Whey proteins: from milk to medicine

Cover......Page 1
Whey Proteins:From Milk to Medicine......Page 3
Copyright......Page 4
List of Contributors......Page 5
 Hilton Deeth......Page 7
 Nidhi Bansal......Page 8
Preface......Page 9
Abbreviations......Page 13
 1.1 Introduction......Page 17
   1.2.1.1 Characteristics......Page 19
   1.2.1.2 Structure......Page 20
   1.2.1.3 Function......Page 21
   1.2.1.4 Significance......Page 22
   1.2.2.1 Characteristics......Page 23
   1.2.2.2 Structure......Page 24
   1.2.2.4 Significance......Page 25
   1.2.3.1 Characteristics......Page 26
   1.2.3.4 Significance......Page 27
   1.2.4.1 Characteristics......Page 28
   1.2.4.2 Structure......Page 29
 1.3 Minor Whey Proteins......Page 30
   1.3.1.1 Characteristics......Page 33
   1.3.1.2 Significance......Page 35
   1.3.2.2 Characteristics of PP3......Page 36
   1.3.2.3 Significance of PP3......Page 37
   1.3.3.1 Characteristics......Page 38
   1.3.3.2 Significance......Page 39
   1.3.4.1 Characteristics......Page 40
   1.3.4.2 Significance......Page 42
   1.3.5.1 Characteristics......Page 43
   1.3.5.2 Significance......Page 44
   1.3.6.1 Characteristics......Page 45
   1.3.6.2 Significance......Page 46
   1.3.7.1 Characteristics......Page 47
   1.3.8.1 Characteristics......Page 49
   1.3.8.2 Significance......Page 50
   1.3.9.1 Characteristics......Page 51
 References......Page 55
 2.1 Introduction......Page 67
  2.2.1 Cellulose Acetate......Page 69
  2.2.2 Polysulfone and Polyethersulfone......Page 70
  2.3.1 Reverse Osmosis......Page 71
   2.3.2.1 In the United States—1970–85......Page 72
   2.3.2.2 In Europe—1975–85......Page 74
   2.3.2.3 In New Zealand—1960–90......Page 77
   2.3.2.4 Domination of the Spiral-Wound Membrane—From the Mid 1980s......Page 80
  2.3.3 Nanofiltration......Page 82
  2.3.4 Ion Exchange Technology and Microfiltration—in the Development of Whey Protein Isolate......Page 85
   2.3.4.2 By-Products of WPI Production......Page 87
   2.4.1.1 Designer Protein—The First Instantized Whey Protein Powder......Page 88
   2.4.1.2 The Growth of Instantized Whey Protein Powders......Page 91
  2.4.2 Whey Protein Fractionation and Whey Protein Hydrolysates for Infant Formula......Page 94
   2.4.2.1 Whey Protein Fractionation......Page 96
 2.5 Whey Proteins and Advances in Cheese Making Technology......Page 98
  2.5.1 Increasing Cheese Output......Page 99
  2.5.2 Increasing Cheese Yield......Page 101
 2.6 Current Whey Protein Products and Their Applications......Page 102
  2.6.2 Physically Functional Applications......Page 103
  2.6.3 Nutritionally Functional Applications......Page 104
 2.7 Further Developments......Page 107
  2.7.2 New Technologies or Processes......Page 108
  2.7.4 New Areas of Application......Page 109
 References......Page 110
 Further Reading......Page 111
 3.1 Whey Protein Concentrates and Isolate by Ultrafiltration......Page 112
  3.1.1 Membrane Performance......Page 115
   3.1.1.1 UF Processing Parameters......Page 117
   3.1.1.2 Effect of Pretreatment—Original Milk and Wheys......Page 118
   3.1.2.1 Continuous Operation and Control......Page 119
   3.1.3.1 Charged Membranes......Page 121
   3.1.3.3 Protein Cross-Linking......Page 122
 3.2 Whey Protein Fractions by Membrane-Based Separations......Page 124
  3.2.1 Absorption Processes......Page 128
 3.3 Microparticulated Whey Protein......Page 129
  3.3.1 Effect of Spray Drying on Microparticulate Functionality......Page 131
  3.3.2 Examples of Commercial Initiatives......Page 132
 3.4 Conclusion......Page 133
 References......Page 134
 4.1 Introduction......Page 138
  4.2.1 Powder Stability and Molecular Mobility......Page 140
   4.2.2.1 Color of Stored Powder......Page 141
   4.2.2.3 Particle Surface Chemistry......Page 142
   4.2.2.5 Caking and Flow Properties......Page 144
   4.2.3.1 Modifications of Protein Structure......Page 145
   4.2.3.2 Protein Crosslinking......Page 146
   4.2.4.1 Maillard Reaction and Storage Conditions......Page 147
   4.2.4.3 Change of State: Crystallization......Page 150
   4.2.5.2 Heat-Induced Aggregation Properties......Page 151
   4.2.5.3 Foaming Properties......Page 153
   4.2.5.5 Interfacial Properties......Page 154
   4.3.1.1 Maillard Reaction......Page 155
   4.3.2.2 Intrinsic Factors......Page 157
  4.3.3 Prediction of Whey Protein Powder Changes......Page 158
 4.4 Conclusions......Page 162
 References......Page 163
 5.1 Introduction......Page 170
 5.2 Process-Induced Molecular Changes Affecting the Analysis of Whey Proteins......Page 173
  5.3.1 Immunological Techniques......Page 176
  5.3.2 Activity Based/Enzymatic Assays......Page 178
  5.3.3 Gel Electrophoresis......Page 180
  5.3.4 Capillary Electrophoresis......Page 182
   5.3.5.1 Preparative Chromatography......Page 183
   5.3.5.2 Analytical Chromatography......Page 185
  5.4.1 What Is Proteomics?......Page 186
  5.4.2 Proteomics in Whey Protein Analysis: Qualitative Versus Quantitative......Page 188
 5.5 Conclusions and Outlook......Page 190
 References......Page 191
 6.1 Introduction......Page 200
  6.2.1 The Influence of Molecular Properties of β-Lg on Denaturation and Aggregation......Page 201
  6.2.2 Kinetics and Thermodynamics of β-Lg Unfolding and Aggregation......Page 211
  6.3.1 Heat-Induced Changes in Whey Proteins Other Than β-Lg......Page 214
  6.3.2 Whey Protein−Whey Protein Interactions......Page 215
  6.3.3 Whey Protein−Casein Interactions......Page 216
  6.3.4 Aggregate Size and Structure of Thermally Denatured Whey Proteins......Page 218
  6.4.1 Rheological Properties......Page 221
  6.4.2 Surface Properties......Page 223
  6.4.3 Digestability of Whey Proteins......Page 226
   6.5.1.1 Physical Modification......Page 228
    6.5.1.2.1 Derivatization of Amino, Carboxyl, and Sulfhydryl groups......Page 230
    6.5.1.2.2 Enzymatic Cross-Linking......Page 233
    6.5.1.2.3 Interaction With Carbohydrates......Page 235
    6.5.1.2.4 Enzymatic Hydrolysis......Page 238
    6.5.1.2.5 Addition of Hydrophobic Compounds......Page 240
    6.5.1.2.6 Soluble Whey Protein Aggregates and Microparticulated Whey Proteins......Page 241
    6.5.1.2.7 Addition of “Chaperone” Proteins......Page 242
   6.5.1.3 Structural Modification......Page 243
 References......Page 246
 Further Reading......Page 262
 7.1 Introduction......Page 263
 7.2 Maillard Reaction Chemistry......Page 265
 7.3 Factors Affecting Maillard-Induced Conjugation of Whey Proteins......Page 267
 7.4 Whey Protein and Carbohydrate Substrates Used in Conjugation......Page 269
 7.5 Approaches Used to Achieve Conjugation......Page 270
 7.6 Techno-Functional Properties of Conjugated Whey Proteins......Page 271
  7.6.1 Solubility......Page 272
  7.6.2 Heat Stability......Page 274
  7.6.3 Emulsification......Page 277
  7.6.4 Foaming......Page 281
  7.6.5 Gelation and Textural Properties......Page 283
 7.7 Nutritional Properties of Conjugated Whey Proteins......Page 284
 7.8 Conclusions......Page 287
 References......Page 288
 8.1 Introduction......Page 295
  8.2.2 High Pressure Processing and Its Effect on Proteins......Page 296
   8.2.3.1 β-Lactoglobulin (β-Lg)......Page 298
   8.2.3.3 Bovine Serum Albumin......Page 299
  8.2.4 HP-Induced Changes in Milk......Page 300
  8.3.2 General Principles......Page 303
  8.3.3 Conformational and Colloidal Modifications of Proteins Due to Shear......Page 305
  8.3.4 Impact of Shear on Properties of Whey Proteins in the Absence of Heat......Page 308
  8.3.5 Impact of Shear Accompanying Preprocess or Simultaneous Application of Heating on the Properties of Whey Proteins – M.........Page 311
  8.4.2 Power Ultrasound: Frequency is Critical......Page 316
  8.4.3 Temperature and Sonication of Whey Protein Solutions......Page 319
  8.4.4 Effects of Power Ultrasound on the Solubility of Reconstituted Whey Protein Powders......Page 320
  8.4.5 Effect of Power Ultrasound on the Viscosity of Whey Protein Solutions......Page 321
  8.4.6 Effect of Power Ultrasound on Whey Protein Gelation......Page 323
  8.5.1 Introduction......Page 326
  8.5.2 Effect on Whey Proteins......Page 328
  8.6.1 Introduction......Page 332
  8.6.2 Effect on Whey Proteins......Page 333
 8.7 Conclusions......Page 335
 References......Page 336
 9.1 Whey Protein-Fortified Beverages......Page 349
  9.1.1 Neutral pH Beverages......Page 351
  9.1.3 Heat and Emulsion Stability......Page 352
   9.1.3.2 The Formation and Role of Soluble Whey Protein Aggregates......Page 355
   9.1.3.3 Chaperone-Protein Effects......Page 356
   9.1.3.5 Novel Fermented Whey-Based Drinks......Page 360
 9.2 Yogurt......Page 361
 9.3 Protein Bars......Page 368
  9.4.1 Fresh Dairy Desserts......Page 371
  9.4.3 Ice Cream......Page 372
 9.5 Cheese......Page 374
  9.5.1 The Contribution of Commercial Whey Protein-Based Fat Replacers......Page 375
  9.5.2 Denatured Whey Protein Concentrates......Page 378
  9.5.4 Incorporation of Whey Proteins Into Pasteurized Processed Cheese Products and Analogue Cheese Products......Page 379
 9.6 Conclusions......Page 381
 References......Page 382
 10.1 Introduction......Page 390
 10.2 Sensory Analysis......Page 391
 10.3 Origin of Flavors in Whey......Page 392
 10.4 Fluid Milk......Page 395
  10.5.1 Liquid Whey......Page 396
  10.5.3 Cheese Type and Influence of Culture on Whey Flavor......Page 398
  10.7.1 Whey Protein Concentrates and Isolates......Page 401
 10.8 Serum Protein......Page 404
 10.9 Hydrolysates......Page 405
  10.10.1 Impact of Bleaching on Whey......Page 406
  10.10.2 General Bleaching......Page 407
  10.10.3 Chemical Bleaching......Page 408
  10.10.4 Enzymatic Bleaching......Page 409
 10.11 Storage......Page 410
 10.12 Spray Drying and Dry Storage......Page 411
 References......Page 413
 11.1 Introduction......Page 420
  11.2.1 Protein Structure Related Properties and Preconditions for Film Forming......Page 421
  11.2.2 General Steps for Film Formation......Page 422
  11.3.1 Wet Coating......Page 423
  11.3.2 Extrusion......Page 425
  11.4.1 Physical Modifications......Page 426
  11.4.2 Chemical Modifications......Page 428
  11.4.3 Biochemical Modifications......Page 429
  11.4.4 Film Modifications: Blends and Composites......Page 430
  11.5.1 Barrier Properties......Page 431
   11.5.1.2 Oxygen Permeability......Page 432
  11.5.2 Mechanical Properties......Page 433
  11.5.3 Surface Properties......Page 434
  11.6.1 Packaging Requirements of Food Products......Page 435
  11.6.2 Merging Food Packaging Requirements and Properties of Whey Protein-Based Films and Coatings......Page 437
 11.7 Food Safety and Regulatory Aspect......Page 438
  11.8.1 Biodegradation of Whey Protein-Based Films and Laminates......Page 439
  11.8.2 Recyclability of Whey Protein-Based Multilayer Laminates......Page 440
 11.9 Conclusions and Industrial Perspectives......Page 442
 References......Page 443
 12.1 Introduction......Page 451
  12.2.1 Whey-Based Infant Formula......Page 454
   12.2.2.1 α-Lactalbumin......Page 458
   12.2.2.2 β-Lactoglobulin......Page 460
   12.2.2.3 Immunoglobulins......Page 461
   12.2.2.4 Glycomacropeptide......Page 462
   12.2.3.1 Lactoferrin......Page 463
   12.2.3.2 Osteopontin......Page 465
   12.2.3.4 Folate Binding Protein......Page 467
   12.2.3.6 Growth Factors......Page 469
   12.2.3.7 Cytokines......Page 470
   12.2.4.2 Oligosaccharides......Page 471
  12.3.1 Development of Whey Protein Ingredients for Infant Formula......Page 472
  12.3.2 Formulation Dynamics......Page 476
  12.3.3 Whey Protein−Casein Interactions in Infant Formula......Page 477
  12.4.1 Whey Proteins and In-Process Emulsion Stability......Page 478
  12.4.2 Thermal Stability of Infant Formula Containing Whey Proteins......Page 482
  12.4.4 Behavior of Whey Proteins During Concentration of Infant Formula Emulsions......Page 484
 12.5 Conclusion......Page 488
 References......Page 489
  13.1.1 Health Benefits of High-Protein Diets......Page 507
  13.1.2 Formulation of High-Protein Nutrition Bars......Page 508
   13.2.1.1 Sensory Properties of High-Protein Nutrition Bars......Page 509
   13.2.1.2 Texture of High-Protein Nutrition Bars......Page 510
   13.2.1.4 Texture Hardening of High-Protein Nutrition Bars......Page 512
    13.2.1.4.1 Moisture Migration......Page 513
    13.2.1.4.2 Protein Aggregation......Page 514
    13.2.1.5.1 Color Changes......Page 517
    13.2.1.5.2 Nutrition Loss......Page 519
  13.3.1 Inhibition of Disulfide Bond Formation......Page 520
  13.3.2 Adding Protein Hydrolysates......Page 521
   13.3.3.1 Extrude and Toast......Page 522
   13.3.3.2 Jet-Milling......Page 523
   13.3.3.3 Superfine Grinding......Page 524
   13.3.3.4 Protein Cross-Linking by Transglutaminase......Page 525
 References......Page 526
 14.1 Introduction......Page 530
 14.2 Bioactive Peptides Derived From Whey Proteins......Page 532
  14.2.1 Antihypertensive Peptides......Page 534
  14.2.2 Antioxidant Peptides......Page 536
  14.2.3 Antidiabetic Peptides......Page 538
  14.2.4 Mineral-Binding Peptides......Page 539
  14.2.6 Opioid Peptides......Page 542
  14.2.7 Immunomodulatory Peptides......Page 543
  14.2.8 Cytomodulatory Peptides......Page 544
  14.3.1 Enzymatic Hydrolysis......Page 545
  14.3.2 Microbial Fermentation......Page 546
 14.4 Glycomacropeptide......Page 547
  14.4.1 Isolation of Glycomacropeptide From Whey......Page 548
 References......Page 549
 15.1 Introduction......Page 559
 15.3 Whey Protein: A Potential Role in Helping to Reduce Undernutrition......Page 560
  15.3.2 Why Linear Growth Is Important, and How Whey Proteins Contribute to This Effect......Page 564
  15.3.3 Whey Protein, Weight Gain and Lean Body Mass......Page 566
  15.4.1 Higher Protein Diets and Weight Loss......Page 568
  15.4.2 Whey Protein and Optimal Body Composition......Page 570
  15.4.3 The Double Burden of Malnutrition......Page 572
  15.5.2 Diabetes......Page 573
  15.6.1 Sarcopenia and Its Economic Impact......Page 574
  15.6.3 Whey Protein Supplementation and Sarcopenia in the Elderly......Page 575
  15.6.4 Hypotheses About the Mechanism of Action of Whey Protein Intake on Sarcopenia......Page 577
 15.7 Conclusion......Page 579
 References......Page 580
 16.1 Introduction......Page 588
  16.2.1 Dairy (Milk) Proteins: Caseins and Whey Proteins......Page 589
 16.3 Types of Whey Protein Products......Page 590
  16.3.1 Amino Acid Composition of Whey Proteins......Page 591
  16.3.2 Meals Versus Supplements......Page 592
  16.4.1 Resistance Exercise......Page 593
   16.4.1.1 Strength Performance and Muscle Mass......Page 594
   16.4.1.2 Recovery From Resistance Exercise......Page 601
   16.4.1.3 Body Composition and Weight Loss......Page 602
   16.4.2.1 Endurance Capacity and Performance......Page 603
   16.4.2.2 Muscle Protein Synthesis Following Endurance Exercise......Page 604
  16.4.3 Multiple-Sprint Sports......Page 605
  16.5.1 Resistance Exercise and Training......Page 606
  16.5.2 Endurance Exercise and Training......Page 608
  16.6.2 Older Age Adults......Page 609
  16.6.3 Female Exercisers......Page 611
  16.6.4 Children and Adolescents......Page 612
 16.7 Dose-Response......Page 613
   16.8.1.2 Endurance Exercise......Page 614
  16.8.2 Caffeine......Page 616
  16.8.3 Creatine......Page 617
  16.8.4 Vitamin D......Page 618
  16.9.1 Insulin Signaling and Glycogen Synthesis......Page 619
  16.9.2 Increase Muscle Mass......Page 620
  16.9.3 Repair of Muscle......Page 622
  16.9.5 Gene Expression......Page 623
  16.9.7 Immune Function......Page 624
   16.9.7.3 Antioxidant Effects......Page 626
  16.10.1 Energy Balance......Page 627
  16.10.2 Lactose Intolerance, Allergies, Dairy-Free Diets......Page 628
 16.11 Limitations of Research and Future Directions......Page 629
 16.12 Conclusions......Page 631
 References......Page 633
 17.1 Introduction......Page 645
  17.2.1 β-Lactoglobulin......Page 647
  17.2.2 α-Lactalbumin......Page 650
  17.2.5 Glycomacropeptide......Page 651
  17.2.6 Lactoferrin......Page 653
  17.2.7 Lactoperoxidase......Page 654
  17.3.1 Cancer......Page 655
  17.3.2 Immune Health......Page 656
  17.3.3 Weight Management......Page 657
  17.3.4 Osteoporosis......Page 658
 17.5 Conclusions......Page 659
 References......Page 666
Author Index......Page 672
Subject Index......Page 699