Nutraceutical Proteins and Peptides in Health and Disease

Note: Supplemental materials are not guaranteed with Rental or Used book purchases.

ISBN: 9780824753542 | 0824753542
Cover: Hardcover
Copyright: 9/29/2005

Rent

(Recommended)

$174.67

Term

Due

Price

Semester

Dec 13

$183.86

Quarter

Aug 16

$174.67

Short Term

Jul 2

$165.47

*This item is part of an exclusive publisher rental program and requires an additional convenience fee. This fee will be reflected in the shopping cart.
Buy New

Usually Ships in 3-5 Business Days

$251.19
eBook

Available Instantly

Online: 180 Days

Downloadable: 180 Days

$185.63

Memorial Univ. of Newfoundland, Canada. Offers research articles on bioactive proteins and peptides in neutraceutical and functional foods. Discusses hypo-allergenic foods, approaches to nutraceutical research, and the impact of protein and peptides on various body systems. For biochemists, health professionals, and scientists.

SECTION I Nutrient Absorption System

Chapter 1 Nutraceutical Proteins and Peptides in Health and Disease: An Overview

(8)

Yoshinori Mine and Fereidoon Shahidi

1.1 The Nutrient Absorption System

(1)

1.2 The Body's Defense System

(1)

1.3 The Body's Regulatory System

(1)

1.4 The Body's Nervous System

(1)

1.5 Hypoallergenic Foods

(1)

1.6 Modern Approaches to Bioactive Proteins and Peptides

(1)

References

(3)

Chapter 2 Calcium Binding Peptides

(18)

David D. Kitts

2.1 Introduction

(2)

2.2 Sources of Calcium-Binding Peptides from Milk Proteins

(3)

2.3 Physicochemical Properties of CPP

(2)

2.4 Proposed Bioactive Properties of CPP

(2)

2.4.1 Bioavailability of Minerals

(1)

2.4.2 CPP and Bone Health

(1)

2.5 Other Potential Applications for CPP

(1)

2.6 Conclusions

(1)

References

(7)

Chapter 3 Mineral-Binding Proteins and Peptides and Bioavailability of Trace Elements

(12)

D. Bouglé and S. Bouhallab

3.1 Introduction

(1)

3.2 Biochemical Interactions among Minerals, TE, and Proteins or Peptides

(1)

3.2.1 Proteins

(1)

3.2.2 Peptides

(1)

3.3 Proteins and Bioavailability of TE

(2)

3.3.1 Calcium

(1)

3.3.2 Zinc

(1)

3.3.3 Iron

(1)

3.4 Peptides and Bioavailability of TE

(1)

3.5 Roles of CPP

(2)

3.5.1 Calcium

(1)

3.5.2 Zinc

(1)

3.5.3 Iron

(1)

3.6 Conclusions

(1)

References

(6)

Chapter 4 Cholesterol-Lowering Proteins and Peptides

(28)

Satoshi Nagaoka

4.1 Background

(1)

4.2 Hypocholesterolemic Milk Proteins and Novel Hypocholesterolemic Peptides

(9)

4.2.1 Serum Cholesterol and Bovine Milk Whey Protein

(1)

4.2.2 The Hypocholesterolemic Action of Major Constituents of Bovine Milk Whey Protein

(1)

4.2.3 The Hypocholesterolemic Action of Bovine Milk Whey Protein, its Major Constituent Protein P-Lactoglobulin, and its Tryptic Hydrolysate

(3)

4.2.4 Identification of Novel Hypocholesterolemic Peptides Derived from Bovine Milk β-Lactoglobulin

(4)

4.3 Cholesterol-Lowering Egg Proteins and Peptides

(3)

4.3.1 Egg White Protein and Cholesterol Metabolism

(1)

4.3.2 Ovomucin and Serum Cholesterol

(2)

4.4 Cholesterol-Lowering Meat Proteins and Peptides

(1)

4.5 Cholesterol-Lowering Fish Proteins

(1)

4.6 Cholesterol-Lowering Buckwheat Proteins and Peptides

(1)

4.7 Novel Cholesterol-Lowering Oligopeptides

(1)

4.8 Cholesterol-Lowering Soybean Proteins, Peptides, and Soybean Peptides with Bound Phospholipids

(6)

4.8.1 Effects of Amino Acid Sequence of Soybean Protein on Cholesterol Metabolism (Especially, Effects on Cholesterol Absorption and Re-Absorption of Bile Acid in the Intestine)

(2)

4.8.2 Effects of Amino Acid Composition of Soybean Protein on Cholesterol Metabolism

(1)

4.8.3 The Relationship between the Hypocholesterolemic Effect of Soybean Protein and the Endocrine System

(1)

4.8.4 Soy Isoflavonoids and Cholesterol Metabolism

(1)

4.8.5 The Health Claim and Industrial Utilization of Soy Protein and Peptides

(3)

References

(8)

Chapter 5 Heavy-Metal-Binding Proteins

(12)

Jennifer Kovacs-Nolan and Yoshinori Mine

5.1 Introduction

(1)

5.2 Metal-Binding Proteins and Peptides

(1)

5.2.1 Metallothioneins and Phytochelatins

(1)

5.2.2 Metallochaperones

(1)

5.2.3 Animal Fibrous Proteins

(1)

5.3 Physiological Function of Metal-Binding Proteins and Peptides

(1)

5.4 Isolation of Metal-Binding Proteins and Peptides

(1)

5.5 Applications of Heavy-Metal-Binding Proteins

(2)

5.5.1 Implications in Human Health and Disease

(1)

5.5.2 Nutritional Supplementation

(1)

5.5.3 Biosorption and Environmental Remediation

(1)

5.6 Genetic Engineering to Modify Metal-Binding and Sequestering Characteristics

(1)

Rcleiences

(5)

Chapter 6 Tight-Junction-Modulatory Factors in Food

(18)

Makoto Shimizu and Akira Mori

6.1 Major Mechanisms for Intestinal Absorption

(2)

6.2 Structure of the Tight Junction

(1)

6.3 Intracellular Signaling Pathway Modulating the Tight-Junction Permeability

(2)

6.4 Regulation of Tight-Junction Permeability by Internal Factors

(3)

6.5 Dietary Substances that Modulate Paracellular Permeability

(3)

References

(7)

SECTION II The Body's Defense System

Chapter 7 Antimicrobial Peptides

(38)

Judy C.K. Chan and Eunice C.Y. Li-Chan

7.1 Introduction

100

(1)

7.2 Sources of Antimicrobial Peptides

100

(14)

7.2.1 Mammalian Sources

100

(1)

7.2.1.1 Mammalian Defensins

100

(1)

7.2.1.2 Mammalian Cathelicidins

101

(1)

7.2.2 Plant Sources

101

(1)

7.2.2.1 Plant Defensins

101

(1)

7.2.2.2 Lipid Transfer Proteins

103

(1)

7.2.2.3 Hevein- and Knottin-Type Peptides

105

(1)

7.2.2.4 Other Novel Plant Antimicrobial Peptides

105

(1)

7.2.3 Marine Sources

105

(1)

7.2.3.1 Antimicrobial Peptides from Fishes

106

(1)

7.2.3.2 Antimicrobial Peptides from Crustaceans

107

(1)

7.2.3.3 Antimicrobial Peptides from Molluscs

110

(1)

7.2.4 Antimicrobial Peptides Derived from Enzymatic Hydrolyzates of Food Proteins

111

(1)

7.2.4.1 Dairy Proteins

111

(1)

7.2.4.2 Egg Proteins

112

(1)

7.2.5 Bacteriocin: Antimicrobial Peptides Produced by Bacteria

113

(1)

7.3 Modes of Antimicrobial Actions

114

(3)

7.3.1 Membrane Interaction

115

(1)

7.3.2 Membrane Penetration

116

(1)

7.3.3 Interactions with Other Cellular Components

117

(1)

7.4 Roles of Antimicrobial Peptides in the Immune System

117

(2)

7.5 Current Applications

119

(2)

7.5.1 The Use of Antimicrobial Peptides in Agriculture

119

(1)

7.5.2 The Use of Antimicrobial Peptides in Foods

119

(1)

7.5.3 The Use of Antimicrobial Peptides for Clinical Applications

120

(1)

7.6 Conclusions

121

(1)

Acknowledgments

121

(1)

References

121

(16)

Chapter 8 Bovine Milk Antibodies for Protection against Microbial Human Diseases

137

(24)

Hannu Korhonen and Pertti Marnila

8.1 Introduction

137

(1)

8.2 Biochemical Characteristics of Bovine Immunoglobulins

138

(1)

8.3 Technological Properties of Bovine Immunoglobulins

139

(1)

8.4 Digestion of Antibodies

140

(1)

8.5 Functions and Activities of Bovine Milk Antibodies

141

(10)

8.5.1 Inhibition of Enzyme Activity

142

(1)

8.5.2 Prevention of Adhesion

143

(1)

8.5.2.1 Caries Streptococci

144

(1)

8.5.2.2 Cryptosporidium parvum

145

(1)

8.5.2.3 Helicobacter

145

(1)

8.5.2.4 Escherichia coli

146

(1)

8.5.2.5 Shigella

146

(1)

8.5.2.6 Candida albicans

147

(1)

8.5.3 Neutralization of Toxins

147

(1)

8.5.4 Neutralization of Viruses

148

(1)

5.5.5 Opsonization

149

(2)

8.6 Synergistic Effects of Milk Antibodies with other Antimicrobial Factors

151

(1)

8.7 How Can Bovine Milk Antibodies Benefit Human Health in the Future

152

(2)

References

154

(7)

Chapter 9 Avian Immunoglobulin Y and Its Application in Human Health and Disease

161

(30)

Jennifer Kovacs-Nolan, Yoshinori Mine, and Hajime Hatta

9.1 Introduction

161

(1)

9.2 Egg Yolk as a Source of Antibodies

162

(3)

9.2.1 Antibodies and Avian Immunity

162

(1)

9.2.2 Advantages of Eggs as an Antibody Source

162

(2)

9.2.3 Production and Purification of IgY

164

(1)

9.3 Structure and Immunochemical Properties of IgY

165

(1)

9.4 Molecular Properties of IgY

166

(2)

9.4.1 Heat and pH Stability

166

(2)

9.4.2 Stability against Proteolytic Enzymes

168

(1)

9.5 Applications of IgY

168

(10)

9.5.1 Immunotherapeutic Applications of IgY

168

(1)

9.5.1.1 Oral Administration of IgY

168

(1)

9.5.1.2 Systemic Administration of IgY

175

(1)

9.5.2 Application of IgY as an Immunological Tool

176

(1)

9.5.2.1 Diagnostic Applications

176

(1)

9.5.2.2 Immunoaffinity Ligands

177

(1)

9.6 Future Applications of IgY

178

(1)

References

179

(12)

Chapter 10 Antiangiogenic Proteins, Peptides, and Amino Acids

191

(26)

Jack N. Losso and Hiba A. Bawadi

10.1 Introduction

192

(1)

10.2 Clinical Significance and Clinical Trials

193

(3)

10.3 Screening Antiangiogenic Compounds

196

(6)

10.3.1 Pitfalls of in vitro Angiogenesis Assays

198

(1)

10.3.1.1 In vivo Angiogenesis Assays

198

(1)

10.3.1.2 In vivo Matrigel Plug Assay

199

(1)

10.3.1.3 The Zebrafish

200

(2)

10.3.2 Pitfalls of in vivo Models

202

(1)

10.4 Antiangiogenic Polypeptides, Peptides, and Amino Acids

202

(4)

10.4.1 Cartilage

202

(1)

10.4.2 Collagen

202

(1)

10.4.3 α2-Macroglobulin

203

(1)

10.4.4 Bowman-Birk Inhibitor

203

(1)

10.4.5 Protamine

204

(1)

10.4.6 Lactoferrin

204

(1)

10.4.7 Lectins

205

(1)

10.4.8 Biliproteins

205

(1)

10.5 Other Proteins, Peptides, and Amino Acids

206

(1)

10.5.1 Opioid Growth Factors

206

(1)

10.5.2 L-Arginine

206

(1)

10.5.3 Glycine

206

(1)

10.5.4 Phenylalanine Metabolite

207

(1)

10.5.5 Selenocysteine

207

(1)

10.6 Challenges to Antiangiogenic Protein, Peptide, and Amino Acid Functional Foods

207

(1)

10.7 Bioavailability and Synergy of Antiangiogenic Polypeptide and Amino-Acid Functional Foods

208

(1)

10.8 Future Directions

209

(1)

10.9 Conclusions

209

(1)

References

210

(7)

Chapter 11 Relevance of Growth Factors for the Gastrointestinal Tract and Other Organs

217

(26)

Subrata Ghosh and Raymond J. Playford

11 1 Introduction

218

(1)

11.2 What are Growth Factors?

219

(5)

11.2.1 Nonpeptide "Trophic Factors"

220

(1)

11.2.2 Hormones

220

(1)

11.2.3 Cytokines

221

(1)

11.2.4 Growth Factors

221

(1)

11.2.4.1 Mucosal Integrity Peptides

221

(1)

11.2.4.2 Luminal Surveillance Peptides

223

(1)

11.2.4.3 Rapid Response Peptides

224

(1)

11.3 Overview of Other Peptides

224

(3)

11.3.1 Transforming Growth Factor-βs (TGF-βs)

224

(1)

11.3.2 Insulin-Like Growth Factors (IGF, Somatomedins) and Their Binding Proteins

224

(1)

11.3.3 Platelet-Derived Growth Factor (PDGF)

225

(1)

11.3.4 Vascular Endothelial Growth Factor (VEGF, Vasculotropin)

226

(1)

11.3.5 Keratinocyte Growth Factor (KGF)

226

(1)

11.3.6 Basic Fibroblast Growth Factor (bFGF)

226

(1)

11.4 Sources of Growth Factors

227

(3)

11.4.1 Natural Products

227

(1)

11.4.2 Partly Purified Natural Products

228

(1)

11.4.3 Isolated Individual Factors from Natural Products

229

(1)

11.4.4 Synthetically Produced Compounds Based on Natural Products

229

(1)

11.4.5 Artificially Modified Products Based on Natural Materials

230

(1)

11.4.6 Completely Artificial Compound with Growth Factor Actions

230

(1)

11.5 Growth Factor Therapy for Gut Disease

230

(3)

11.5.1 Short Bowel Syndrome

230

(1)

11.5.2 Nonsteroidal Antiinflammatory Drug (NSAID)-Induced Gut Injury

231

(501)

11.5.3 Chemotherapy-Induced Mucositis

732

(1)

11.5.4 Inflammatory Bowel Disease

732

11.5.5 Necrotizing Enterocolitis

232

(1)

11.6 Growth Factor Peptides in Therapy of Nongastrointestinal Diseases

233

(501)

11.6.1 Blocking of Angiogenesis as Therapy of Cancer

233

(1)

11.6.2 Promoting Angiogenesis in Ischemic Disease

233

(501)

11.6.3 Repair of Articular Cartilage

734

(1)

11.6.4 Use of Growth Factors to Stimulate Repair Following Eye Injury

734

(1)

11.7 Routes of Administration

734

(1)

11.8 Summary

734

(1)

Acknowledgments

735

(1)

References

735

Chapter 12 Cystatin: A Novel Bioactive Protein

243

(26)

Soichiro Nakamura

12.1 Introduction

243

(1)

12.2 Formation of the Cystatin Superfamily

244

(5)

12.3 Production and Use of Recombinant Cystatins

249

(7)

12.3.1 Application of Genetically Glycosylated Cystatin to Surimi Manufacturing

249

(3)

12.3.2 Anti-Salmonella and Anti-Rotavirus Effects of Genetically Glycosylated Cystatin

252

(2)

12.3.3 Anticancer Effects of Double-Mutated Cystatin

254

(2)

12.4 High-Level Production for Further Applications

256

(2)

12.5 Conclusions

258

(1)

Acknowledgment

259

(1)

References

259

(10)

SECTION III The Body's Regulating System

Chapter 13 ACE Inhibitory Peptides

269

(48)

Hans Meisel, Daniel J. Walsh, Brian Murray, and Richard J. FitzGerald

13.1 Introduction

269

(1)

13.2 Food-Protein-Derived ACE-Inhibitory Peptides

270

(9)

13.3 Structural Features of ACE Inhibition

279

(3)

13.4 Phenomenon of Multifunctionality of Milk-Protein-Derived ACE Inhibitors

282

(2)

13.5 Proteolytic Activation of Encrypted Ace-Inhibitory Peptides

284

(11)

13.6 Hypotensive Mechanisms

295

(3)

13.6.1 The Renin–Angiotensin System (RAS)

295

(2)

13.6.2 The Renin–Chymase System (RCS)

297

(1)

13.6.3 The Kinin–Nitric Oxide System (KNOS)

297

(1)

13.6.4 The Neutral Endopeptidase System (NEPS)

297

(1)

13.7 Hypotensive Effects In vivo

298

(1)

13.7.1 Animal Studies

298

(1)

13.7.2 Human Studies

299

(1)

13.8 Consumer Aspects

299

(5)

13.9 Potential Applications

304

(1)

Acknowledgment

305

(1)

References

305

(12)

Chapter 14 Regulation of Bone Metabolism: Milk Basic Protein

317

(18)

Yukihiro Takada and Seiichiro Aoe

14.1 Introduction

317

(1)

14.2 Bone Metabolism

318

(2)

14.3 MBP in Milk

320

(1)

14.4 Study on Osteoblasts

320

(3)

14.4.1 MBP

320

(1)

14.4.2 Kininogen Fragment 1.2

321

(1)

14.4.3 HMG-like Protein

322

(1)

14.5 Study on Osteoclasts

323

(1)

14.5.1 MBP

323

(1)

14.5.2 Milk Cystatin

324

(1)

14.6 Transport Ability of the Active Components by the Small Intestine

324

(1)

14.7 In vivo Studies Using Rats

325

(3)

14.7.1 Young OVX Rats

325

(1)

14.7.2 Growing Rats

326

(1)

14.7.3 Aged OVX Rats

327

(1)

14.8 Human Studies

328

(3)

14.8.1 Human Study 1

328

(2)

14.8.2 Human Study 2

330

(1)

14.9 Conclusions

331

(1)

References

332

(3)

Chapter 15 Anticariogenic Peptides

335

(18)

K.J. Cross, N.L. Huq, and E.C. Reynolds

15.1 Introduction — Dental Caries

335

(1)

15.2 Anticariogenic Food Groups

336

(1)

15.3 Anticariogenic Casein Phosphopeptides

337

(7)

15.3.1 Interaction of CPP with Calcium Phosphate

338

(1)

15.3.2 Anticariogenicity of CPP—ACP in the Rat

338

(1)

15.3.3 In vitro Remineralization of Enamel Lesions by CPP—ACP

339

(1)

15.3.4 Anticariogenicity of CPP—ACP in Human in situ Studies

340

(2)

15.3.5 Interaction of CPP—ACP with Fluoride

342

(2)

15.4 Casein Micelle Structure

344

(1)

15.5 Structure of the Anticariogenic CPP

344

(4)

15.6 Conclusions

348

(1)

References

349

(4)

Chapter 16 The Potential Therapeutic Role of Fibrinolytic Enzymes from Food in Cardiovascular Disease

353

(14)

Ada H.-K. Wong and Yoshinori Mine

16.1 Introduction – Cardiovascular Disease

353

(5)

16.2 Functional Foods

358

(1)

16.3 The Fibrinolysis System

359

(1)

16.4 Fibrinolytic Enzymes

359

(3)

16.4.1 Non-food Sources

360

(1)

16.4.2 Food Sources

361

(1)

References

362

(5)

SECTION IV The Body's Nervous System

Chapter 17 Opioid Peptides

367

(10)

Benjamin Guesdon, Lisa Pichon, and Daniel Tomé

17.1 Introduction — Opioids

367

(6)

17.1.1 The Mammalian Opioidergic System: Opioid Receptors and Endogenous Ligands

367

(2)

17.1.2 Exogenous Opioid Agonists and Antagonists

369

(3)

17.1.3 Functional Significance of Nutraceutical Opioid Peptides

372

(1)

References

373

(4)

Chapter 18 Factors that Affect the Body's Nervous System: Relaxation Effects of Tea L-Theanine

377

(16)

M. Ozeki, T.P. Rao, and L.R. Juneja

18.1 Introduction

377

(1)

18.2 Psychological Relaxation Effects

378

(3)

18.3 Physiological Relaxation Effects

381

(6)

18.3.1 Relaxation Effect in PMS

381

(1)

18.3.2 Antagonistic Effect Against Caffeine

382

(3)

18.3.3 Lowering Blood Pressure

385

(2)

18.4 Absorption and metabolism of L-theanine

387

(1)

18.5 Applications of Suntheanine®

388

(1)

18.6 Safety Aspects of Suntheanine®

389

(1)

18.7 Conclusions

389

(1)

References

389

(4)

SECTION V Hypoallergenic Foods

Chapter 19 Introduction to Food Allergy

393

(18)

Steve L. Taylor and Susan L. Hefle

19.1 Introduction

393

(1)

19.2 IgE-Mediated Food Allergy

394

(8)

19.2.1 Mechanism

394

(2)

19.2.2 Symptoms

396

(1)

19.2.3 Prevalence

397

(1)

19.2.4 Persistence

398

(1)

19.2.5 Commonly Allergenic Foods

398

(1)

19.2.6 Food Allergens

399

(1)

19.2.7 Diagnosis

399

(1)

19.2.8 Treatment

400

(1)

19.2.9 Prevention

401

(1)

19.2.10 Effect of Processing on Allergenicity

402

(1)

19.3 Delayed Hypersensitivity (Celiac Disease Example)

402

(2)

19.3.1 Symptoms

403

(1)

19.3.2 Prevalence

403

(1)

19.3.3 Causative Factor

403

(1)

19.3.4 Treatment

404

(1)

19.4 Conclusions

404

(1)

References

404

(7)

Chapter 20 The Production of Hypoallergenic Wheat Flour for Wheat-Allergic Patients

411

(20)

Soichi Tanabe and Jun Watanabe

20.1 Introduction

412

(1)

20.2 Symptoms of Adverse Reactions to Wheat Flour and their Responsible Determinants

412

(2)

20.2.1 Celiac Disease

412

(1)

20.2.2 Baker's Asthma

413

(1)

20.2.3 Atopic Dermatitis

413

(1)

20.2.4 Food-Dependent Exercise-Induced Anaphylaxis

414

(1)

20.3 Identification of Wheat Allergens and their Epitopes

414

(5)

20.3.1 Gluten Fraction

414

(1)

20.3.1.1 An Allergenic Peptide from Low-Molecular-Weight Glutenin

414

(1)

20.3.1.2 Gln-Gln-Gln-Pro-Pro as an IgE-binding Epitope

415

(1)

20.3.2 Albumin/Globulin Fractions, Especially Glycoproteins

416

(2)

20.3.3 Mannogluc an

418

(1)

20.4 Production of HWF and Hypoallergenic Products

419

(3)

20.4.1 Enzymatic Treatment of Wheat Flour to Produce Hypoallergenic Flour (HWF)

419

(2)

20.4.2 Hypoallergenic Wheat Products

421

(1)

20.4.3 Clinical Evaluation of HWF

421

(1)

20.5 Preventive and Suppressive Effects of HWF on Food Allergy

422

(3)

20.5.1 Inhibition of Allergen Absorption from the Intestinal Tract by HWF

423

(1)

20.5.2 Induction of Oral Tolerance by HWF

423

(2)

20.5.3 Haptenic Activity of HWF

425

(1)

References

425

(6)

Chapter 21 Milk Proteins

431

(14)

Koko Mizumachi and Jun-ichi Kurisaki

21.1 Introduction

431

(1)

21.2 Currently Available Hypoallergenic Formulas

432

(3)

21.2.1 Alternatives or Elimination of Cow's Milk

433

(1)

21.2.1.1 Soy Protein-Based Formulas

433

(1)

21.2.1.2 Amino Acid-Based Formulas

434

(1)

21.2.1.3 Goat's Milk

434

(1)

21.2.2 Destruction of Antigenic Structure

434

(1)

21.2.2.1 Heat Denaturation

434

(1)

21.2.2.2 Hydrolysis

435

(1)

21.3 Approaches to Antiallergic Foods Containing Milk Proteins

435

(4)

21.3.1 Genetic Modification of Milk Proteins

436

(2)

21.3.2 Oral Tolerance

438

(1)

21.3.3 Probiotics

438

(1)

21.4 Conclusions

439

(1)

References

439

(6)

Chapter 22 Egg Proteins

445

(16)

Prithy Rupa and Yoshinori Mine

22.1 Introduction

445

(1)

22.2 Physicochemical Characteristics of Eggs

446

(5)

22.2.1 Major Egg White Allergens

446

(1)

22.2.2 Ovomucoid

447

(1)

22.2.3 Ovalbumin

448

(2)

22.2.4 Ovotransferrin

450

(1)

22.2.5 Lysozyme

450

(1)

22.3 Processing of Eggs and Its Value-Added Hypoallergenic Application

451

(3)

22.3.1 Heat Denaturation and Enzymatic Digestions

452

(1)

22.3.2 Suppression of Allergic Potential of Egg White by Genetic Modification

453

(1)

References

454

(7)

Chapter 23 Soybean

461

(20)

Tadashi Ogawa

23.1 Introduction

461

(2)

23.2 Major Allergens in Soybean

463

(5)

23.2.1 Gly m Bd 30K

463

(1)

23.2.2 Gly m Bd 28K

464

(2)

23.2.3 Gly m Bd 60K (α-subunit of &bbeta;-conglycinin)

466

(1)

23.2.4 Other Allergenic Proteins

466

(2)

23.3 Development of Hypoallergenic Soybean Products

468

(7)

23.3.1 Determination of Allergenicity

468

(1)

23.3.2 Molecular Breeding

468

(1)

23.3.3 Reduction of Gly m Bd 30K by Genetic Modification

469

(1)

23.3.4 Physicochemical Reduction

470

(2)

23.3.5 Enzymatic Digestion

472

(2)

23.3.6 Chemical Modification

474

(1)

23.3.7 Extrusion Cooking

475

(1)

23.4 Evaluation of Hypoallergenic Soybean Products and Perspectives

475

(1)

References

476

(5)

Chapter 24 Meat Allergy

481

(12)

Soichi Tanabe and Toshihide Nishimura

24.1 Introduction

481

(1)

24.2 Beef Allergy and its Allergens

482

(2)

24.3 Pork Allergy and its Allergens

484

(1)

24.4 Chicken Allergy and its Allergens

485

(1)

24.5 Serum Albumin as a Cross-Reacting Meat Allergen

486

(1)

24.6 Methods of Reducing The Allergenicity of Meat Allergens

487

(2)

24.6.1 Heat Treatment

487

(1)

24.6.2 Enzymatic Treatment

488

(1)

24.6.3 Other Treatments

488

(1)

24.7 Summary

489

(1)

References

489

(4)

Chapter 25 Rice-Seed Allergenic Proteins and Hypoallergenic Rice

493

(20)

Tsukasa Matsuda, Masayuki Nakase, Angelina M. Alvarez, Hidehiko Izumi, Takeo Kato, and Yuichi Tada

25.1 Introduction – Adverse Allergenic Reactions to Rice

493

(1)

25.2 Rice-Seed Proteins and Allergens

494

(8)

25.2.1 Rice-Seed Proteins and Their Allergenic Potentials

494

(3)

25.2.2 Rice-Seed Allergens

497

(1)

25.2.2.1 Allergens with MW of ~14~ to ~16~kDa

497

(1)

25.2.2.2 Allergens with MW of 26-kDa

500

(1)

25.2.2.3 Allergens with MW of 33-kDa

501

(1)

25.2.3 Other Allergens

502

(1)

25.3 Hypoallergenic Rice

502

(6)

25.3.1 Degradation and Removal by Enzymatic Hydrolysis

502

(3)

25.3.2 Release and Removal by High Hydrostatic Pressure

505

(1)

25.3.3 Suppression of Biosynthesis by Genetic Modification

506

(2)

References

508

(5)

Chapter 26 Buckwheat Allergy

513

(30)

Chein-Soo Hong and Kyu-Earn Kim

26.1 Introduction

513

(1)

26.2 General Chemical and Nutritional Properties of Buckwheat Seeds

514

(1)

26.3 Uses of Buckwheat

515

(2)

26.4 Adverse Effects of Buckwheat

517

(1)

26.5 Pathogenetic Mechanism of Buckwheat Allergy

518

(1)

26.6 Prevalence of Buckwheat Allergy

519

(3)

26.7 Allergic Reaction and Symptoms

522

(4)

26.8 Occupational Lung Disease

526

(2)

26.9 Hypersensitivity Reaction to Buckwheat Other Than Allergy

528

(1)

26.10 Allergen Characterization

528

(2)

26.11 Cross Allergenicity

530

(2)

26.12 Diagnosis of Buckwheat Allergy

532

(2)

26.13 Treatment and Prevention

534

(3)

26.14 Prognosis of Buckwheat Allergy

537

(1)

References

537

(6)

SECTION VI Modern Approaches to Bioactive Proteins and Peptides

Chapter 27 Database of Protein and Bioactive Peptide Sequences

543

(22)

Jerzy Dziuba and Anna Iwaniak

27.1 Introduction

543

(2)

27.2 An Overview of Computer Methods Applied in Protein Sequence Analysis

545

(4)

27.2.1 Protein Data Bank

545

(1)

27.2.2 CATH

545

(1)

27.2.3 SWISS-PROT Database

546

(1)

27.2.4 Prosite

546

(1)

27.2.5 InterPro

547

(1)

27.2.6 SCOP — A Database of Structural Classification of Proteins

547

(1)

27.2.7 CluStr Database

548

(1)

27.2.8 Homology and Predict 7

548

(1)

27.3 The Database of Protein and Bioactive Peptide Sequences — BIOPEP

549

(11)

27.3.1 Database Description

549

(1)

27.3.2 New Criteria of Protein Evaluation in BIOPEP

550

(1)

27.3.3 Analysis of Protein in BIOPEP According to the New Criteria

551

(7)

27.3.4 Proteolytic Process Design in BIOPEP

558

(2)

27.4 Conclusions

560

(1)

Acknowledgments

560

(1)

References

560

(5)

Chapter 28 Rational Designing of Bioactive Peptides

565

(18)

Shuryo Nakai and Nooshin Alizadeh-Pasdar

28.1 Introduction

565

(2)

28.2 QSAR

567

(2)

28.3 Functional Sequence Analysis

569

(8)

28.4 Optimization

577

(1)

28.5 Rational Designing Strategy

578

(2)

28.6 Conclusions

580

(1)

Acknowledgment

580

(1)

References

580

(3)

Chapter 29 Engineering Hen Egg-White Lysozyme

583

(20)

Akio Kato

29.1 Introduction

583

(1)

29.2 Hyperglycosylation of Lysozyme by Genetic Engineering

584

(4)

29.3 Heat Stability of Oligomannosyl and Polymannosyl Lysozymes

588

(3)

29.4 Emulsifying Property of Oligomannosyl and Polymannosyl Lysozymes

591

(1)

29.5 Modification of Antimicrobial Action of Lysozyme

592

(9)

29.5.1 Reduction of Antigenic Structure of Lysozyme by Genetic Modifications

594

(3)

29.5.2 Amyloidogenic Mutant Lysozymes

597

(1)

29.5.3 Quality Control of Abnormal Proteins by Molecular Chaperones

598

(3)

Acknowledgment

601

(1)

References

601

(2)

Chapter 30 New Methodologies for the Synthesis of Oligopeptides and Conformation-Constrained Peptidomimetics

603

(16)

Kazuhiro Chiba

30.1 Introduction

603

(1)

30.2 New Liquid-Phase Pepeptide Synthesis (Lpps) Method Based on Thermomorphic Biphasic Organic Solutions

604

(7)

30.3 Electrolytic Cyclization of Dipeptides Involving Proline-Moiety for Construction of Conformation-Constrained Peptidomimetics

611

(5)

References

616

(3)

Chapter 31 Lacticin 3147

619

(20)

Paul D. Cotter, Colin Hill, and R. Paul Ross

31.1 Introduction

619

(2)

31.2 Applications for Lacticin 3147 in Food and in Medicine

621

(7)

31.2.1 Inhibition of Nonstarter Lactic Bacteria and the Regulation of Flavor and Quality in Cheese

621

(2)

31.2.2 Inhibition of Pathogens in Food

623

(2)

31.2.3 Mastitis Prevention in Cattle

625

(1)

31.2.4 Tolerance, Resistance, and Immunity

626

(2)

31.3 Molecular Analysis of Lacticin 3147 Production and Immunity

628

(3)

31.4 Discussion

631

(2)

Acknowledgments

633

(1)

References

633

(6)

Chapter 32 Membrane-Based Fractionation and Purification Strategies for Bioactive Peptides

639

(20)

Yves Pouliot, Sylvie F. Gauthier, and Prude Emilie Groleau

32.1 Introduction

640

(1)

32.2 Pressure-Driven Membrane-Based Separation

640

(3)

32.2.1 Separation Domains

640

(1)

32.2.2 Tangential Filtration

641

(2)

32.3 Strategies for Peptide Fractionation

643

(9)

32.3.1 Background Data

643

(1)

32.3.2 Overview of the Options

644

(1)

32.3.3 Pretreatments

645

(1)

32.3.3.1 Adsorbents

645

(1)

32.3.3.2 Salt- or pH-Induced Precipitation

646

(1)

32.3.3.3 Solvent Precipitation

646

(1)

32.3.4 Membrane-Based Separation

647

(2)

32.3.5 Purification Techniques

649

(1)

32.3.5.1 Chromatographic Methods

649

(1)

32.3.5.2 Other Techniques

651

(1)

32.4 Examples and Applications

652

(2)

32.4.1 Separation of Casein Phosphopeptides (CPP)

652

(1)

32.4.2 Production of Lactoferricin

652

(1)

32.4.3 Recovery of Nisin from Fermentation Broths

653

(1)

32.5 Conclusions

654

(1)

References

655

(4)

Index

659

Please wait while the item is added to your bag...

FREE SHIPPING

Amazon no longer offers textbook rentals. We do!

Nutraceutical Proteins and Peptides in Health and Disease

Summary

Table of Contents

Supplemental Materials