Nutraceutical Proteins and Peptides in Health and Disease (Nutraceutical Science and Technology Book 4)

Reports of the beneficial health effects of some peptides have begun to make their way into the scientific literature. Peptides can act as immunomodulators, and have been shown to have a positive influence on calcium absorption, and on regulation of serum cholesterol. A number of peptides may also possess antimicrobial properties that enhance the body's defense mechanisms, and others may produce inhibitory effects for angiotensin-I-converting enzyme (ACE), leading to novel treatments for blood pressure conditions, heart failure, and diabetes. Modern food biotechnology may also allow for the production of highly important products for those suffering life-altering food allergies. A compendium of cutting-edge information for research scientists and clinicians Nutraceutical Proteins and Peptides in Health and Disease is the first book that provides comprehensive discussions on bioactive proteins and peptides in the area of nutraceutical and functional foods. It looks at protein and peptide impact on the body's absorption, defense, regulating, and nervous systems, then delves into hypo-allergenic foods and modern approaches to nutraceutical research and production. With 32 chapters written by 63 scientists working at the frontier of this revolutionizing field, it includes state-of-the-art information on— The cholesterol-lowering capabilities of proteins and peptides Opioid-like peptides The antibodies found in milk and egg yolks Enzymes derived from traditional Asian fermented foods found useful in novel thrombolytic therapy ACE-inhibitory peptides Enzymatic treatments used to create anti-allergenic food Recent developments in proteomics that are making certain processes economically feasible, including those employed in the binding of bioactive peptides Nutraceutical Proteins and Peptides in Health and Disease provides a compendium of cutting-edge information that can be put to direct use in research, therapy, and production. Biochemists, nutritional scientists, food scientists, and health professionals, as well as graduate students in these fields, will find this book highly useful. DK2148fm.pdf......Page 1 Nutraceutical Proteins and Peptides in Health and Disease......Page 3 Preface......Page 5 Editors......Page 6 Contributors......Page 8 Table of Contents......Page 13 Section I: Nutrient Absorption System......Page 17 Table of Contents......Page 0 CONTENTS......Page 18 1.2 THE BODY’S DEFENSE SYSTEM......Page 19 1.4 THE BODY’S NERVOUS SYSTEM......Page 20 1.5 HYPOALLERGENIC FOODS......Page 21 1.6 MODERN APPROACHES TO BIOACTIVE PROTEINS AND PEPTIDES......Page 22 REFERENCES......Page 23 2.1 INTRODUCTION......Page 25 2.2 SOURCES OF CALCIUM-BINDING PEPTIDES FROM MILK PROTEINS......Page 27 2.3 PHYSICOCHEMICAL PROPERTIES OF CPP......Page 30 2.4.1 BIOAVAILABILITY OF MINERALS......Page 32 2.4.2 CPP AND BONE HEALTH......Page 33 2.5 OTHER POTENTIAL APPLICATIONS FOR CPP......Page 34 2.6 CONCLUSIONS......Page 35 REFERENCES......Page 36 3.1 INTRODUCTION......Page 42 3.2.2 PEPTIDES......Page 43 3.3.1 CALCIUM......Page 44 3.3.3 IRON......Page 45 3.5 ROLES OF CPP......Page 46 3.5.2 ZINC......Page 47 REFERENCES......Page 48 CONTENTS......Page 54 4.2.1 SERUM CHOLESTEROL AND BOVINE MILK WHEY PROTEIN......Page 55 4.2.2 THE HYPOCHOLESTEROLEMIC ACTION OF MAJOR CONSTITUENTS OF BOVINE MILK WHEY PROTEIN......Page 56 4.2.3 THE HYPOCHOLESTEROLEMIC ACTION OF BOVINE MILK WHEY PROTEIN, ITS MAJOR CONSTITUENT PROTEIN beta-LACTOGLOBULIN, AND ITS TRYPTIC HYDROLYSATE......Page 57 4.2.4 IDENTIFICATION OF NOVEL HYPOCHOLESTEROLEMIC PEPTIDES DERIVED FROM BOVINE MILK beta-LACTOGLOBULIN......Page 60 4.3.1 EGG WHITE PROTEIN AND CHOLESTEROL METABOLISM......Page 64 4.3.2 OVOMUCIN AND SERUM CHOLESTEROL......Page 65 4.5 CHOLESTEROL-LOWERING FISH PROTEINS......Page 67 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)......Page 68 4.8.4 SOY ISOFLAVONOIDS CHOLESTEROL METABOLISM......Page 70 4.8.5 THE HEALTH CLAIM AND INDUSTRIAL UTILIZATION OF SOY PROTEIN AND PEPTIDES......Page 71 REFERENCES......Page 74 5.1 INTRODUCTION......Page 81 5.2.1 METALLOTHIONEINS AND PHYTOCHELATINS......Page 82 5.3 PHYSIOLOGICAL FUNCTION OF METAL-BINDING PROTEINS AND PEPTIDES......Page 83 5.4 ISOLATION OF METAL-BINDING PROTEINS AND PEPTIDES......Page 84 5.5.1 IMPLICATIONS IN HUMAN HEALTH AND DISEASE......Page 85 5.5.2 NUTRITIONAL SUPPLEMENTATION......Page 86 5.6 GENETIC ENGINEERING TO MODIFY METAL-BINDING AND SEQUESTERING CHARACTERISTICS......Page 87 REFERENCES......Page 88 6.1 MAJOR MECHANISMS FOR INTESTINAL ABSORPTION......Page 93 6.2 STRUCTURE OF THE TIGHT JUNCTION......Page 95 6.3 INTRACELLULAR SIGNALING PATHWAY MODULATING THE TIGHT-JUNCTION PERMEABILITY......Page 96 6.4 REGULATION OF TIGHT-JUNCTION PERMEABILITY BY INTERNAL FACTORS......Page 98 6.5 DIETARY SUBSTANCES THAT MODULATE PARACELLULAR PERMEABILITY......Page 101 REFERENCES......Page 104 Section II: The Body’s Defense System......Page 108 CONTENTS......Page 109 7.2.1.1 Mammalian Defensins......Page 110 7.2.2.1 Plant Defensins......Page 111 7.2.2.2 Lipid Transfer Proteins......Page 113 7.2.3 MARINE SOURCES......Page 115 7.2.3.1 Antimicrobial Peptides from Fishes......Page 116 7.2.3.2 Antimicrobial Peptides from Crustaceans......Page 117 7.2.3.3 Antimicrobial Peptides from Molluscs......Page 120 7.2.4.1 Dairy Proteins......Page 121 7.2.4.2 Egg Proteins......Page 122 7.2.5 BACTERIOCIN: ANTIMICROBIAL PEPTIDES PRODUCED BY BACTERIA......Page 123 7.3 MODES OF ANTIMICROBIAL ACTIONS......Page 124 7.3.1 MEMBRANE INTERACTION......Page 125 7.3.2 MEMBRANE PENETRATION......Page 126 7.4 ROLES OF ANTIMICROBIAL PEPTIDES IN THE IMMUNE SYSTEM......Page 127 7.5.2 THE USE OF ANTIMICROBIAL PEPTIDES IN FOODS......Page 129 7.5.3 THE USE OF ANTIMICROBIAL PEPTIDES FOR CLINICAL APPLICATIONS......Page 130 REFERENCES......Page 131 8.1 INTRODUCTION......Page 147 8.2 BIOCHEMICAL CHARACTERISTICS OF BOVINE IMMUNOGLOBULINS......Page 148 8.3 TECHNOLOGICAL PROPERTIES OF BOVINE IMMUNOGLOBULINS......Page 149 8.4 DIGESTION OF ANTIBODIES......Page 150 8.5 FUNCTIONS AND ACTIVITIES OF BOVINE MILK ANTIBODIES......Page 151 8.5.1 INHIBITION OF ENZYME ACTIVITY......Page 152 8.5.2 PREVENTION OF ADHESION......Page 153 8.5.2.1 Caries Streptococci......Page 154 8.5.2.3 Helicobacter......Page 155 8.5.2.5 Shigella......Page 156 8.5.3 NEUTRALIZATION OF TOXINS......Page 157 8.5.4 NEUTRALIZATION OF VIRUSES......Page 158 8.5.5 OPSONIZATION......Page 159 8.6 SYNERGISTIC EFFECTS OF MILK ANTIBODIES WITH OTHER ANTIMICROBIAL FACTORS......Page 161 8.7 HOW CAN BOVINE MILK ANTIBODIES BENEFIT HUMAN HEALTH IN THE FUTURE......Page 162 REFERENCES......Page 164 9.1 INTRODUCTION......Page 170 9.2.2 ADVANTAGES OF EGGS AS AN ANTIBODY SOURCE......Page 171 9.2.3 PRODUCTION AND PURIFICATION OF IGY......Page 173 9.3 STRUCTURE AND IMMUNOCHEMICAL PROPERTIES OF IGY......Page 174 9.4.1 HEAT AND PH STABILITY......Page 175 9.5.1.1 Oral Administration of IgY......Page 177 9.5.1.1.2 Salmonella spp.......Page 178 9.5.1.1.3 Rotavirus......Page 181 9.5.1.1.5. Helicobacter pylori......Page 182 9.5.1.1.7 Inflammatory bowel disease......Page 183 9.5.1.2.1 Neutralization of venom......Page 184 9.5.2.1 Diagnostic Applications......Page 185 9.5.2.2 Immunoaffinity Ligands......Page 186 9.6 FUTURE APPLICATIONS OF IGY......Page 187 REFERENCES......Page 188 CONTENTS......Page 199 10.1 INTRODUCTION......Page 200 10.2 CLINICAL SIGNIFICANCE AND CLINICAL TRIALS......Page 201 10.3 SCREENING ANTIANGIOGENIC COMPOUNDS......Page 204 10.3.1.1.2 The Cornea Assay......Page 206 10.3.1.2 In vivo Matrigel Plug Assay......Page 207 10.3.1.3 The Zebrafish......Page 208 10.4.2 COLLAGEN......Page 210 10.4.4 BOWMAN-BIRK INHIBITOR......Page 211 10.4.6 LACTOFERRIN......Page 212 10.4.8 BILIPROTEINS......Page 213 10.5.3 GLYCINE......Page 214 10.6 CHALLENGES TO ANTIANGIOGENIC PROTEIN, PEPTIDE, AND AMINO ACID FUNCTIONAL FOODS......Page 215 10.7 BIOAVAILABILITY AND SYNERGY OF ANTIANGIOGENIC POLYPEPTIDE AND AMINO-ACID FUNCTIONAL FOODS......Page 216 10.9 CONCLUSIONS......Page 217 REFERENCES......Page 218 CONTENTS......Page 224 11.1 INTRODUCTION......Page 225 11.2 WHAT ARE GROWTH FACTORS?......Page 226 11.2.2 HORMONES......Page 227 11.2.4.1 Mucosal Integrity Peptides......Page 228 11.2.4.2 Luminal Surveillance Peptides......Page 230 11.3.2 INSULIN-LIKE GROWTH FACTORS (IGF, SOMATOMEDINS) AND THEIR BINDING PROTEINS......Page 231 11.3.3 PLATELET-DERIVED GROWTH FACTOR (PDGF)......Page 232 11.3.6 BASIC FIBROBLAST GROWTH FACTOR (BFGF)......Page 233 11.4.1 NATURAL PRODUCTS......Page 234 11.4.2 PARTLY PURIFIED NATURAL PRODUCTS......Page 235 11.4.4 SYNTHETICALLY PRODUCED COMPOUNDS BASED ON NATURAL PRODUCTS......Page 236 11.5.1 SHORT BOWEL SYNDROME......Page 237 11.5.2 NONSTEROIDAL ANTIINFLAMMATORY DRUG (NSAID)-INDUCED GUT INJURY......Page 238 11.5.5 NECROTIZING ENTEROCOLITIS......Page 239 11.6.2 PROMOTING ANGIOGENESIS IN ISCHEMIC DISEASE......Page 240 11.8 SUMMARY......Page 241 REFERENCES......Page 242 12.1 INTRODUCTION......Page 249 12.2 FORMATION OF THE CYSTATIN SUPERFAMILY......Page 250 12.3.1 APPLICATION OF GENETICALLY GLYCOSYLATED CYSTATIN TO SURIMI MANUFACTURING......Page 255 12.3.2 ANTI-SALMONELLA AND ANTI-ROTAVIRUS EFFECTS OF GENETICALLY GLYCOSYLATED CYSTATIN......Page 258 12.3.3 ANTICANCER EFFECTS OF DOUBLE-MUTATED CYSTATIN......Page 260 12.4 HIGH-LEVEL PRODUCTION FOR FURTHER APPLICATIONS......Page 262 12.5 CONCLUSIONS......Page 264 REFERENCES......Page 265 Section III: The Body’s Regulating System......Page 273 13.1 INTRODUCTION......Page 274 13.2 FOOD-PROTEIN-DERIVED ACE-INHIBITORY PEPTIDES......Page 275 13.3 STRUCTURAL FEATURES OF ACE INHIBITION......Page 284 13.4 PHENOMENON OF MULTIFUNCTIONALITY OF MILK-PROTEIN-DERIVED ACE INHIBITORS......Page 287 13.5 PROTEOLYTIC ACTIVATION OF ENCRYPTED ACE-INHIBITORY PEPTIDES......Page 289 13.6.1 THE RENIN–ANGIOTENSIN SYSTEM (RAS)......Page 300 13.6.4 THE NEUTRAL ENDOPEPTIDASE SYSTEM (NEPS)......Page 302 13.7.1 ANIMAL STUDIES......Page 303 13.8 CONSUMER ASPECTS......Page 304 13.9 POTENTIAL APPLICATIONS......Page 309 REFERENCES......Page 310 14.1 INTRODUCTION......Page 321 14.2 BONE METABOLISM......Page 322 14.4.1 MBP......Page 324 14.4.2 KININOGEN FRAGMENT 1.2......Page 325 14.4.3 HMG-LIKE PROTEIN......Page 326 14.5.1 MBP......Page 327 14.6 TRANSPORT ABILITY OF THE ACTIVE COMPONENTS BY THE SMALL INTESTINE......Page 328 14.7.1 YOUNG OVX RATS......Page 329 14.7.2 GROWING RATS......Page 330 14.7.3 AGED OVX RATS......Page 331 14.8.1 HUMAN STUDY 1......Page 332 14.8.2 HUMAN STUDY 2......Page 334 14.9 CONCLUSIONS......Page 335 REFERENCES......Page 336 15.1 INTRODUCTION – DENTAL CARIES......Page 339 15.2 ANTICARIOGENIC FOOD GROUPS......Page 340 15.3 ANTICARIOGENIC CASEIN PHOSPHOPEPTIDES......Page 341 15.3.2 ANTICARIOGENICITY OF CPP–ACP IN THE RAT......Page 342 15.3.3 IN VITRO REMINERALIZATION OF ENAMEL LESIONS BY CPP–ACP......Page 343 15.3.4 ANTICARIOGENICITY OF CPP–ACP IN HUMAN IN SITU STUDIES......Page 344 15.3.5 INTERACTION OF CPP–ACP WITH FLUORIDE......Page 346 15.5 STRUCTURE OF THE ANTICARIOGENIC CPP......Page 348 15.6 CONCLUSIONS......Page 352 REFERENCES......Page 353 15.1 INTRODUCTION – DENTAL CARIES......Page 356 15.2 ANTICARIOGENIC FOOD GROUPS......Page 357 15.3 ANTICARIOGENIC CASEIN PHOSPHOPEPTIDES......Page 358 15.3.2 ANTICARIOGENICITY OF CPP–ACP IN THE RAT......Page 359 15.3.3 IN VITRO REMINERALIZATION OF ENAMEL LESIONS BY CPP–ACP......Page 360 15.3.4 ANTICARIOGENICITY OF CPP–ACP IN HUMAN IN SITU STUDIES......Page 361 15.3.5 INTERACTION OF CPP–ACP WITH FLUORIDE......Page 363 15.5 STRUCTURE OF THE ANTICARIOGENIC CPP......Page 365 15.6 CONCLUSIONS......Page 369 REFERENCES......Page 370 16.1 INTRODUCTION – CARDIOVASCULAR DISEASE......Page 373 16.2 FUNCTIONAL FOODS......Page 378 16.4 FIBRINOLYTIC ENZYMES......Page 379 16.4.1 NON-FOOD SOURCES......Page 380 16.4.2 FOOD SOURCES......Page 381 REFERENCES......Page 382 Section IV: The Body’s Nervous System......Page 385 17.1.1 THE MAMMALIAN OPIOIDERGIC SYSTEM: OPIOID RECEPTORS AND ENDOGENOUS LIGANDS......Page 386 17.1.2 EXOGENOUS OPIOID AGONISTS AND ANTAGONISTS......Page 388 17.1.3 FUNCTIONAL SIGNIFICANCE OF NUTRACEUTICAL OPIOID PEPTIDES......Page 391 REFERENCES......Page 392 18.1 INTRODUCTION......Page 396 18.2 PSYCHOLOGICAL RELAXATION EFFECTS......Page 397 18.3.1 RELAXATION EFFECT IN PMS......Page 400 18.3.2. ANTAGONISTIC EFFECT AGAINST CAFFEINE......Page 401 18.3.3 LOWERING BLOOD PRESSURE......Page 404 18.4 ABSORPTION AND METABOLISM OF L-THEANINE......Page 406 18.5 APPLICATIONS OF SUNTHEANINE®......Page 407 REFERENCES......Page 408 Section V: Hypoallergenic Foods......Page 410 19.1 INTRODUCTION......Page 411 19.2.1 MECHANISM......Page 412 19.2.2 SYMPTOMS......Page 414 19.2.3 PREVALENCE......Page 415 19.2.5 COMMONLY ALLERGENIC FOODS......Page 416 19.2.7 DIAGNOSIS......Page 417 19.2.8 TREATMENT......Page 418 19.2.9 PREVENTION......Page 419 19.3 DELAYED HYPERSENSITIVITY (CELIAC DISEASE EXAMPLE)......Page 420 19.3.3 CAUSATIVE FACTOR......Page 421 REFERENCES......Page 422 CONTENTS......Page 429 20.2.1 CELIAC DISEASE......Page 430 20.2.3 ATOPIC DERMATITIS......Page 431 20.3.1.1 An Allergenic Peptide from Low-Molecular-Weight Glutenin......Page 432 20.3.1.2 Gln-Gln-Gln-Pro-Pro as an IgE-binding Epitope......Page 433 20.3.2 ALBUMIN/GLOBULIN FRACTIONS, ESPECIALLY GLYCOPROTEINS......Page 434 20.3.3 MANNOGLUCAN......Page 436 20.4.1 ENZYMATIC TREATMENT OF WHEAT FLOUR TO PRODUCE HYPOALLERGENIC FLOUR (HWF)......Page 437 20.4.3 CLINICAL EVALUATION OF HWF......Page 439 20.5 PREVENTIVE AND SUPPRESSIVE EFFECTS OF HWF ON FOOD ALLERGY......Page 440 20.5.2 INDUCTION OF ORAL TOLERANCE BY HWF......Page 441 REFERENCES......Page 443 21.1 INTRODUCTION......Page 448 21.2 CURRENTLY AVAILABLE HYPOALLERGENIC FORMULAS......Page 449 21.2.1.1 Soy Protein-Based Formulas......Page 450 21.2.2.1 Heat Denaturation......Page 451 21.3 APPROACHES TO ANTIALLERGIC FOODS CONTAINING MILK PROTEINS......Page 452 21.3.1 GENETIC MODIFICATION OF MILK PROTEINS......Page 453 21.3.3 PROBIOTICS......Page 455 REFERENCES......Page 456 22.1 INTRODUCTION......Page 462 22.2.1 MAJOR EGG WHITE ALLERGENS......Page 463 22.2.2 OVOMUCOID......Page 464 22.2.3 OVALBUMIN......Page 465 22.2.5 LYSOZYME......Page 467 22.3 PROCESSING OF EGGS AND ITS VALUE-ADDED HYPOALLERGENIC APPLICATION......Page 468 22.3.1 HEAT DENATURATION AND ENZYMATIC DIGESTIONS......Page 469 22.3.2 SUPPRESSION OF ALLERGIC POTENTIAL OF EGG WHITE BY GENETIC MODIFICATION......Page 470 REFERENCES......Page 471 23.1 INTRODUCTION......Page 477 23.2.1 GLY M BD 30K......Page 479 23.2.2 GLY M BD 28K......Page 480 23.2.4 OTHER ALLERGENIC PROTEINS......Page 482 23.3.2 MOLECULAR BREEDING......Page 484 23.3.3 REDUCTION OF GLY M BD 30K BY GENETIC MODIFICATION......Page 485 23.3.4 PHYSICOCHEMICAL REDUCTION......Page 486 23.3.5 ENZYMATIC DIGESTION......Page 488 23.3.6 CHEMICAL MODIFICATION......Page 490 23.4 EVALUATION OF HYPOALLERGENIC SOYBEAN PRODUCTS AND PERSPECTIVES......Page 491 REFERENCES......Page 492 24.1 INTRODUCTION......Page 496 24.2 BEEF ALLERGY AND ITS ALLERGENS......Page 497 24.3 PORK ALLERGY AND ITS ALLERGENS......Page 499 24.4 CHICKEN ALLERGY AND ITS ALLERGENS......Page 500 24.5 SERUM ALBUMIN AS A CROSS-REACTING MEAT ALLERGEN......Page 501 24.6.1 HEAT TREATMENT......Page 502 24.6.3 OTHER TREATMENTS......Page 503 REFERENCES......Page 504 25.1 INTRODUCTION – ADVERSE ALLERGENIC REACTIONS TO RICE......Page 507 25.2.1 RICE-SEED PROTEINS AND THEIR ALLERGENIC POTENTIALS......Page 508 25.2.2.1 Allergens with MW of ~14- to ~16-kDa......Page 511 25.2.2.2 Allergens with MW of 26-kDa......Page 514 25.2.2.3 Allergens with MW of 33-kDa......Page 515 25.3.1 DEGRADATION AND REMOVAL BY ENZYMATIC HYDROLYSIS......Page 516 25.3.2 RELEASE AND REMOVAL BY HIGH HYDROSTATIC PRESSURE......Page 519 25.3.3 SUPPRESSION OF BIOSYNTHESIS BY GENETIC MODIFICATION......Page 520 REFERENCES......Page 522 26.1 INTRODUCTION......Page 526 26.2 GENERAL CHEMICAL AND NUTRITIONAL PROPERTIES OF BUCKWHEAT SEEDS......Page 527 26.3 USES OF BUCKWHEAT......Page 528 26.4 ADVERSE EFFECTS OF BUCKWHEAT......Page 530 26.5 PATHOGENETIC MECHANISM OF BUCKWHEAT ALLERGY......Page 531 26.6 PREVALENCE OF BUCKWHEAT ALLERGY......Page 532 26.7 ALLERGIC REACTION AND SYMPTOMS......Page 535 26.8 OCCUPATIONAL LUNG DISEASE......Page 539 26.10 ALLERGEN CHARACTERIZATION......Page 541 26.11 CROSS ALLERGENICITY......Page 543 26.12 DIAGNOSIS OF BUCKWHEAT ALLERGY......Page 545 26.13 TREATMENT AND PREVENTION......Page 547 REFERENCES......Page 550 Section VI: Modern Approaches to Bioactive Proteins and Peptides......Page 554 27.1 INTRODUCTION......Page 555 27.2.2 CATH......Page 557 27.2.4 PROSITE......Page 558 27.2.6 SCOP — A DATABASE OF STRUCTURAL CLASSIFICATION OF PROTEINS......Page 559 27.2.8 HOMOLOGY AND PREDICT 7......Page 560 27.3.1 DATABASE DESCRIPTION......Page 561 27.3.2 NEW CRITERIA OF PROTEIN EVALUATION IN BIOPEP......Page 562 27.3.3 ANALYSIS OF PROTEIN IN BIOPEP ACCORDING TO THE NEW CRITERIA......Page 563 27.3.4 PROTEOLYTIC PROCESS DESIGN IN BIOPEP......Page 570 REFERENCES......Page 572 28.1 INTRODUCTION......Page 576 28.2 QSAR......Page 578 28.3 FUNCTIONAL SEQUENCE ANALYSIS......Page 580 28.4 OPTIMIZATION......Page 588 28.5 RATIONAL DESIGNING STRATEGY......Page 589 REFERENCES......Page 591 29.1 INTRODUCTION......Page 594 29.2 HYPERGLYCOSYLATION OF LYSOZYME BY GENETIC ENGINEERING......Page 595 29.3 HEAT STABILITY OF OLIGOMANNOSYL AND POLYMANNOSYL LYSOZYMES......Page 599 29.4 EMULSIFYING PROPERTY OF OLIGOMANNOSYL AND POLYMANNOSYL LYSOZYMES......Page 602 29.5 MODIFICATION OF ANTIMICROBIAL ACTION OF LYSOZYME......Page 603 29.5.1 REDUCTION OF ANTIGENIC STRUCTURE OF LYSOZYME BY GENETIC MODIFICATIONS......Page 605 29.5.2 AMYLOIDOGENIC MUTANT LYSOZYMES......Page 608 29.5.3 QUALITY CONTROL OF ABNORMAL PROTEINS BY MOLECULAR CHAPERONES......Page 609 REFERENCES......Page 612 30.1 INTRODUCTION......Page 614 30.2 NEW LIQUID-PHASE PEPEPTIDE SYNTHESIS (LPPS) METHOD BASED ON THERMOMORPHIC BIPHASIC ORGANIC SOLUTIONS......Page 615 30.3 ELECTROLYTIC CYCLIZATION OF DIPEPTIDES INVOLVING PROLINE-MOIETY FOR CONSTRUCTION OF CONFORMATION-CONSTRAINED PEPTIDOMIMETICS......Page 622 REFERENCES......Page 627 31.1 INTRODUCTION......Page 630 31.2.1 INHIBITION OF NONSTARTER LACTIC BACTERIA AND THE REGULATION OF FLAVOR AND QUALITY IN CHEESE......Page 632 31.2.2 INHIBITION OF PATHOGENS IN FOOD......Page 634 31.2.3 MASTITIS PREVENTION IN CATTLE......Page 636 31.2.4 TOLERANCE, RESISTANCE, AND IMMUNITY......Page 637 31.3 MOLECULAR ANALYSIS OF LACTICIN 3147 PRODUCTION AND IMMUNITY......Page 639 31.4 DISCUSSION......Page 642 REFERENCES......Page 644 CONTENTS......Page 649 32.2.1 SEPARATION DOMAINS......Page 650 32.2.2 TANGENTIAL FILTRATION......Page 651 32.3.1 BACKGROUND DATA......Page 653 32.3.2 OVERVIEW OF THE OPTIONS......Page 654 32.3.3.1 Adsorbents......Page 655 32.3.3.3 Solvent Precipitation......Page 656 32.3.4 MEMBRANE-BASED SEPARATION......Page 657 32.3.5.1.2 Hydrophobic Interaction Chromatography......Page 659 32.3.5.1.4 Affinity Chromatography......Page 660 32.3.5.2.2 Isoelectric Focusing......Page 661 32.4.2 PRODUCTION OF LACTOFERRICIN......Page 662 32.4.3 RECOVERY OF NISIN FROM FERMENTATION BROTHS......Page 663 32.5 CONCLUSIONS......Page 664 REFERENCES......Page 665 "Reports of the beneficial health effects of some peptides have begun to make their way into the scientific literature. Peptides can act as immunomodulators, and have been shown to have a positive influence on calcium absorption, and on regulation of serum cholesterol. A number of peptides may also possess antimicrobial properties that enhance the body's defense mechanisms, and others may produce inhibitory effects for angiotensin-I-converting enzyme (ACE), leading to novel treatments for blood pressure conditions, heart failure, and diabetes. Modern food biotechnology may also allow for the production of highly important products for those suffering life-altering food allergies. A compendium of cutting-edge information for research scientists and clinicians Nutraceutical Proteins and Peptides in Health and Disease is the first book that provides comprehensive discussions on bioactive proteins and peptides in the area of nutraceutical and functional foods. It looks at protein and peptide impact on the body's absorption, defense, regulating, and nervous systems, then delves into hypo-allergenic foods and modern approaches to nutraceutical research and production. With 32 chapters written by 63 scientists working at the frontier of this revolutionizing field, it includes state-of-the-art information on-- The cholesterol-lowering capabilities of proteins and peptides Opioid-like peptides The antibodies found in milk and egg yolks Enzymes derived from traditional Asian fermented foods found useful in novel thrombolytic therapy ACE-inhibitory peptides Enzymatic treatments used to create anti-allergenic food Recent developments in proteomics that are making certain processes economically feasible, including those employed in the binding of bioactive peptides Nutraceutical Proteins and Peptides in Health and Disease provides a compendium of cutting-edge information that can be put to direct use in research, therapy, and production. Biochemists, nutritional scientists, food scientists, and health professionals, as well as graduate students in these fields, will find this book highly useful."--Publisher's website Nutraceutical Proteins and Peptides in Health and Disease is the first book to provide comprehensive discussions on bioactive proteins and peptides in the area of nutraceutical and functional foods. It looks at protein and peptide impact on the body's various systems, and also delves into hypo-allergenic foods and modern approaches to nutraceutical research and production. With 32 chapters written by 63 pioneering scientists, it provides a number of highly relevant findings that give evidence to: Peptides that can perform like opioids or as ACE inhibitors, Milk and egg yolks as a source of antibodies, Asian fermented foods that provide enzymes found useful in novel thrombolytic therapy, Enzymatic treatments used to create anti-allergenic food.This book also details recent developments in proteomics that are making certain processes economically feasible, including those employed in the binding of bioactive peptides. Biochemists, nutritional and food scientists, and health professionals will find that this work is thoughtfully organized to help guide present application as well as future exploration.