Oils

443

(2)

17.1.2 Oleaginous Microorganisms and Lipid Accumulation

445

(4)

17.2 General Principles, Economics and Processes for SCO Production

449

(3)

17.3 SCO Production Processes

452

(12)

17.3.1 Process for the Production of a Cocoa Butter Equivalent Fat

452

(1)

17.3.2 Polyunsaturated Fatty Acids (PUFAs)

453

(1)

17.3.2.1 Dietetic Significance of Long Chain Polyunsaturated Fatty Acids

454

(1)

17.3.2.2 Processes for the Production of Various PUFAs

457

(7)

17.4 Safety of Single Cell Oils

464

(4)

17.5 Commercial Significance of SCOs

468

(1)

References

469

(4)

Chapter 1.18 Potential Uses of Cyanobacterial Polysaccharides in the Food Industry

473

(18)

Xue-Jun Liu and Feng Chen

18.1 Introduction

473

(2)

18.2 The Algae Cyanobacteria

475

(1)

18.3 Possible Roles of Cyanobactreial Polysaccharides

476

(2)

18.4 Correlation Between Chemical Composition and Physical Properties of Cyanobacterial Polysaccharides

478

(3)

18.5 Factors Influencing Production of Cyanobacterial Polysaccharides

481

(3)

18.6 Perspectives for Commercialization of Cyanobacterial Polysaccharides in the Food Industry

484

(2)

18.7 Summary

486

(1)

Acknowledgment

487

(1)

References

487

(4)

Chapter 1.19 Food Applications of Algae

491

(34)

G.A. Ravishankar, R. Sarada, B. Sandesh Kamath, and K.K. Namitha

19.1 Historical Perspectives

492

(1)

19.2 Nutritional Value of Micro- and Macroalgae

493

(5)

19.2.1 Proteins

494

(1)

19.2.2 Minerals

494

(2)

19.2.3 Vitamins

496

(1)

19.2.4 Lipids

496

(2)

19.3 Algae as a Source of Nutraceuticals

498

(3)

19.3.1 Carotenoids

498

(1)

19.3.2 Fatty Acids

499

(1)

19.3.3 Phycobilins

500

(1)

19.3.4 Bioactive Compounds

500

(1)

19.4 Industrial Production Processes

501

(7)

19.4.1 Chlorella

501

(1)

19.4.1.1 Nutritive Value

501

(1)

19.4.1.2 Beneficial Effects

502

(1)

19.4.2 Spirulina

502

(1)

19.4.2.1 Nutritive Value

502

(1)

19.4.2.2 Beneficial Effects

502

(1)

19.4.3 Dunaliella

503

(1)

19.4.4 Haematococcus

504

(1)

19.4.4.1 Astaxanthin as a Nutraceutical

504

(1)

19.4.4.2 Astaxanthin as Antioxidant

504

(1)

19.4.4.3 Astaxanthin for Health

505

(1)

19.4.4.4 Astaxanthin for Salmon and Trout Feeds

505

(1)

19.4.5 Porphyra

506

(1)

19.4.5.1 Nutritive Value

506

(1)

19.4.5.2 Cultivation Methods

507

(1)

19.4.5.3 Food Uses

507

(1)

19.4.6 Enteromorpha

507

(1)

19.4.6.1 Nutritive Value

507

(1)

19.4.6.2 Cultivation Methods

507

(1)

19.4.6.3 Food Uses

507

(1)

19.4.7 Eucheuma

508

(1)

19.5 Algae Based Industrial Products of Food Processing

508

(6)

19.5.1 Agar

508

(1)

19.5.1.1 Cultivation Methods

508

(1)

19.5.1.2 Extraction of Agar

509

(1)

19.5.1.3 Food Applications

509

(1)

19.5.2 Alginate

509

(1)

19.5.2.1 Cultivation Methods

509

(1)

19.5.2.2 Extraction of Alginate

510

(1)

19.5.2.3 Food Applications

510

(1)

19.5.2.4 Other Uses

512

(1)

19.5.3 Carrageenan

512

(1)

19.5.3.1 Cultivation Methods

512

(1)

19.5.3.2 Extraction of Carrageenan

512

(1)

19.5.3.3 Food Applications

513

(1)

19.6 Summary and Future Prospects

514

(1)

References

515

(10)

Chapter 1.20 Butanol Production from Agricultural Biomass

525

(26)

Nasib Qureshi and Hans P Blaschek

20.1 Introduction

526

(2)

20.2 Substrates

528

(3)

20.2.1 Corn/Degermed Corn

528

(1)

20.2.2 Molasses

529

(1)

20.2.3 Whey Permeate

529

(1)

20.2.4 Other Butanol Fermentation Substrates

529

(1)

20.2.4.1 Soy Molasses

530

(1)

20.2.4.2 Agricultural Wastes

530

(1)

20.2.4.3 Jerusalem Artichokes

531

(1)

20.2.4.4 Potatoes

531

(1)

20.3 Upstream Processing of Substrates

531

(1)

20.4 Microbial Cultures

532

(1)

20.5 Genetics of Clostridium Beijerinckii

533

(2)

20.6 Sugar Transport

535

(1)

20.7 Fermentation

535

(3)

20.7.1 Batch Process

535

(1)

20.7.2 Fed-Batch Fermentation

536

(1)

20.7.3 Continuous Fermentation

537

(1)

20.8 Immobilized Cell Bioreactors

538

(1)

20.9 Recovery

538

(3)

20.9.1 Distillation

538

(1)

20.9.2 Gas Stripping

539

(1)

20.9.3 Pervaporation

539

(1)

20.9.4 Liquid–Liquid Extraction

540

(1)

20.9.5 Other Recovery Techniques

541

(1)

20.10 Butanol Fermentation Limitations

541

(10)

SECTION 2 PLANT AND ANIMAL FOOD APPLICATIONS AND FUNCTIONAL FOODS

551

(706)

Chapter 2.01 Methods in Plant Tissue Culture

553

(50)

Hector G. Nunez-Palenius, Daniel J. Cantliffe, Harry H. Klee, Nejtali Ochoa-Alejo, Rafael Ramirez-Malagon, and Eugenio Perez-Molphe

1.1 Introduction

554

(1)

1.2 History

554

(1)

1.3 Laboratory Operations

555

(10)

1.3.1 Laboratory Facilities

555

(1)

1.3.2 Sterile Techniques

556

(3)

1.3.3 Media Composition, Preparation, and Handling

559

(5)

1.3.4 Explant Selection and Culture Conditions

564

(1)

1.4 Differentiation and Morphogenesis

565

(3)

1.4.1 Organogenesis (Direct and Indirect)

565

(1)

1.4.2 Somatic Embryogenesis (Direct and Indirect)

565

(2)

1.4.3 Somaclonal Variation

567

(1)

1.5 Plant Cell, Tissue, and Organ Cultures

568

(15)

1.5.1 Initiation and Maintenance of Callus

568

(1)

1.5.2 Initiation and Maintenance of Suspension Cultures

569

(3)

1.5.3 Bioreactors, Immobilized Plant Cells, and Secondary Metabolites

572

(1)

1.5.4 Root Cultures

573

(1)

1.5.5 Shoot Cultures

574

(1)

1.5.5.1 Apex Culture

575

(1)

1.5.5.2 Axillary Bud Culture

575

(1)

1.5.5.3 Meristem

575

(1)

1.5.5.4 Acclimatization

578

(1)

1.5.5.5 Current Approaches for Mass Clonal Propagation

578

(1)

1.5.6 Isolation and Culture of Protoplasts

579

(1)

1.5.7 Anther, Pollen, and Ovule Cultures

579

(1)

1.5.7.1 Physiology of Donor Plants

580

(1)

1.5.7.2 Physical Factors of Culture

580

(1)

1.5.7.3 Developmental Stage of Pollen

580

(1)

1.5.7.4 Genotype

580

(1)

1.5.7.5 Culture Media

581

(1)

1.5.7.6 Microspore Culture

581

(1)

1.5.7.7 Ovule Culture

581

(1)

1.5.8 Germplasm Storage

582

(1)

1.6 Genetic Manipulation

583

(6)

1.6.1 Somatic Hybridization

585

(1)

1.6.2 Direct Transformation

586

(1)

1.6.2.1 Gene Transfer to Protoplast

586

(1)

1.6.2.2 Gene Transfer Using Biolistics

586

(1)

1.6.2.3 Other Direct Transformation Systems

587

(1)

1.6.3 Agrobacterium-Mediated Transformation

587

(1)

1.6.3.1 Agrobacterium tumefaciens

587

(1)

1.6.3.2 Agrobacterium rhizogenes

588

(1)

1.7 Concluding Remarks

589

(1)

References

590

(13)

Chapter 2.02 Clonal Screening and Sprout Based Bioprocessing of Phenolic Phytochemicals for Functional Foods

603

(24)

Kalidas Shetty, Fergus M. Clydesdale, and Dhiraj A. Vattem

2.1 Phenolic Phytochemical Ingredients and Benefits

603

(1)

2.2 Biological Function of Phenolic Phytochemicals

604

(2)

2.3 Phytochemicals and Functional Food

606

(5)

2.4 Relevance of Phenolic Antioxidants for Functional Food and Comparative Metabolic Biology Considerations

611

(2)

2.5 Clonal Screening of Phenolic Synthesis in Herb Shoot Culture Systems

613

(3)

2.6 Phenolic Synthesis in Seed Sprouts

616

(1)

2.7 Summary of Strategies and Implications

617

(1)

References

618

(9)

Chapter 2.03 Genomic Basics for Food Improvement

627

(22)

Gabriela Olmedo, Socorro Parra, and Plinio Guzmán

3.1 Introduction

627

(1)

3.2 Whole Genome Sequencing of Plant Genomes

628

(3)

3.3 Large Scale EST Sequencing Projects in Crop Species

631

(3)

3.4 Genome Wide Analysis of Gene Expression Using DNA Microarrays

634

(6)

3.5 Proteomics: Systematic and High Throughput Characterization of Gene Products

640

(1)

3.6 Impact of Genomics on Nutrition

641

(3)

References

644

(5)

Chapter 2.04 Molecular Design of Soybean Proteins for Enhanced Food Quality

649

(26)

Nobuyuki Maruyama, Evelyn Mae Tecson-Mendoza, Yukie Maruyama, Motoyasu Adachi, and Shigeru Utsumi

4.1 Introduction

650

(1)

4.2 Soybean Proteins

651

(1)

4.2.1 β-Conglycinin

651

(1)

4.2.2 Glycinin

651

(1)

4.3 Three Dimensional Structures of Soybean Proteins

652

(6)

4.3.1 Crystallization

652

(1)

4.3.2 X-ray Crystallography

653

(1)

4.3.2.1 β-Conglycinin

653

(1)

4.3.2.2 Glycinin

655

(2)

4.3.3 Cupin Superfamily

657

(1)

4.4 Structural Features of Soybean Proteins

658

(2)

4.4.1 f3-Conglycinin

658

(1)

4.4.2 Glycinin

659

(1)

4.5 Improvement of Nutritional Quality by Protein Engineering

660

(2)

4.5.1 Increasing Sulfur Containing Amino Acids

660

(1)

4.5.2 Increasing Digestibility

661

(1)

4.6 Improvement in Physicochemical Functions by Protein Engineering

662

(4)

4.6.1 Structure to Physicochemical Function Relationships of Soybean Proteins

662

(1)

4.6.2 Improvement in the Physicochemical Functions of Glycinin

663

(3)

4.7 Improvement and Addition of Physiological Properties of Soybean Proteins

666

(4)

4.7.1 Fortifying the Bile Acid Binding Ability

666

(1)

4.7.2 Addition of Phagocytosis Stimulating Activity

667

(2)

4.7.3 Antimitotic Activity of Lunasin

669

(1)

4.8 Future Trends

670

(1)

References

670

(5)

Chapter 2.05 Genetic Modification of Plant Starches for Food Applications

675

(34)

Jeffrey D. Klucinec and Peter L. Keeling

5.1 Introduction

676

(1)

5.2 Structure

676

(4)

5.3 Synthesis

680

(3)

5.3.1 Granule Bound Starch Synthase

681

(1)

5.3.2 Soluble Starch Synthase

682

(1)

5.3.3 Branching Enzyme

682

(1)

5.3.4 Debranching Enzyme

682

(1)

5.4 Modifications

683

(5)

5.4.1 Modification of GBSSI Activity

684

(1)

5.4.2 Modification of SS Activity

685

(1)

5.4.3 Modification of SBE Activity

686

(1)

5.4.4 Modification of DeBE Activity

687

(1)

5.4.5 Modification of Multiple Pathway Enzymes

687

(1)

5.5 Functionality

688

(4)

5.5.1 Amylopectin Retrogradation

689

(1)

5.5.2 Amylose Gelation

690

(1)

5.5.3 Gelation of Mixtures of Amylose and Amylopectin

691

(1)

5.6 Applications

692

(5)

5.6.1 Amylose Free Starch

692

(1)

5.6.2 Low Amylose Starch

693

(1)

5.6.3 High Amylose Starch

694

(1)

5.6.4 Amylopectin Chain Length

695

(1)

5.6.5 Novel Starches

696

(1)

Acknowledgments

697

(1)

References

697

(12)

Chapter 2.06 Bioprocessing of Starch Using Enzyme Technology

709

(14)

K. Ravi-Kumar and S. Umesh-Kumar

6.1 Introduction

709

(1)

6.2 Enzymes Involved in Starch Degradation

710

(4)

6.2.1 α-Amylase (1,4-α-D-glucan Glucanohydrolase EC 3.2.1.1)

710

(2)

6.2.2 Glucoamylase or Amyloglucosidase (1,4-α-D-glucan Glucanohydrolase EC 3.2.1.3)

712

(2)

6.2.3 β-Amylase (1,4-α-D-glucan Maltohydrolase, EC 3.2.1.2)

714

(1)

6.2.4 Isoamylase (Glycogen 6-glucanohydrolase, EC 3.2.1.68)

714

(1)

6.2.5 Pullulanase (α-dextrin 6-glucanohydrolase EC 3.2.1.4)

714

(1)

6.2.6 α-Glucosidase, (α-D-glucoside Glucohydrolase EC 3.2.1.20)

714

(1)

6.2.7 Glucose Isomerase or Xylose Isomerase (EC 5.3.1.5)

714

(1)

6.3 Starch Processing

714

(4)

6.3.1 Production of Sweeteners and Confectionaries

715

(2)

6.3.2 In situ Starch Modifications for Food and Beverage Preparations

717

(1)

6.4 Current Status

718

(2)

References

720

(3)

Chapter 2.07 Genetic Modification of Plant Oils for Food Uses

723

(12)

Anthony J. Kinney

7.1 Introduction

723

(1)

7.2 Frying Oils

724

(1)

7.3 Oils for Baking and Confectionary Applications

725

(2)

7.4 Fatty Acids for Food Ingredients

727

(3)

References

730

(5)

Chapter 2.08 Molecular Biotechnology for Nutraceutical Enrichment of Food Crops: The Case of Minerals and Vitamins

735

(36)

Octavio Paredes-López and Juan Alberto Osuna-Castro

8.1 Micronutrients: Alleviating Nutritional Disorders by Nutraceuticals

735

(11)

8.2 Micronutrient Bioavailability and Approaches to Reduce Micronutrient Malnutrition

746

(4)

8.3 Minerals

750

(5)

8.3.1 Iron

750

(4)

8.3.2 Zinc

754

(1)

8.3.3 Calcium

754

(1)

8.3.4 Phytic Acid

754

(1)

8.4 Vitamins and Nutraceuticals

755

(11)

8.4.1 Carotenoids as Food Pigment and Provitamin A

755

(1)

8.4.1.1 Carotenogenesis in Tomato

758

(1)

8.4.1.2 Carotenogenesis in Other Food Crops

760

(2)

8.4.2 Vitamin E

762

(1)

8.4.3 Vitamin C

763

(3)

Acknowledgments

766

(1)

References

766

(5)

Chapter 2.09 Potential Health Benefits of Soybean Isoflavonoids and Related Phenolic Antioxidants

771

(18)

Patrick P. McCue and Kalidas Shetty

9.1 Introduction

772

(1)

9.2 Consumption of Soybean and Reduced Incidence of Disease

772

(5)

9.2.1 Soybean Isoflavonoids

772

(1)

9.2.2 Major Bioactivities of Soybean Isoflavonoids

773

(1)

9.2.2.1 Phytoestrogenic and Postmenopausal Activity

773

(1)

9.2.2.2 Cancer Chemoprevention

773

(1)

9.2.2.3 Prevention of Cardiovascular Disease

774

(1)

9.2.3 Approaches Toward Isoflavone Enrichment of Soybean

774

(1)

9.2.3.1 Genetic Modulation of Soybean

774

(1)

9.2.3.2 Enrichment of Soybean Isoflavone Content via Nongenetic Approaches

775

(1)

9.2.4 Toward a Model Mechanism for Action of Soybean Isoflavonoids and Related Phenolic Antioxidants against Cancer

775

(1)

9.2.4.1 Metabolism of Dietary Isoflavonoids

775

(1)

9.2.4.2 Control of Energy Metabolism and Oxidative Stress in a Healthy Cell

776

(1)

9.2.4.3 Control of Energy Metabolism and Oxidative Stress in a Tumorigenic Cell

776

(1)

9.2.5 Stress Response and the Proline Linked Pentose—Phosphate Pathway

776

(1)

9.3 A Hypothetical Model for the Cancer Chemopreventive Action of the Soybean Isoflavone Genistein

777

(2)

9.4 Summary and Implications

779

(1)

References

780

(9)

Chapter 2.10 Functional Phytochemicals from Cranberries: Their Mechanism of Action and Strategies to Improve Functionality

789

(36)

Dhiraj A. Vattem and K. Shetty

10.1 Introduction: Phenolic Phytochemicals

790

(1)

10.2 Chemical Nature and Biosynthesis of Phenolic Phytochemicals

790

(19)

10.2.1 Phenolic Phytochemicals from Berries

791

(1)

10.2.1.1 Cranberry

794

(1)

10.2.1.2 Cranberry Pomace

794

(1)

10.2.2 Oxidative Stress Mediated Pathogenesis

795

(1)

10.2.2.1 Antioxidant Defense Systems

797

(1)

10.2.2.2 Phenolic Phytochemicals in Nutritional Managementof Antioxidant Defense

799

(1)

10.2.3 Biological Function of Phenolic Phytochemicals

800

(1)

10.2.3.1 Biological Functionality of Cranberry Phenolics

801

(1)

10.2.3.2 Ellagic Acid

803

(1)

10.2.3.3 Alternate Model for the Function of Ellagic Acid and Related Phenolic Phytochemicals from Cranberries

804

(1)

10.2.3.4 A Model for Antimicrobial Activity of Ellagic Acid and Related Phenolics Against Bacterial Pathogens

807

(2)

10.3 Innovative Strategies to Enrich Fruits with Phenolic Antioxidants

809

(1)

10.4 Solid-State Bioprocessing

810

(1)

10.5 Cranberry Synergies with Functional Phytochemicals and Other Fruit Extracts

811

(1)

10.6 Conclusions

812

(1)

References

813

(12)

Chapter 2.11 Rosmarinic Acid Biosynthesis and Mechanism of Action

825

(22)

Kalidas Shetty

11.1 Introduction

825

(1)

11.2 Rosmarinic Acid Sources and Functional Pharmacological Effects

826

(2)

11.3 RA Biosynthesis in Cell Cultures

828

(4)

11.3.1 Pathways Associated with Rosmarinic Acid Biosynthesis

828

(2)

11.3.2 RA Biosynthesis and Generation of High RA Clonal Lines

830

(1)

11.3.3 Role of Proline Linked Pentose—Phosphate Pathway in RA Biosynthesis in Clonal Systems

830

(2)

11.4 Mechanism of RA Action Through Stimulation of Host Antioxidant Response

832

(6)

11.5 Summary

838

(1)

References

839

(8)

Chapter 2.12 Bioprocessing Strategies to Enhance L-DOPA and Phenolic Antioxidants in the Fava Bean (Vicia faba)

847

(20)

Kalidas Shetty, Reena Randhir, and Preethi Shetty

12.1 Introduction and Role of Phenolic Secondary Metabolites

847

(2)

12.2 Plant Phenolics in Human Health and as Antioxidants

849

(2)

12.3 Biosynthesis of Phenolic Metabolites and L-DOPA

851

(2)

12.4 L-DOPA and Parkinsonian Syndrome

853

(3)

12.4.1 L-DOPA from Natural Sources

855

(1)

12.4.2 L-DOPA from Fava bean

855

(1)

12.5 Linking L-DOPA Synthesis to the Pentose Phosphate and Phenylpropanoid Pathways

856

(2)

12.6 Recent Progress on Elicitation Linked Bioprocessing to Enhance L-DOPA and Phenolics in Fava Bean Sprouts

858

(2)

12.7 Recent Progress on Solid-State Bioprocessing of the Fava Bean to Enhance L-DOPA and Phenolics Using Food Grade Fungal Systems

860

(1)

12.8 Implications and Summary

860

(1)

References

861

(6)

Chapter 2.13 Phytochemicals and Breast Cancer Chemoprevention

867

(32)

Sallie Smith-Schneider, Louis A. Roberts, and Kalidas Shetty

13.1 Introduction

868

(4)

13.1.1 Background

868

(1)

13.1.2 Susceptibility and Chemoprevention: Molecular Pathways

869

(3)

13.2 Molecular Pathways of Breast Cancer Chemoprevention

872

(11)

13.2.1 p53

872

(1)

13.2.2 Estrogen Signaling

873

(1)

13.2.2.1 Background

873

(1)

13.2.2.2 Estrogen Regulation

873

(1)

13.2.2.3 Protection and Susceptibility Duality of Estrogen Signaling

874

(1)

13.2.2.4 Estrogenic Phytochemicals

874

(1)

13.2.3 CYP1A1 and Aryl Hydrocarbon Receptor (AhR)

875

(1)

13.2.4 Growth Factor Signaling

876

(1)

13.2.4.1 Background

876

(1)

13.2.4.2 Epidermal Growth Factor (EGF)

876

(1)

13.2.4.3 Insulin-Like Growth Factor (IGF)

877

(1)

13.2.4.4 Transforming Growth Factor Beta (TGF-f3)

878

(1)

13.2.4.5 Vascular Endothelial Growth Factor (VEGF)

880

(1)

13.2.5 Arachidonic Acid Metabolism

880

(1)

13.2.5.1 Background

880

(1)

13.2.5.2 Cyclooxygenase (COX)

880

(1)

13.2.5.3 Lipoxygenase (LO)

882

(1)

13.3 Strategies for Phytochemical Enrichment for Chemoprevention

883

(3)

13.3.1 Consistency of Phytochemicals

883

(1)

13.3.2 Clonal Screening of Phytochemicals from a Heterogeneous Genetic Background

884

(1)

13.3.3 Stress and Elicitor Induced Sprouting

884

(1)

13.3.4 Solid-State Bioprocessing

885

(1)

13.3.5 Liquid Fermentation

886

(1)

References

886

(13)

Chapter 2.14 Biotechnology in Wine Industry

899

(16)

Moustapha Oke, Gopinadhan Paliyath, and K. Helen Fisher

14.1 Introduction

899

(1)

14.2 Grape Cultivars and Wine Types

900

(4)

14.2.1 Vitis vinifera Cultivars

901

(1)

14.2.1.1 White Cultivars

901

(1)

14.2.1.2 Red Cultivars

902

(1)

14.2.2 French—American Hybrids

903

(1)

14.2.3 American Hybrids

904

(1)

14.3 Genetic Engineering of Wine Grapes

904

(3)

14.3.1 Clonal Selection

905

(1)

14.3.2 Somaclonal Selection

906

(1)

14.3.3 Biotechnology in Viticulture

906

(1)

14.4 Genetic Engineering of Yeast for Fermentation

907

(3)

14.4.1 Ideal Yeast

908

(1)

14.4.2 Yeast Breeding and Wine Quality

909

(1)

14.4.3 Wine as a Functional Food

910

(1)

14.5 Conclusions

910

(1)

References

910

(5)

Chapter 2.15 Biotechnology of Nonnutritive Sweeteners

915

(18)

Reena Randhir and Kalidas Shetty

15.1 Introduction

915

(2)

15.2 Saccharin

917

(1)

15.3 Acesulfame-K

917

(1)

15.4 Sucralose

918

(1)

15.5 Aspartame

919

(2)

15.6 Neotame

921

(1)

15.7 Stevioside

921

(2)

15.8 Monellin

923

(1)

15.9 Brazzein

924

(1)

15.10 Thaumatin

924

(3)

15.11 Mabinlin

927

(1)

15.12 Conclusion

927

(1)

References

928

(5)

Chapter 2.16 Biotechnological Approaches to Improve Nutritional Quality and Shelf Life of Fruits and Vegetables

933

(36)

Reena Grittle Pinhero and Gopinadhan Paliyath

16.1 Introduction

934

(1)

16.2 Potatoes

934

(17)

16.2.1 Factors Affecting Accumulation of Reducing Sugars in Potatoes

935

(1)

16.2.2 Low Temperature Sweetening in Potatoes

935

(1)

16.2.3 Metabolism of Starch in Tuber

936

(1)

16.2.3.1 Starch Synthesis

937

(1)

16.2.3.2 Starch Degradation

938

(2)

16.2.4 Starch—Sugar Balance

940

(1)

16.2.5 Sucrose Metabolism

941

(1)

16.2.5.1 Sucrose Degradation

943

(1)

16.2.6 Glycolysis

944

(2)

16.2.7 Oxidative Pentose Phosphate Pathway (PPP)

946

(1)

16.2.8 Mitochondrial Respiration

946

(1)

16.2.9 Compartmentation and Stress Induced Membrane Changes

947

(1)

16.2.9.1 Lipid Composition

947

(1)

16.2.9.2 Membrane Permeability

948

(2)

16.2.10 Free radicals and Antioxidant Enzymes

950

(1)

16.3 Tomato

951

(7)

16.3.1 Role of Membrane in Shelf life

951

(1)

16.3.2 Phospholipase D Gene Family

952

(1)

16.3.2.1 Role of PLD in Senescence and Chilling

952

(1)

16.3.2.2 Regulation of PLD Activity

953

(1)

16.3.2.3 Antisense Suppression of PLD Activity

953

(1)

16.3.3 Lipoxygenase

954

(1)

16.3.3.1 Role of Lipoxygenase in Membrane Deterioration

954

(1)

16.3.3.2 Tomato fruit Ripening and Lipoxygenases

956

(1)

16.3.3.3 Regulation of LOX by Genetic Manipulation

956

(1)

16.3.4 Cell Wall Metabolism and Fruit Softening

957

(1)

16.4 Conclusion

958

(1)

References

958

(11)

Chapter 2.17 Genetic Modification of Peanut as a Solution to Peanut Allergy

969

(20)

Hortense Dodo, Koffi Konan, and Olga Viquez

17.1 Prevalence and Impact of Allergic Diseases

970

(4)

17.1.1 Peanut is One of the Most Potent Sources of Food Allergy

970

(1)

17.1.1.1 The Symptoms

970

(1)

17.1.1.2 Accidental Ingestion of Peanut Is Increasing

970

(1)

17.1.1.3 Nutritional Impact of Peanut

971

(1)

17.1.1.4 Economic Impact of Peanut Allergy

971

(1)

17.1.1.5 Peanut Allergy is a Liability to the Peanut and Food Industry

972

(1)

17.1.2 Attempted Solutions to Peanut Allergy

972

(1)

17.1.2.1 Thermal Processing

972

(1)

17.1.2.2 Immunotherapy

972

(1)

17.1.2.3 Anti-IgE Vaccine

972

(1)

17.1.2.4 DNA Vaccine

973

(1)

17.1.3 Search for a Naturally Occurring Hypoallergenic or Allergen Free Peanut Variety

973

(1)

17.2 Strategy to Develop a Genetically Modified Hypoallergenic Peanut

974

(10)

17.2.1 The Gene Silencing Principles

974

(1)

17.2.1.1 Posttranscriptional Gene Silencing (PTGS) Strategies to Produce a Hypoallergenic Peanut

974

(1)

17.2.1.2 Mechanism of PTGS

975

(1)

17.2.1.3 PTGS for Crop Improvement

976

(1)

17.2.2 Application of the Gene Silencing Principles to Peanut

976

(1)

17.2.2.1 Step 1: Identification and Isolation of Peanut Allergens Genes

976

(1)

17.2.2.2 Step 2: Construction of Peanut Ara h 2 Inverted Repeat Vectors

980

(1)

17.2.2.3 Step 3: Induction of Peanut Somatic Embryos

980

(1)

17.2.2.4 Step 4: Transformation and Regeneration of Transgenic Peanut

980

(1)

17.2.3 Molecular Analyses

981

(1)

17.2.3.1 PCR Analysis

981

(1)

17.2.3.2 Southern Hybridization

981

(1)

17.2.3.3 Northern Analysis

981

(1)

17.2.2.4 Accumulation of Endogenous Ara h 2 Transcripts

981

(2)

17.2.4 Current and Future Prospects: Production of Fertile Transgenic Peanut with Ara h Introns Hairpin RNA (ArahihpRNA) Constructs

983

(1)

References

984

(5)

Chapter 2.18 Recombinant Lipoxygenases and Oxylipin Metabolism in Relation to Food Quality

989

(32)

Rod Casey and Richard K. Hughes

18.1 Introduction

989

(4)

18.1.1 LOX Isoforms and Heterogeneity

991

(1)

18.1.2 The Value of Recombinant LOX

992

(1)

18.2 The Structure of LOXs

993

(2)

18.3 LOX Reaction Mechanism

995

(4)

18.4 Substrate Specificity

999

(1)

18.5 Product (Regio- and Stereo-) Specificity

999

(2)

18.6 Cooxidation

1001

(1)

18.7 Applications of LOX to Food Quality

1002

(7)

18.7.1 Flavors and Aromas

1002

(3)

18.7.2 Cooxidation and Food Quality

1005

(1)

18.7.2.1 Destruction of Vitamins

1005

(1)

18.7.2.2 Pigment Bleaching

1006

(1)

18.7.2.3 Bread-Making and Dough Rheology

1006

(3)

18.8 Future Trends and Applications of Recombinant Lipoxygenases and Oxylipin Metabolism

1009

(1)

18.9 Lipoxygenases, Oxylipin Metabolism, Plant Defense, and Food Quality

1010

(1)

18.10 Conclusions

1011

(1)

References

1011

(10)

Chapter 2.19 Genetic Modification of Production Traits in Farm Animals

1021

(18)

Vernon G. Pursel

19.1 Introduction

1022

(1)

19.2 Increasing Growth Rate and Feed Efficiency

1022

(4)

19.2.1 GH and GRF Transgenics

1023

(1)

19.2.2 IGF-I Transgenics

1024

(2)

19.3 Modification of Milk Composition

1026

(3)

19.3.1 Caseins

1027

(1)

19.3.2 Reduction in Butterfat

1027

(1)

19.3.3 Lactose

1027

(1)

19.3.4 Human Milk Proteins

1028

(1)

19.4 Improved Wool Production

1029

(1)

19.4.1 Synthesis of Cysteine

1029

(1)

19.4.2 Wool Keratin Proteins

1030

(1)

19.4.3 IGF-I for Wool Follicle Growth

1030

(1)

19.5 Enhanced Animal Health

1030

(3)

19.5.1 Naturally Occurring Disease Resistance

1031

(1)

19.5.2 Preformed Antibodies

1031

(1)

19.5.3 Intracellular Immunization

1032

(1)

19.5.4 Anti Bacterial Peptides

1032

(1)

19.6 Reducing Environmental Pollution

1033

(1)

19.7 Conclusions

1033

(1)

References

1033

(6)

Chapter 2.20 Enzyme Technology for the Dairy Industry

1039

(28)

Kieran Kilcawley

20.1 Introduction

1040

(1)

20.2 Indigenous Enzymes of Bovine Milk

1040

(5)

20.2.1 Lipases

1041

(1)

20.2.1.1 Lipoprotein Lipase

1041

(1)

20.2.1.2 Bacterial Lipases

1042

(1)

20.2.1.3 Phospholipases

1042

(1)

20.2.2 Proteinases

1042

(1)

20.2.2.1 Plasmin or Milk Alkaline Proteinase

1042

(1)

20.2.2.2 Cathepsin D or Acid Milk Proteinase

1043

(1)

20.2.3 Phosphatases

1043

(1)

20.2.3.1 Alkaline Phosphomonoesterase (Phosphatase)

1043

(1)

20.2.3.2 Acid Phosphomonoesterase (Phosphatase)

1043

(1)

20.2.4 Lactoperoxidase

1044

(1)

20.2.5 Lysozymes

1044

(1)

20.2.6 Xanthine Oxidase

1044

(1)

20.2.7 y-Glutamyl Transpeptidase (Transferase)

1044

(1)

20.2.8 Other Enzymes

1045

(1)

20.3 Exogenous Enzymes Used in the Dairy Industry

1045

(18)

20.3.1 Exogenous Enzymes – Role in Natural Cheese Making

1045

(1)

20.3.1.1 Milk Clotting Enzymes (Rennet and Coagulants) – Role in Natural Cheese Making

1045

(4)

20.3.2 Lipase – Role in Natural Cheese Making

1049

(1)

20.3.2.1 Indigenous Milk Lipases – Role in Cheese Making

1049

(1)

20.3.2.2 Rennet Paste – Role in Cheese Making

1049

(1)

20.3.2.3 Pregastric Esterases (PGE) – Role in Cheese Making

1050

(1)

20.3.2.4 Microbial Lipases – Role in Cheese Making

1051

(1)

20.3.3 Accelerated Cheese Ripening

1052

(1)

20.3.3.1 Nonenzymatic Methods For Accelerating Cheese Ripening

1052

(1)

20.3.3.2 Accelerating Cheddar Cheese Ripening Using Enzyme Technology

1053

(3)

20.3.4 Enzyme Technology in Cheese as an Ingredient

1056

(1)

20.3.4.1 Fast Ripened Cheese

1056

(1)

20.3.4.2 Enzyme Modified Cheese

1056

(1)

20.3.4.3 Dehydrated Cheese Products

1059

(1)

20.3.4.4 Substitute or Imitation Cheese

1060

(1)

20.3.5 Lipolysed Cream and Butter Products

1060

(1)

20.3.6 Protein Hydrolysis

1061

(1)

20.3.7 Lactose Hydrolysis

1062

(1)

20.3.8 Lysozymes

1062

(1)

20.3.9 Transglutaminase

1062

(1)

References

1063

(4)

Chapter 2.21 Egg Yolk Antibody Farming for Passive Immunotherapy

1067

(20)

Jennifer Kovacs-Nolan and Yoshinori Mine

21.1 Introduction

1068

(1)

21.2 Avian Egg Antibodies

1068

(4)

21.2.1 Avian Immune System

1068

(1)

21.2.2 Molecular Properties of IgY

1069

(1)

21.2.2.1 Structure of IgY

1069

(1)

21.2.2.2 Physicochemical Properties of IgY

1069

(2)

21.2.3 Advantages of IgY

1071

(1)

21.3 Passive Immunization with IgY

1072

(5)

21.3.1 Immunotherapeutic Applications of IgY

1072

(1)

21.3.1.1 Rotavirus

1072

(1)

21.3.1.2 Escherichia coli

1072

(1)

21.3.1.3 Salmonella species

1074

(1)

21.3.1.4 Pseudomonas aeruginosa

1075

(1)

21.3.1.5 Streptococcus mutans

1076

(1)

21.3.1.6 Helicobacter pylori

1076

(1)

21.3.1.7 Coronavirus

1076

(1)

21.3.1.8 Fish Pathogens

1077

(1)

21.3.1.9 Others

1077

(1)

21.4 Antibody Stability

1077

(2)

21.4.1 Physiology of the Gastrointestinal Tract

1077

(1)

21.4.2 Degradation and Stability of IgY

1078

(1)

21.5 Biotechnology of Avian Egg Antibodies

1079

(1)

References

1079

(8)

Chapter 2.22 Application of Transgenic Fish Technology in Sea Food Production

1087

(22)

Pinwen Peter Chiou, Jenny Khoo, and Thomas T. Chen

22.1 Introduction

1087

(1)

22.2 Methods of Transgenic Fish Production

1088

(8)

22.2.1 Types of Transgene Constructs

1088

(3)

22.2.2 Selection of Fish Species

1091

(1)

22.2.3 Methods of Gene Transfer

1092

(3)

22.2.4 Characterization of Transgenic Fish

1095

(1)

22.3 Biotechnological Application of the Transgenic Fish Technology

1096

(6)

22.3.1 Growth Hormone Transgenic Fish

1096

(2)

22.3.2 Transgenic Fish with Enhanced Resistance to Pathogen Infection

1098

(1)

22.3.3 Transgenic Fish with Different Body Color

1099

(1)

22.3.4 Transgenic Fish as Environmental Biomonitors

1099

(2)

22.3.5 Other Examples of Transgenic Fish

1101

(1)

22.4 Concerns and Future Perspectives

1102

(1)

Acknowledgment

1103

(1)

References

1103

(6)

Chapter 2.23 The Production, Properties, and Utilization of Fish Protein Hydrolysates

1109

(24)

Hordur G. Kristinsson

23.1 Introduction

1109

(2)

23.2 The Enzymatic Hydrolysis Process

1111

(6)

23.2.1 Importance of Raw Material Source

1113

(1)

23.2.2 The Choice of Enzyme and pH Conditions

1113

(4)

23.3 Properties, Applications, and Potential Uses of Fish Protein Hydrolysates

1117

(5)

23.3.1 Food Functionality

1117

(1)

23.3.2 Solubility and Water-Binding Properties

1117

(2)

23.3.3 Interfacial and Surface Properties

1119

(1)

23.3.4 Lipid Binding

1120

(1)

23.3.5 Flavor Properties

1120

(2)

23.3.6 Antioxidant Properties

1122

(1)

23.4 Nutritional and Physiological Properties

1122

(3)

23.4.1 Animal Feed

1122

(2)

23.4.2 Plant Growth

1124

(1)

23.4.3 Bioactivity

1124

(1)

23.4.4 Microbial Media

1125

(1)

References

1125

(8)

Chapter 2.24 Human Gut Microflora in Health and Disease: Focus on Prebiotics

1133

(34)

Tamara Casci, Robert A. Rastall, and Glenn R. Gibson

24.1 Introduction to Human Gut Microflora and Fermentation Properties

1134

(2)

24.2 Gut Microflora in Health and Disease

1136

(4)

24.2.1 Acute Infections and Inflammatory Reactions

1136

(1)

24.2.2 Antibiotic Associated Diarrhea (AAD)

1137

(1)

24.2.3 Immune Stimulation

1137

(1)

24.2.4 Lactose Intolerance

1138

(1)

24.2.5 Colon Cancer

1138

(2)

24.2.6 Cholesterol Lowering Effect and Lipid Metabolism

1140

(1)

24.3 Structure to Function Relationships in Prebiotic Oligosaccharides

1140

(11)

24.3.1 Fructooligo sacchari des

1141

(1)

24.3.1.1 Fermentability of FOS

1141

(1)

24.3.1.2 FOS Interactions with Lipid Metabolism

1143

(1)

24.3.1.3 FOS Interactions with Mineral Absorption

1143

(1)

24.3.1.4 FOS Interactions with Cancer

1143

(1)

24.3.2 Galactooligosaccharides

1144

(1)

24.3.3 Isomaltooligosaccharides

1145

(1)

24.3.4 Lactulose

1146

(1)

24.3.4.1 Colon cancer

1147

(1)

24.3.4.2 Mineral absorption

1147

(1)

24.3.4.3 Constipation

1147

(1)

24.3.5 Soya products

1148

(2)

24.3.6 Lactosucrose

1150

(1)

24.3.7 Xylooligosaccharides

1150

(1)

24.4 Structure to Function Relationships in Other Oligosaccharides

1151

(2)

24.4.1 Lactitol

1151

(1)

24.4.2 Laevan Type Prebiotics

1151

(1)

24.4.3 Gentiooligosaccharides

1152

(1)

24.4.4 Glucose Based Oligosaccharides

1153

(1)

24.5 Conclusions

1153

(1)

References

1154

(13)

Chapter 2.25 Immunomodulating Effects of Lactic Acid Bacteria

1167

(38)

Hanne Risager Christensen and Hanne Frøkiœr

25.1 Introduction

1168

(1)

25.2 The Gut Mucosa — A Unique Compartment of the Immune System

1169

(7)

25.2.1 Organization of GALT

1169

(2)

25.2.2 Immune Responses of GALT and Peripheral Immune System

1171

(1)

25.2.2.1 Nonspecific Response Mechanisms

1172

(1)

25.2.2.2 Specific Response Mechanisms — Immunity vs. Tolerance

1172

(4)

25.3 Influence of the Gut Flora on the Immune Function

1176

(3)

25.3.1 The Gut Flora

1176

(2)

25.3.2 Interactions Between the Gut Flora and the Host Immune System

1178

(1)

25.4 Immunomodulatory Mechanisms of LAB

1179

(8)

25.4.1 Methods Used for Assessing Immunomodulatory Effect of LAB

1180

(2)

25.4.2 Effects of LAB on Nonimmunologic Mucosa Barrier Functions

1182

(1)

25.4.3 Effects on Phagocytic Cells

1182

(1)

25.4.4 Effects on NK Cell Activity

1183

(1)

25.4.5 Interactions Between LAB and Intestinal Epithelial Cells

1184

(1)

25.4.6 Effects on Cytokine Production

1184

(1)

25.4.7 Effects on Lymphocyte Proliferation

1185

(1)

25.4.8 Effects on Specific Immune Responses — Adjuvant Capacity of LAB

1186

(1)

25.4.9 Enhancement of IgA Production

1187

(1)

25.5 Effects of LAB on Diseases

1187

(6)

25.5.1 Effects of LAB on Intestinal Infections

1188

(1)

25.5.2 Effects on Inflammatory Bowel Disease

1189

(1)

25.5.3 Antiallergy Properties of LAB

1190

(1)

25.5.4 Antitumor Effect of LAB

1191

(1)

25.5.5 Impact of Viability and Dose on the Effects of LAB

1192

(1)

25.6 Concluding Remarks and Future Perspectives

1193

(1)

Acknowledgment

1193

(1)

References

1193

(12)

Chapter 2.26 Biochemical Markers for Antioxidant Functionality

1205

(24)

Dhiraj A. Vattem and K. Shetty

26.1 Introduction

1206

(1)

26.2 Direct Measurement of Reactive Oxygen Species

1207

(1)

26.3 Antioxidant Asssays

1208

(3)

26.3.1 Antioxidant Assays Based on Free Radical Neutralization

1208

(1)

26.3.2 2,2'-Azinobis-(3-ethylbenzthiazoline-6-sulfonic acid)

1209

(1)

26.3.3 Ferric Reducing Ability of Plasma (FRAP)

1210

(1)

26.3.4 Oxygen Radical Absorbance Capacity (ORAC) Assay

1210

(1)

26.3.5 β-carotene Oxidation (Bleaching) Assay

1211

(1)

26.4 Lipid Oxidation Products

1211

(2)

26.4.1 Malondialdehyde

1212

(1)

26.4.2 LDL Resistance to Oxidation

1212

(1)

26.4.3 F2 Isoprostanes

1213

(1)

26.5 DNA Oxidation Products

1213

(6)

26.5.1 8-Oxo-7,8-dihydro-2'-deoxyguanosine

1213

(1)

26.5.2 Glutathione Reduced (GSH) and Oxidized (GSSG)

1214

(2)

26.5.3 Glutathione Peroxidase

1216

(1)

26.5.4 Glutathione-S-Transferases

1216

(1)

26.5.5 Superoxide Dismutase

1216

(1)

26.5.6 Catalase

1217

(1)

26.5.7 Xanthine Oxidase and Uric acid

1217

(1)

26.5.8 NADPH Oxidoreductase

1218

(1)

26.5.9 Myeloperoxidase

1218

(1)

26.6 Plant Phenolic Dependent Peroxidases

1219

(1)

References

1219

(10)

Chapter 2.27 Enzymatic Synthesis of Oligosaccharides: Progress and Recent Trends

1229

(28)

V. Maitin and R.A. Rastall

27.1 Oligosaccharides

1230

(1)

27.1.1 Biological Importance of Oligosaccharides

1230

(1)

27.1.2 Oligosaccharides as Drugs and Functional Foods

1230

(1)

27.2 Chemical Synthesis

1231

(5)

27.2.1 Enzymatic Synthesis

1232

(1)

27.2.2 Glycosyltransferases

1232

(3)

27.2.3 Glycosidases

1235

(1)

27.3 Equilibrium Controlled Synthesis

1236

(2)

27.3.1 Kinetically Controlled Synthesis

1237

(1)

27.4 Influence of Reaction Components and Conditions on Yield and Selectivity

1238

(7)

27.4.1 Donor:Acceptor Sugar Ratio

1238

(2)

27.4.2 Temperature

1240

(1)

27.4.3 Enzyme Origin

1240

(1)

27.4.4 Use of Organic Solvents

1241

(1)

27.4.5 Substrate Concentration

1242

(1)

27.4.6 pH

1243

(1)

27.4.7 Time

1243

(1)

27.4.8 Enzyme Immobilization

1244

(1)

27.5 Recombinant and Engineered Glycosidases in Oligosaccharide Synthesis

1245

(3)

27.5.1 Mutant Glycosidases

1245

(1)

27.5.1.1 Glycosynthases

1245

(1)

27.5.1.2 Mutant Enzymes other than Glycosynthases

1247

(1)

27.5.1.3 Mutant Glycosidases Created by Directed Evolution

1247

(1)

27.6 Conclusions

1248

(1)

References

1248

(9)

SECTION 3 FOOD SAFETY, NOVEL BIOPROCESSING, TRADITIONAL FERMENTATIONS, AND REGULATORY ISSUES

1257

Chapter 3.01 Molecular Evolution and Diversity of Food Borne Pathogens

1259

(34)

Katy Windham, Kendra Kerr Nightingale, and Martin Wiedmann

1.1 Introduction

1260

(1)

1.2 Mechanisms of Bacterial Evolution

1261

(6)

1.2.1 Mutations

1262

(1)

1.2.1.1 Substitutions

1263

(1)

1.2.1.2 Insertions and Deletions

1263

(1)

1.2.1.3 Inversions

1263

(1)

1.2.1.4 Recombination

1264

(1)

1.2.2 Horizontal Gene Transfer

1264

(1)

1.2.2.1 Horizontal Gene Transfer of Homologous Gene Sequences

1265

(1)

1.2.2.2 Horizontal Gene Transfer of Nonhomologous Gene Sequences

1266

(1)

1.2.3 Natural Selection

1266

(1)

1.3 Molecular Subtyping Methods to Study Evolution of Food Borne Pathogens

1267

(2)

1.3.1 Phenotype Based Subtyping Methods

1267

(1)

1.3.2 DNA Based Subtyping Methods

1268

(1)

1.3.2.1 DNA Sequencing Based Subtyping and Characterization Methods

1268

(1)

1.3.2.2 MLVA

1269

(1)

1.3.2.3 Whole Genome Sequencing and Whole Genome Microarray Based Characterization Methods

1269

(1)

1.4 Phylogenetic and Population Genetic Methods

1269

(9)

1.4.1 Models of DNA Substitution

1270

(1)

1.4.2 Estimating Phylogenetic Trees

1271

(1)

1.4.2.1 Distance Based Methods to Infer Phylogeny

1272

(1)

1.4.2.2 Parsimony Methods to Infer Phylogeny

1272

(1)

1.4.2.3 Maximum Likelihood Methods to Infer Phylogeny

1272

(1)

1.4.2.4 Measures of Confidence for Traditional Phylogeny Estimation Methods

1273

(1)

1.4.2.5 Bayesian Methods

1273

(1)

1.4.3 Measuring Recombination

1273

(1)

1.4.3.1 Nonparametric Methods to Detect Recombination

1273

(1)

1.4.3.2 Parametric Methods to Detect Recombination and Measure Rate of Recombination

1275

(1)

1.4.4 Detecting Natural Selection and Models of Population Genetics

1276

(1)

1.4.4.1 Estimating Synonymous and Nonsynonymous Substitution Rates

1277

(1)

1.4.4.2 Prediction of Amino Acid Sites Under Positive Selection

1277

(1)

1.4.4.3 Detecting Adaptive Evolution in Lineages

1278

(1)

1.5 Molecular Evolution and Diversity of Selected Food Borne Pathogens

1278

(6)

1.5.1 Evolution of Escherichia coli

1278

(2)

1.5.2 Evolution and Diversity of Salmonella

1280

(2)

1.5.3 Evolution and Diversity of Listeria monocytogenes

1282

(2)

1.6 Conclusions

1284

(1)

References

1285

(8)

Chapter 3.02 Genetics and Physiology of Pathogenicity in Food Borne Bacterial Pathogens

1293

(36)

Michael Gray and Kathryn J. Boor

2.1 Introduction

1294

(1)

2.2 Clostridium botulinum

1295

(6)

2.2.1 Introduction and History

1295

(1)

2.2.1.1 Characteristics of Botulism

1295

(1)

2.2.1.2 Characteristics of Clostridium botulinum

1296

(1)

2.2.1.3 Classification of C. botulinum

1296

(1)

2.2.1.4 Sources in the Environment

1297

(1)

2.2.2 Virulence Factors

1297

(1)

2.2.2.1 The Botulism Toxin

1297

(1)

2.2.2.2 Toxin Structure

1297

(1)

2.2.3 Sporulation

1298

(1)

2.2.4 Genetics and Regulation

1298

(1)

2.2.4.1 Toxin Genes

1298

(1)

2.2.4.2 Regulation of Toxin Production

1299

(1)

2.2.4.3 Sporulation Genes

1300

(1)

2.2.5 Summary

1300

(1)

2.3 Escherichia coli 0157:H7

1301

(9)

2.3.1 Introduction and History

1301

(1)

2.3.1.1 Characteristics of Disease

1301

(1)

2.3.1.2 Characteristics of E. coli 0157:H7

1301

(1)

2.3.1.3 Relatives of E. coli 0157:H7

1302

(1)

2.3.1.4 Sources in the Environment

1303

(1)

2.3.2 Virulence Factors

1303

(1)

2.3.2.1 Acid Tolerance and Low Infective Dose

1303

(1)

2.3.2.2 Adhesion to the Intestinal Epithelium

1303

(1)

2.3.2.3 A/E Lesions

1303

(1)

2.3.2.4 The Locus of Enterocyte Effacement (LEE)

1304

(1)

2.3.2.5 Type III Secretion

1304

(1)

2.3.2.6 Shiga-Like Toxin

1305

(1)

2.3.2.7 Other Potential Virulence Factors

1305

(1)

2.3.3 Genetics and Regulation

1305

(1)

2.3.3.1 Structure of the LEE

1306

(1)

2.3.3.2 Regulation of the LEE

1306

(1)

2.3.3.3 LEE Encoded Regulator (Ler)

1307

(1)

2.3.3.4 Quorum Sensing

1307

(1)

2.3.3.5 Alternative Sigma Factors

1308

(1)

2.3.3.6 Regulation of Shiga Toxin Production

1308

(1)

2.3.3.7 Bacteriophage Lambda (A)

1308

(1)

2.3.3.8 Regulation of Stx Genes

1309

(1)

2.3.4 Summary

1310

(1)

2.4 Listeria monocytogenes

1310

(8)

2.4.1 Introduction and History

1310

(1)

2.4.1.1 Characteristics of Listeriosis

1310

(1)

2.4.1.2 Characteristics of Listeria monocytogenes

1311

(1)

2.4.1.3 Classification of Listeria monocytogenes

1311

(1)

2.4.1.4 Sources in the Environment

1312

(1)

2.4.2 Virulence Factors

1313

(1)

2.4.2.1 Internalins

1313

(1)

2.4.2.2 Listeriolysin 0 (LLO)

1313

(1)

2.4.2.3 Phospholipases

1314

(1)

2.4.2.4 ActA and Actin Based Motility

1314

(1)

2.4.2.5 Other Virulence Factors

1315

(1)

2.4.3 Genetics and Regulation

1315

(1)

2.4.3.1 Organization of Virulence Genes

1315

(1)

2.4.3.2 PrfA

1315

(1)

2.4.3.3 Regulation of PrfA Expression

1316

(1)

2.4.3.4 Regulation of Virulence Genes

1317

(1)

2.4.4 Summary

1317

(1)

2.5 Conclusions

1318

(3)

2.5.1 Common Themes in Bacterial Pathogenesis

1318

(1)

2.5.2 Pathogenicity Islands, Horizontal Gene Transfer, and the Evolution of Pathogens

1318

(1)

2.5.3 Emerging Pathogens and Human Food Practices

1319

(1)

2.5.4 Applications of Genetic and Molecular Understanding of Pathogenesis

1320

(1)

2.6 Recommended Reading

1321

(1)

References

1322

(7)

Chapter 3.03 Biofilm Production by Listeria monocytogenes

1329

(14)

William K. Shaw, Jr and Lynne McLandsborough

3.1 Introduction

1329

(1)

3.2 Biofilm Formation and Structure

1330

(1)

3.3 Listeria monocytogenes

1331

(6)

3.3.1 Biofilm Formation by Listeria monocytogenes

1332

(1)

3.3.1.1 Attachment and Biofilm Formation of L. monocytogenes to Surfaces

1332

(1)

3.3.1.2 Genetics and Proteomics of Biofilm Formation

1333

(1)

3.3.1.3 Influence of Lineages on Biofilm Formation

1334

(1)

3.3.2 Listeria in the Processing Environment

1335

(1)

3.3.3 Resistance of L. monocytogenes Biofilms to Sanitizing Agents

1336

(1)

3.4 Future Directions

1337

(1)

Acknowledgments

1338

(1)

References

1338

(5)

Chapter 3.04 Application of Microbial Molecular Techniques to Food Systems

1343

(16)

Robert E. Levin

4.1 The Polymerase Chain Reaction (PCR)

1344

(8)

4.1.1 Introduction

1344

(1)

4.1.2 Requirements for the PCR

1344

(1)

4.1.3 Sample Preparation Without Enrichment

1345

(1)

4.1.4 Lysing of Cells and Isolation of Bacterial DNA

1345

(1)

4.1.5 PCR for Identification of Pure Cultures

1346

(1)

4.1.6 Quantitative PCR

1346

(1)

4.1.7 Use of an Internal Standard for Quantitative PCR

1347

(1)

4.1.8 Construction of an Internal Standard for Quantitative PCR

1347

(1)

4.1.9 Construction of a Calibration Curve for Quantitative PCR

1348

(1)

4.1.10 The Use of Immunomagnetic Beads in Conjunction with PCR

1349

(1)

4.1.11 Nested PCR

1350

(2)

4.2 Random Amplification of Polymorphic DNA

1352

(1)

4.2.1 Introduction

1352

(1)

4.2.2 Mechanism of RAPD

1352

(1)

4.3 Pulsed Field Gel Electrophoresis

1353

(2)

4.3.1 Introduction

1353

(1)

4.3.2 Mechanism of PFGE

1353

(2)

4.3.3 Interpretation of PFGE Banding Patterns

1355

(1)

4.4 Summary

1355

(1)

References

1355

(4)

Chapter 3.05 Control of Food Borne Bacterial Pathogens in Animals and Animal Products through Microbial Antagonism

1359

(32)

Mindy M. Brashears, Alejandro Amezquita, and Divya Jaroni

5.1 Microbial Antagonism

1360

(1)

5.1.1 Lactic Acid Bacteria

1360

(1)

5.2 Reduction of Food Borne Pathogens in Foods of Animal Origin

1361

(9)

5.2.1 Antimicrobial Substances Produced by Lactic Acid Bacteria During In Vitro Application

1361

(1)

5.2.1.1 Hydrogen Peroxide

1361

(1)

5.2.1.2 Weak Organic Acids

1362

(1)

5.2.1.3 Reuterin

1362

(1)

5.2.1.4 Diacetyl

1363

(1)

5.2.1.5 Bacteriocins

1363

(1)

5.2.1.6 Low Molecular Weight Metabolites

1364

(1)

5.2.2 Lactic Acid Bacteria and Inhibition of Food Borne Pathogens in Meat Products

1364

(6)

5.3 Use of Lactic Acid Bacteria for In Vivo Reduction of Food Borne Pathogens

1370

(11)

5.3.1 Definition of Probiotic and Direct Fed Microbial

1370

(1)

5.3.2 Use of Direct Fed Microbials in Farm Animals

1371

(1)

5.3.2.1 Concept of Direct Fed Microbials

1371

(1)

5.3.2.2 Microorganisms Used in Direct Fed Microbials

1371

(1)

5.3.2.3 Direct Fed Microbials and Microbial Angogonism in Animals

1372

(1)

5.3.2.4 Pathogen Reduction

1372

(1)

5.3.2.5 Improved Animal Performance

1375

(1)

5.3.2.6 Effect on Immune Response

1375

(1)

5.3.3 Selection Criteria for Lactic Acid Bacteria to be Used as Direct Fed Microbials

1376

(1)

5.3.3.1 Survival in the Gastrointestinal Tract

1376

(1)

5.3.3.2 Adhesion to Intestinal Epithelium

1377

(1)

5.3.3.3 Host Specificity

1377

(1)

5.3.3.4 Production of Antimicrobial Compounds

1377

(1)

5.3.3.5 Antibiotic Susceptibility

1378

(1)

5.3.3.6 Technological Properties

1378

(1)

5.3.3.7 Possible In Vivo Mechanisms of Action

1379

(2)

References

1381

(10)

Chapter 3.06 Bacteriocins: Antimicrobial Activity and Applications

1391

(48)

A. Satyanarayan Naidu, Ragip Unal, and Joseph Tulpinski

6.1 Introduction

1392

(1)

6.2 Biosynthesis and Function

1393

(4)

6.2.1 Genetics

1393

(1)

6.2.2 Regulation

1394

(2)

6.2.3 Post-translational Events

1396

(1)

6.2.4 Immunity and Resistance

1397

(1)

6.3 Isolation and Characterization

1397

(2)

6.3.1 Purification Methods

1397

(1)

6.3.2 Quantitative Assays

1398

(1)

6.4 Classification

1399

(4)

6.4.1 Class I: Lantibiotics

1399

(1)

6.4.1.1 Type A

1400

(1)

6.4.1.2 Type B

1401

(1)

6.4.2 Class II: Small Heat Stable Peptides (Non-lantibiotics)

1401

(1)

6.4.2.1 Class IIa

1401

(1)

6.4.2.2 Class IIb

1401

(1)

6.4.2.3 Class IIc

1401

(1)

6.4.2.4 Class IId

1401

(1)

6.4.2.5 Class IIe

1403

(1)

6.4.2.6 Class IIf – Atypical Class II Bacteriocins

1403

(1)

6.4.3 Class III: Large Heat Labile Proteins

1403

(1)

6.4.4 Class IV: Complex Proteins

1403

(1)

6.5 Class I: Lantibiotics

1403

(7)

6.5.1 Type A: Nisin

1403

(1)

6.5.1.1 Mechanism of Action

1406

(1)

6.5.1.2 Antimicrobial Spectrum

1407

(1)

6.5.1.3 Applications

1408

(2)

6.6 Class II: Small Heat Stable Peptides

1410

(4)

6.6.1 Class Ha: Pediocins

1410

(1)

6.6.1.1 Mechanism of Action

1410

(1)

6.6.1.2 Antimicrobial spectrum

1411

(1)

6.6.1.3 Applications

1411

(2)

6.6.2 Class Hb: Sakacins

1413

(1)

6.6.2.1 Mechanism of Action

1413

(1)

6.6.2.2 Antimicrobial Spectrum

1413

(1)

6.6.2.3 Applications

1414

(1)

6.7 Food Applications

1414

(3)

6.7.1 Dairy Products

1414

(1)

6.7.2 Meat Products

1415

(1)

6.7.3 Seafood Products

1416

(1)

6.7.4 Canned Foods

1417

(1)

6.7.5 Beverages

1417

(1)

6.8 "Multiple Hurdle" Applications

1417

(5)

6.8.1 Thermal Processing

1419

(1)

6.8.2 Nonthermal Food Processing

1419

(1)

6.8.3 Metal Chelators and Detergents

1420

(1)

6.8.4 Lactoperoxidase (LPO) System

1420

(1)

6.8.5 Acid Interventions

1421

(1)

6.8.6 Plant Extracts and Essential Oils

1421

(1)

6.8.7 Bacteriocin Cocktails

1421

(1)

6.9 Food Packaging Applications

1422

(1)

6.10 Regulatory Status

1422

(1)

6.11 Conclusions

1423

(1)

References

1424

(15)

Chapter 3.07 Genetic Characterization of Antimicrobial Peptides

1439

(40)

Haijing Hu, Matthew M. Moake, and Randy W. Worobo

7.1 Introduction

1440

(1)

7.2 Gram-Positive Bacteriocins

1440

(19)

7.2.1 Class I Bacteriocins: Lantibiotics

1441

(1)

7.2.1.1 Nisin

1441

(1)

7.2.1.2 Biosynthesis of Other Lantibiotics

1448

(1)

7.2.2 Class II Bacteriocins: Small, Heat Stable,Non-Lanthionine-Containing Peptides

1449

(1)

7.2.2.1 Class Ha Bacteriocins

1450

(1)

7.2.2.2 Class lib and lIc Bacteriocins

1456

(1)

7.2.3 Class III Bacteriocins: Large, Heat Labile Proteins

1457

(1)

7.2.3.1 Helveticin J

1458

(1)

7.2.4 Class IV Bacteriocins: Complex, Modified Bacteriocins

1458

(1)

7.3 Gram-Negative Bacteriocins and Bacteriocin-Like Compounds

1459

(5)

7.3.1 Microcins

1459

(1)

7.3.1.1 Microcin Biosynthesis

1460

(2)

7.3.2 Colicins

1462

(1)

7.3.2.1 Structure and Mode of Action

1462

(1)

7.3.2.2 Colicin Biosynthesis

1463

(1)

7.3.3 Other Gram-Negative Bacteriocins

1463

(1)

7.4 Peptide Antibiotics

1464

(1)

7.5 Industrial Applications of Antimicrobial Peptides

1465

(2)

7.6 Future Prospectus

1467

(1)

Acknowledgments

1468

(1)

References

1468

(11)

Chapter 3.08 Phenolic Antimicrobials from Plants for Control of Bacterial Pathogens

1479

(26)

Kalidas Shetty and Yuan-Tong Lin

8.1 Phenolic Antimicrobials from Plants

1480

(2)

8.2 Potential of Lamiaceae as Source of Phenolic Antimicrobials

1482

(3)

8.2.1 Control of Staphylococcus Aureus by Phenolic Phytochemicals as a Model for Plant Based Antimicrobials

1482

(1)

8.2.2 Control of Listeria Monocytogenes by Oregano Clonal Extracts as a Model for Developing Herb Phenolics as Antimicrobials

1483

(2)

8.3 Filling Gaps in Antimicrobial Strategy with Tissue Culture Based Screening of Elite Phenolic Phytochemical-Producing Lines

1485

(7)

8.3.1 Novel Model for Mechanism of Action of Phenolic Phytochemicals

1486

(4)

8.3.2 Control of Helicobacter Pylon by Phenolic Antimicrobials from Plants

1490

(1)

8.3.3 Current Treatment Strategies for H. Pylori and Its Limitations

1491

(1)

8.3.4 Dietary Phenolic Phytochemical Strategies for Control of H. Pylon

1492

(1)

8.4 Dietary Soybean Approach for Control of H. Pylori

1492

(3)

8.4.1 Sprouting of Soybean and Phenolic Antioxidant Stimulation Methods

1493

(2)

8.4.2 Phenolic Response and Characterization of Soybean Extracts Inhibiting H. Pylon Urease

1495

(1)

8.4.3 Solid-State Bioprocessing of Soybean Using Rhizopus Oligosporus

1495

(1)

8.5 Recent Progress and Other Strategies for Designing Phenolics Phytochemicals as Antimicrobials

1495

(1)

8.6 Summary

1496

(1)

References

1496

(9)

Chapter 3.09 Genetic Mechanisms Involved in Regulation of Mycotoxin Biosynthesis

1505

(38)

Michael J. Miller and John E. Linz

9.1 Introduction

1506

(5)

9.1.1 Mycotoxins

1506

(1)

9.1.1.1 Aflatoxins

1506

(1)

9.1.1.2 Trichothecenes.

1508

(1)

9.1.1.3 Fumonisins

1510

(1)

9.2 Mechanisms of Mycotoxin Gene Regulation

1511

(21)

9.2.1 Transcriptional Regulation

1511

(1)

9.2.1.1 Aflatoxin Synthesis

1512

(1)

9.2.1.2 Trichothecene Synthesis

1515

(1)

9.2.1.3 Other Mycotoxins

1516

(1)

9.2.1.4 Activation and Inactivation of Transcription Factors

1516

(1)

9.2.2 Posttranscriptional Regulation

1516

(1)

9.2.3 Overview of Regulatory Inputs

1517

(1)

9.2.3.1 Nutrients

1517

(1)

9.2.3.2 Environment

1521

(1)

9.2.4 Signal Transduction Pathways

1522

(1)

9.2.4.1 G-Protein and Protein Kinase A (PKA) Signaling

1522

(1)

9.2.4.2 Lipids and Psi Factors

1525

(1)

9.2.4.3 Ethylene Signaling

1526

(1)

9.2.4.4 Other Volatiles

1526

(1)

9.2.4.5 Cyclins

1526

(1)

9.2.5 Gene Clusters and Positional Effects

1527

(1)

9.2.5.1 Organization of Gene Clusters

1527

(1)

9.2.5.2 Gene Cluster Dependent Regulation

1529

(1)

9.2.5.3 Significance of Gene Cluster Dependent Regulation

1530

(1)

9.2.5.4 Evolution of Mycotoxin Gene Clusters

1531

(1)

9.2.6 Summary

1532

(1)

References

1532

(11)

Chapter 3.10 Application of ELISA Assays for Detection and Quantitation of Toxins in Foods

1543

(24)

Robert E. Levin

10.1 Introduction

1544

(1)

10.2 Haptens and Their Conjugation to Proteins

1544

(1)

10.3 The Use of Enzymes in ELISA Assays

1545

(1)

10.4 The Use of Microtiter Plates in ELISA Assays

1545

(3)

10.5 The Use of the Avidin-Biotin System in ELISA Assays

1548

(3)

10.5.1 Nature of the Avidin-Biotin Complex

1548

(1)

10.5.2 Biotinylation of ELISA Components and Conjugation of Avidin and Streptavidin to Proteins

1549

(2)

10.6 ELISA Detection of Toxins in Foods

1551

(10)

10.6.1 Seafood Toxins (Figure 10.5)

1551

(1)

10.6.1.1 Saxitoxins

1551

(1)

10.6.1.2 Ciguatoxin and Maitotoxin

1554

(1)

10.6.1.3 Brevitoxins

1555

(1)

10.6.1.4 Domoic Acid

1555

(1)

10.6.1.5 Okadaic Acid

1555

(1)

10.6.1.6 Seafood Allergens

1556

(1)

10.6.2 Fungal Toxins (Figure 10.7)

1557

(1)

10.6.2.1 Aflatoxins

1557

(1)

10.6.2.2 Ochratoxin

1559

(1)

10.6.2.3 Trichothecenes

1559

(1)

10.6.3 Natural Plant Toxins

1560

(1)

10.6.3.1 Ricin

1560

(1)

10.7 Summary

1561

(1)

References

1561

(6)

Chapter 3.11 Biosensors for Food Quality Assessment

1567

(38)

Michele Del Carlo, Mihaela Nistor, Dario Campagnone, Bo Mattiasson, and Elisabeth Csöregi

11.1 Introduction

1567

(2)

11.1.1 Background

1567

(1)

11.1.2 Food Products as Analytical Samples

1568

(1)

11.2 General Aspects of Biosensors

1569

(1)

11.3 Potential Applications

1570

(19)

11.3.1 Biosensors for Food Components Analysis

1570

(1)

11.3.1.1 Monitoring of Wine Quality: Biosensors for Ethanol, Glucose and Glycerol

1576

(1)

11.3.1.2 Monitoring of Fish Quality: Biosensors for Biogenic Amines

1577

(2)

11.3.2 Biosensors for Food Contaminants Analysis

1579

(1)

11.3.2.1 Microorganisms in Food

1579

(1)

11.3.2.2 Pesticides in Food

1585

(1)

11.3.2.3 Antibiotics in Food

1587

(1)

11.3.2.4 Heavy Metals in Food

1587

(2)

11.4 Commercially Available Biosensors for Food Analysis

1589

(5)

11.5 Conclusions

1594

(2)

Acknowledgments

1596

(1)

References

1597

(9)

Abstract

1606

Chapter 3.12 Enzymatic Bioprocessing of Tropical Seafood Wastes

1605

(26)

Rupsankar Chakrabarti

12.1 Introduction

1606

(3)

12.2 Tropical Fishery Waste

1609

(4)

12.2.1 Fishing Vessel Catch Waste

1609

(1)

12.2.2 Waste During Handling at Landing Centers at Shore

1610

(1)

12.2.3 Waste from Filleting Units

1610

(1)

12.2.4 Waste from the Freezing Units

1611

(1)

12.2.4.1 Waste During Processing of Fin Fish

1611

(1)

12.2.4.2 Wastes from Peeling and Deveining of Shrimps and Lobsters

1611

(1)

12.2.4.3 Waste from Processing Units of Crabs and Cephalopods

1611

(1)

12.2.5 Wastes from Fish Canning Units

1611

(1)

12.2.6 Losses During Salting

1612

(1)

12.2.7 Losses During Reduction to Fishmeal

1612

(1)

12.2.8 Waste from Meat and Bone Separator Units

1613

(1)

12.2.9 Losses from Surimi Plants

1613

(1)

12.3 Product Development from Waste

1613

(14)

12.3.1 Products from Small and Bony Fish

1613

(1)

12.3.1.1 Fish Protein Hydrolysate

1613

(1)

12.3.1.2 Fish Paste and Fish Sauce

1616

(1)

12.3.2 Products from Filleting Waste

1617

(1)

12.3.3 Products from Head and Viscera Waste

1618

(2)

12.3.4 Use of Red Meat from Tuna Waste

1620

(1)

12.3.5 Waste Water from Surimi Plants

1620

(1)

12.3.6 Product from Stick Water

1621

(1)

12.3.7 Recovery of Chitin and Protein from Shellfish Waste

1621

(1)

12.3.8 Extraction of Carotenoprotein and Protein Isolate from Shellfish Waste

1621

(2)

12.3.9 Production of Seafood Flavorings

1623

(2)

12.3.10 Pearl Paste

1625

(1)

12.3.11 Products from Liver Waste

1626

(1)

References

1627

(4)

Chapter 3.13 Cold Active Enzymes in Food Processing

1631

(24)

Rajni Hatti-Kaul, Hákon Örn Birgisson, and Bo Mattiasson

13.1 Introduction

1632

(1)

13.2 Cold Adapted Organisms as a Source of Cold Active Enzymes

1633

(1)

13.3 Basis of Cold Activity

1633

(3)

13.3.1 Kinetic and Thermodynamic Adaptations

1633

(1)

13.3.2 Flexibility Versus Stability

1634

(1)

13.3.3 Active Site of Cold Active Enzymes

1635

(1)

13.3.4 Structural Adaptations

1635

(1)

13.3.5 Mutational Analysis of Cold Activity

1635

(1)

13.4 Directed Evolution as a Tool for Creation of Cold Active Enzymes

1636

(1)

13.5 Cold Active Enzymes of Interest for Food Processing

1637

(9)

13.5.1 Proteases

1637

(1)

13.5.1.1 Cold Active Proteases from Fish

1639

(1)

13.5.1.2 Proteases Made Cold Active by Mutagenesis

1641

(1)

13.5.2 Glycosidases

1641

(1)

13.5.2.1 Cold Active (3-galactosidases

1642

(1)

13.5.2.2 Cold Active Pectinases

1644

(1)

13.5.2.3 Cold Active a-amylase

1644

(1)

13.5.2.4 Cold Active Xylanase

1644

(1)

13.5.2.5 Cold Active Endoglucanases

1645

(1)

13.5.2.6 Cold Active Lysozyme

1645

(1)

13.5.3 Lipase

1645

(1)

13.5.4 Catalase

1645

(1)

13.5.5 Other Potential Applications

1646

(1)

13.6 Aspects on Production of Cold Active Enzymes

1646

(1)

References

1647

(8)

Chapter 3.14 Biotransformations as Applicable to Food Industries

1655

(36)

B. Suresh, T Ritu and G.A. Ravishankar

14.1 Introduction

1656

(5)

14.1.1 Potential of Microbial Cells and Plant Cells to Carry Out Biotransformation

1657

(1)

14.1.2 Reactions Involved in Biotransformation

1657

(1)

14.1.3 Advantages of Biotransformation

1658

(1)

14.1.4 Design of Biotransformation Processes

1658

(1)

14.1.4.1 Selection of Microorganism

1658

(1)

14.1.4.2 Methods for Carrying Out Biotransformation Process

1658

(2)

14.1.5 Improvement of Biotransformation Process

1660

(1)

14.1.5.1 Optimization of Environmental Conditions

1660

(1)

14.1.5.2 Strain Improvement

1660

(1)

14.1.5.3 Elimination of Side Reactions

1660

(1)

14.1.6 Downstream Processing or Product Isolation

1660

(1)

14.2 High Fructose Corn Syrup

1661

(5)

14.2.1 Biotechnology Involved in Process

1661

(1)

14.2.2 Source of Enzyme for Production

1661

(1)

14.2.3 Production of HFCS and Immobilization of Enzyme

1662

(2)

14.2.4 Salient features of xylose isomerase and glucose isomerase

1664

(2)

14.2.5 Process Parameters

1666

(1)

14.3 Oligosaccharides

1666

(4)

14.3.1 Classification of Oligosaccharides

1667

(1)

14.3.2 Fructooligosaccharides

1668

(1)

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Food Biotechnology, Second Edition

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Table of Contents

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Rent More, Save More! Use code: BBRENTAL

5% off 1 book, 7% off 2 books, 10% off 3+ books

Food Biotechnology, Second Edition

Summary

Table of Contents

Supplemental Materials

Digital License