Advanced dairy chemistry volume 1a proteins basic aspects 4th edition

Advanced Dairy Chemistry Paul L.H McSweeney • Patrick F Fox Editors Advanced Dairy Chemistry Volume 1A: Proteins: Basic Aspects, 4th Edition Editors Paul L.H McSweeney University College Cork School of Food and Nutritional Sciences Cork, Ireland Patrick F Fox University College Cork School of Food and Nutritional Sciences Cork, Ireland ISBN 978-1-4614-4713-9 ISBN 978-1-4614-4714-6 (eBook) DOI 10.1007/978-1-4614-4714-6 Springer New York Heidelberg Dordrecht London Library of Congress Control Number: 2012951431 © Springer Science+Business Media New York 2013 This work is subject to copyright All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed Exempted from this legal reservation are brief excerpts in connection with reviews or scholarly analysis or material supplied specifically for the purpose of being entered and executed on a computer system, for exclusive use by the purchaser of the work Duplication of this publication or parts thereof is permitted only under the provisions of the Copyright Law of the Publisher’s location, in its current version, and permission for use must always be obtained from Springer Permissions for use may be obtained through RightsLink at the Copyright Clearance Center Violations are liable to prosecution under the respective Copyright Law The use of general descriptive names, registered names, trademarks, service marks, etc in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use While the advice and information in this book are believed to be true and accurate at the date of publication, neither the authors nor the editors nor the publisher can accept any legal responsibility for any errors or omissions that may be made The publisher makes no warranty, express or implied, with respect to the material contained herein Printed on acid-free paper Springer is part of Springer Science+Business Media (www.springer.com) Preface to the Fourth Edition Advanced Dairy Chemistry-1A: Proteins: Basic Aspects is the first volume of the fourth edition of the series on advanced topics in dairy chemistry, which started in 1982 with the publication of Developments in Dairy Chemistry The second and third editions of this work were published in 1992 and 2003, respectively This series of volumes is an authoritative treatise on dairy chemistry Like the earlier series, this work is intended for academics, researchers at universities and industry and senior students; each chapter is referenced extensively The chemistry and physico-chemical properties of milk proteins are perhaps the largest and most rapidly evolving area in dairy chemistry, and it has proved impossible to cover this topic at the desired depth in one volume Hence, coverage of dairy proteins in the fourth edition of Advanced Dairy Chemistry will be split between basic (this volume) and applied aspects (Volume 1B, forthcoming) All chapters in the third edition on basic aspects of dairy proteins have been retained but have been revised and expanded The chapters on the chemistry of the caseins (Chap 4), genetic polymorphism (Chap 15) and nutritional aspects of milk proteins (Chap 16) have been revised by new authors, and new chapters have been included on the evolution of the mammary gland (Chap 1) and on minor proteins and growth factors in milk (Chap 11) We wish to thank sincerely the 37 contributors (from countries) of the 16 chapters of this volume, whose co-operation made our task as editors a pleasure We wish to acknowledge the assistance given by our editor at Springer Science + Business Media, New York, Ms Susan Safren and Ms Rita Beck, assistant editor at Springer, for help in preparing the manuscript Cork, Ireland Paul L.H McSweeney Patrick F Fox v Preface to the Third Edition Advanced Dairy Chemistry—1: Proteins is the first volume of the third edition of the series on advanced topics in Dairy Chemistry, which started in 1982 with the publication of Developments in Dairy Chemistry This series of volumes is intended to be a coordinated and authoritative treatise on Dairy Chemistry In the decade since the second edition of this volume was published (1992), there have been considerable advances in the study of milk proteins, which are reflected in changes to this book All topics included in the second edition are retained in the current edition, which has been updated and considerably expanded from 18 to 29 chapters Owing to its size, the book is divided into two parts; Part A (Chapters 1–11) describes the more basic aspects of milk proteins while Part B (Chapters 12–29) reviews the more applied aspects Chapter 1, a new chapter, presents an overview of the milk protein system, especially from an historical viewpoint Chapters 2–5, 7–9, 15, and 16 are revisions of chapters in the second edition and cover analytical aspects, chemical and physiochemical properties, biosynthesis and genetic polymorphism of the principal milk proteins Non-bovine caseins are reviewed in Chapter Biological properties of milk proteins, which were covered in three chapters in the second edition, are now expanded to five chapters; a separate chapter, Chapter 10, is devoted to lactoferrin and Chapter 11, on indigenous enzymes in milk, has been restructured and expanded Nutritional aspects, allergenicity of milk proteins, and bioactive peptides are discussed in Chapters 12, 13, and 14, respectively Because of significant developments in the area in the last decade, Chapter 17 on genetic engineering of milk proteins has been included Various aspects of the stability of milk proteins are covered in Chapter 18 (enzymatic coagulation), Chapter 19 (heat-induced coagulation), Chapter 20 (age gelation of sterilized milk), Chapter 21 (ethanol stability), and Chapter 22 (acid coagulation, a new chapter) The book includes four chapters on the scientific aspects of protein-rich dairy products (milk powders, Chapter 23; ice cream, Chapter 24; cheese, Chapter 25; functional milk proteins, Chapter 26) and three chapters on technologically important properties of milk proteins (surface properties, vii viii Preface to the Third Edition Chapter 27; thermal denaturation aggregation, Chapter 28; hydration and viscosity, Chapter 29) Like its predecessors, this book is intended for academics, researchers at universities and industry, and senior students; each chapter is referenced extensively We wish to thank sincerely the 60 contributors to the 29 chapters of this volume, whose cooperation made our task as editors a pleasure The generous assistance of Ms Anne Cahalane is gratefully acknowledged Cork, Ireland P.F Fox Paul L.H Mcsweeney Preface to the Second Edition Considerable progress has been made on various aspects of milk proteins since Developments in Dairy Chemistry 1—Proteins was published in 1982 Advanced Dairy Chemistry can be regarded as the second edition of Development in Dairy Chemistry which has been updated and considerably expanded Many of the original chapters have been revised and updated, e.g ‘Association of Caseins and Casein Micelle Structure’, ‘Biosynthesis of Milk Proteins’, ‘Enzymatic Coagulation of Milk’, ‘Heat Stability of Milk’, ‘Age Gelation of Sterilized Milks’ and ‘Nutritional Aspects of Milk Proteins’ Chapter in Developments, i.e ‘Chemistry of Milk Proteins’, has been subdivided and extended to chapters: chemistry and physico-chemical properties of the caseins, b-lactoglobulin, a-lactalbumin and immunoglobulins New chapters have been added, including ‘Analytical Methods for Milk Proteins’, ‘Biologically Active Proteins and Peptides’, ‘Indigenous Enzymes in Milk’, ‘Genetic Polymorphism of Milk Proteins’, ‘Genetic Engineering of Milk Proteins’, ‘Ethanol Stability of Milk’ and ‘Significance of Proteins in Milk Powders’ A few subjects have been deleted or abbreviated; the three chapters on functional milk proteins in Developments have been abbreviated to one in view of the recently published 4th volume of Developments in Dairy Chemistry—4— Functional Milk Proteins Like its predecessor, the book is intended for lecturers, senior students and research personnel and each chapter is extensively referenced I would like to thank all the authors who contributed to the book and whose cooperation made my task a pleasure Cork, Ireland P.F Fox ix 534 Alkanhal, H.A., Al-Othman, A.A and Hewedi, F.M (2001) Changes in protein nutritional quality in fresh and recombined ultra high temperature treated milk during storage Int J Food Sci Nutr 52, 509–514 Badger, T.M., Ronis, M.J and 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defense mechanisms in naive rats Biosci Biotechnol Biochem 67, 577–583 Wang, Q., Allen, J.C and Swaisgood, H.E (1997) Binding of vitamin D and cholesterol to b-lactoglobulin J Dairy Sci 80, 1054–1059 Weinberg, E.D (2007) Antibiotic properties and applications of lactoferrin Curr Pharmaceut Des 13, 801–811 Willis, A., Beander, H.U., Steel, G and Valle, D (2008) PRODH variants and risk for schizophrenia Amino Acids 35, 673–679 Wu, G (2009) Amino acids: metabolism, functions, and nutrition Amino Acids 37, 1–17 Wu, G and Morris, S.M (1998) Arginine metabolism: nitric oxide and beyond Biochem J 336, 1–17 Wu, G., Bazer, F.W., Wallace, J.M and Spencer, T.E (2006) Intrauterine growth retardation: implications for the animal sciences J Anim Sci 84, 2316–2337 Young, V.R and Pellett, P.L (1990) Current concepts concerning indispensable amino acid needs in adult and their implications for international nutrition planning Food Nutr Bull 12, 289–300 Young, G.P., Taranto, T.M., Jonas, H.A., Cox, A.J., Hogg, A and Werther, G.A (1990) Insulin-like growth factors and the developing and mature rat small intestine: receptors and biological actions Digestion 46, 240–252 Yudkoff, M (1997) Brain metabolism of branched-chain amino acids GLIA 21, 92–98 Index A ACE See Angiotensin-converting enzyme (ACE) Acid phosphatase (AcP) assay methods, 360 isolation and characterisation, 360 significance, 361 Adipophilin, 20, 418 Adulteration, of dairy products, 121–122 Aldolase, indigenous enzymes, 369 Alkaline phosphatase, indigenous enzymes assay methods chemiluminescent assay, 357 ELISA, 357 fluorometric methods, 357 isolation and characterisation, 355–356 reactivation of, 357–358 significance, 358–359 American Dairy Science Association (ADSA), 56 Amino acid transport Na+ dependent transport mechanisms, 448–449 Na+ independent transport mechanisms, 449–450 peptides, 451 transport and metabolism, 450 volume-activated amino acid transport, 450 whey proteins comparison with casein, 49–50 as sources, 27 Amniotes, 5–6 Amphibian skin glands, Amylase, indigenous enzymes, 367–368 Angiotensin-converting enzyme (ACE), 319–320 Anti-adipogenic effects, lactoferrin, 305 Anticancer effects, lactoferrin, 302–303 Antigen-binding fragments (Fab), 276 Antiviral effects, lactoferrin, 303 Apocrine glands, 10–12 Apo-pilo-sebaceous unit (APSU), 11–12 Aspergillus A awamori, 298 A nidulans, 298 Atherosclerosis, 344 B Bacterial peptidases, 119 Bile salts-stimulated lipase, 351 Binding proteins FBPs, 324 riboflavin, 325 vitamin B12, 325 vitamin D, 324–325 Biosensors, 116–117 b-Lactoglobulin (BLG) amino acid residues, 406 cell culture tests, 407 genomic organisation, 405 polymorphic variants, 407 quantitative effects, 407 BLG See b-lactoglobulin (BLG) Blood serum albumin (BSA), 62 BML See Bovine milk lysozyme (BML) BMPs See Bone morphogenetic proteins (BMPs) Bone morphogenetic proteins (BMPs), 12 Boulengerula taitanus, Bovine milk angiogenin, 319 Bovine milk lysozyme (BML), 365, 366 Bovine milk proteins as1-casein, 468–469 as2-casein, 471, 472 b-casein, 468, 470 k-casein, 471–472 a-lactoglobulin, 474, 475 b-lactoglobulin, 472–474 Bovine mucin 15 (MUC15), 328 Bovine serum albumin (BSA), 118, 328 Breast cancer resistance protein (BRCP), 495 BSA See Bovine serum albumin (BSA) Butyrophilins, 19–20, 413–415 539 P.L.H McSweeney and P.F Fox (eds.), Advanced Dairy Chemistry: Volume 1A: Proteins: Basic Aspects, 4th Edition, DOI 10.1007/978-1-4614-4714-6, © Springer Science+Business Media New York 2013 Index 540 C Caecilians, Capillary electrophoresis (CE), 101 Capillary zone electrophoresis (CZE), 107 Caprine milk proteins k-casein, 482, 484 as1-Casein, 474–479 as2-casein, 480, 482, 483 b-casein, 479–480 a-lactoglobulin, 484 b-lactoglobulin, 484 as1-Casein, 392 bovine milk proteins, 468–469 genetic variation, 139 hydrophobic dimers and oligomers double ribbon structure, 167 fragments f136–196, 166–168 weight-average molecular weights, 166 interactions with calcium, 140–141 ovine milk proteins, 484, 486–487 primary structure, 136–138 secondary structure, 139 self association, 139–140 three-dimensional molecular models, 163 as2-Casein, 395–397 association properties, 144 bovine milk proteins, 471, 472 genetic polymorphism, 142, 143 interactions with calcium, 144 molecular modeling, 173–174 ovine milk proteins, 487, 489–490 primary structure, 141–142 secondary structure, 143–144 b-Casein amino acid sequence, 394 association properties, 148 bovine milk proteins, 468, 470 cations, 149 exon skipping, 395 gene encoding, 395 genetic polymorphism, 145, 147 interactions with calcium, 149 molecular modeling, 168–170 ovine milk proteins, 487 primary structure, 144–145 secondary structure, 147 k-Casein, 397 association behavior, 154 bovine milk proteins, 471–472 disulphide-bonding patterns, 153 genetic variation, 151–152 glycosylation, 152–153 interactions with calcium, 154–155 molecular modeling, 170–173 ovine milk proteins, 490 primary structure, 149–151 secondary structure, 153 Caseinates preparation, 49 Casein chemistry b-casein association properties, 148 cations, 149 genetic polymorphism, 145, 147 interactions with calcium, 149 primary structure, 144–146 secondary structure, 147 composition and nomenclature, 135–136 k-casein association behavior, 154 disulphide-bonding patterns, 153 genetic variation, 151–152 glycosylation, 152–153 interactions with calcium, 154–155 primary structure, 149–151 secondary structure, 153 as1-casein genetic variation, 139 interactions with calcium, 140–141 primary structure, 136–138 secondary structure, 139 self association, 139–140 as2-casein association properties, 144 genetic polymorphism, 142, 143 interactions with calcium, 144 primary structure, 141–143 secondary structure, 143–144 Casein-encoding genes gene cluster, 432–433 individual gene structures, 433–434 Casein micelles (CM) calcium phosphate, 193–194 casein polymerization, 190–193 characteristics of, 68 microstructural imaging bovine milk, 195 stereo pairs, 195, 196 TEM, 194 modeling polyelectrolyte brush model, 188 subunit model, 188 X-ray scattering, 189 physical properties, 189–190 stability, 69–70 structure dual-bonding model, 73 principal features, 70–71 sub-micelle model, 71–73 supramolecule acidification of milk, 199–202 calcium phosphate nanoclusters, 197, 198 calcium sequestration, 202–203 cooling of milk, 198–199 ethanol, 204–205 heating of milk, 203–204 interlocked lattice, 196–198 pH, 201–202 thermodynamic forces, 190 Casein nitrogen, 91 Caseinomacropeptide (CMP), 397 Casein protein preparation caseinates preparation, 49 Index centrifugation after calcium enrichment, 47 cryoprecipitation, 48 ethanol precipitation, 48 gel filtration, 48 isoelectric precipitation, 46–47 membrane filtration, 47–48 rennet coagulation, 48 salting-out methods, 47 ultracentrifugation, 47 Caseins as1-casein, 392 as2-casein, 395–397 b-casein amino acid sequence, 394 exon skipping, 395 gene encoding, 395 casein gene locus, 389–392 comparison with whey proteins amino acid composition, 49–50 biosynthesis site, 50 coagulation by limited proteolysis, 49 heat stability, 49 physical state, 50 solubility at pH 4.6, 49 functions of, 161 heterogeneity and fractionation, 50–53 interspecies comparison, 74–75 k-casein, 397 micelle model, 388 micelle organisation, 404–405 microheterogeneity, 54–56 molecular modeling as1-casein, 165–168 as2-casein, 173–174 b-casein, 168–170 k-casein, 170–173 mixed associations, 174–175 sodium caseinate, 176–179 post-translational modifications glycosylation, 404 phosphorylation, 402–403 post-translational process, 389 pre-mammalian origin, 14 protein structure classification, 165 IUP/NU, 163 PMG, 163, 164 properties, 163 SAA deficit, 27 secretory calcium-binding phosphoproteins, 14–18 splice variants cryptic splice sites, 399 genetic polymorphism, 400–401 “species-specific” casual exon skipping, 399–400 tensegrity hypothesis and resolution, 179–182 three-dimensional molecular models, 163 vitellogenins, 18 Catalase, indigenous enzymes, 341–342 CCP See Colloidal calcium phosphate (CCP) CE See Capillary electrophoresis (CE) CHC See Chronic hepatitis C (CHC) 541 Chromatin, 440–441 Chronic hepatitis C (CHC), 303 CID See Collision-induced dissociation (CID) CIFN See Consensus interferon (CIFN) Circular dichroism (CD), 111–112, 169 CIS See Crystalline insoluble substance (CIS) CMP See Caseinomacropeptide (CMP) CMV See Cytomegalovirus (CMV) Cobalamin, 325 Collision-induced dissociation (CID), 108 Colloidal calcium phosphate (CCP), 46 Colostrum milk immunoglobulins intestinal actions, 283–284 nutritional value, 284–285 role of, 285 Column chromatography gel filtration, 101–102 hydrophobic interaction and reversed-phase (RP)-HPLC, 104–105 ion exchange, 102–104 Consensus interferon (CIFN), 303 Conversion factors, quantitation, 89–90 Crocidura russula, Cryoprecipitation, 48 Crystalline insoluble substance (CIS), 58 Cytomegalovirus (CMV), 303 CZE See Capillary zone electrophoresis (CZE) D Dietary proteins amino acid requirements, 517–518 protein digestibility, 519–520 protein requirements, 516–517 protein utilisation, 520–521 Disulfide bonding, 55 Dual-bonding model, casein micelle, 73 E EGF See Epidermal growth factor (EGF) Egg-white lysozyme (EWL), 364–367 Electron micrographs (EM), 176 Electrophoresis capillary, 101 isoelectric focusing, 100–101 microfluidic “lab-on-a-chip” techniques, 101 milk proteins applications, 53–54 native, 99 SDS, 99–100 two-dimensional, 101 Electrospray ionisation mass spectrometry (ESI-MS), 106–107 ELISA See Enzyme-linked immunosorbent assay (ELISA) EM See Electron micrographs (EM) Enzyme-linked immunosorbent assay (ELISA) accuracy and precision, 116 advantages, 115 BSA, 118 a-lactalbumin, 118 Index 542 Enzyme-linked immunosorbent assay (ELISA) (cont.) lactoferrin, 118–119 b-lactoglobulin, 117–118 plasmin, 119 sensitivity, definition of, 116 types of, 115 Epidermal growth factor (EGF), 324 ESI-MS See Electrospray ionisation mass spectrometry (ESI-MS) Estemmosuchus, Ethanol precipitation, 48 EWL See Egg-white lysozyme (EWL) F FABP See Fatty acid-binding proteins (FABP) Fatty acid-binding proteins (FABP), 495–496 FBPs See Folate-binding proteins (FBPs) Feedback inhibitor of lactation (FIL), 326 FIL See Feedback inhibitor of lactation (FIL) Fluorescence resonance energy transfer (FRET), 234 Folate-binding proteins (FBPs), 324 Fourier transform infrared (FTIR) b-casein, 169 k-casein, 172 sodium caseinate, 177–179 Fractionation and heterogeneity of caseins, 50–53 whey proteins, 57–58 FRET See Fluorescence resonance energy transfer (FRET) FTIR See Fourier transform infrared (FTIR) G b4-Galactosyltransferase-1 (b4Gal-T1), 23–26 Gastrointestinal tract EGF and TGFa, 324 IGF-1 and IGF-2, 323–324 Gel filtration casein preparation, 48 column chromatography, quantitation, 101–102 Genetic polymorphism, 55 casein genes vs milk production traits, 497–498 population and phylogeny studies, 498–500 dairy ruminants bovine milk proteins, 468–475 caprine milk proteins, 474–484 ovine milk proteins, 484–490 detection methods DNA level, 465–466 mass spectrometry analysis, 464–465 “top-down” process, 464–465 human nutrition bioactive peptides, 500–502 milk allergy, 502 milk-fat globule membrane proteins ABCG2, 495 butyrophilin, 493–494 FABP3, 495–496 fatty acid synthase, 493 MFGE8, 494–495 MUC-1, 491, 493 protein-encoding gene, 496 molecular basis, 466–467 g-Glutamyl transferase (GGT), 347–348 Glutathione peroxidase (GSHPOx), 347 Glycomacropeptide (GMP), 171, 172 Glycosylation k-casein, 152–153 post-translational modifications, 404 GMP See Glycomacropeptide (GMP) GSHPOx See Glutathione peroxidase (GSHPOx) Gut-associated lymphoid tissue (GALT), 279 H Hadrocodium wui, Haptodus, HARP See Heparin affin regulatory peptide (HARP) HCV See Hepatitis C virus (HCV) Heat stability, 49 Heparin affin regulatory peptide (HARP), 320 Hepatitis C virus (HCV), 303 Higher order structures molecular modeling as1-casein, 165–168 as2-casein, 173–174 b-casein, 168–170 k-casein, 170–173 mixed associations, 174–175 sodium caseinate, 176–179 protein structure, 162–165 three-dimensional molecular models, 163 HML See Human milk lysozyme (HML) Hooded seal, 10 HT-29 See Human enterocyte-like cell line (HT-29) Human enterocyte-like cell line (HT-29), 304 Human milk lysozyme (HML), 365–367 Hylonomus, I Ichthyophis glutinosus, IEF See Isoelectric focusing (IEF) IGF See Insulin-like growth factor (IGF) IGF-binding proteins (IGFBPs), 323–324 Immune function b2-microglobulin, 321 lactoperoxidase, 322–323 lysozyme, 323 osteopontin, 321–322 proteose peptone 3, 322 TGFb1 and 2, 323 Immunoblotting, 116 Immunochemical methods, quantitation antibody arrays, 117 applications, 117–123 biosensor, 116–117 ELISA, 115–116 general characteristics of, 114 immunoblotting, 116 Index microparticle-enhanced nephelometric immunoassay, 116 precipitation in gel, 116 significance and developments, 123 Immunoglobulins (Igs) biological fluids, 277 classes and structure, 275–277 mammary gland immunity heterologous transfer, 286 homologous transfer, 285–286 mammary gland transport IgA and IgM, 280–281 IgG, 280 neonate colostrum, 283–285 and immunity, 283 milk immunoglobulins, 283–285 passive immunity transfer intestinal uptake, 282 neonate, 281–282 properties of, 277–279 sources, 279 transport control, 281 whey proteins, 62–63 Indigenous enzymes acid phosphatase assay methods, 360 isolation and characterisation, 360 significance, 361 aldolase, 369 alkaline phosphatase assay methods, 356–357 isolation and characterisation, 355–356 reactivation of, 357–358 significance, 358–359 amylase, 367–368 b-N-acetylglucosaminidase, 368–369 catalase, 341–342 g-glutamyl transferase, 347–348 glutathione peroxidase, 347 lactoperoxidase, 339–341 lipases bile salts-stimulated lipase, 351 esterases, 351–352 LPL, 349–351 phospholipase, 351 lysozyme, 364–367 minor enzymes, 339 nucleases catalytic antibodies, oligonuclease activity, 363–364 5’-nucleotidase, 364 ribonuclease, 361–363 proteinases cathepsin D, 353 human milk, 354 plasmin, 352–353 significance of, 354 somatic cells, 354 sulphydryl oxidase, 346 543 superoxide dismutase, 345–346 xanthine oxidoreductase assay methods, 343 atherosclerosis, 344 bactericidal activity, 344 effect of processing, 343 evolution of mammals, 344–345 heat treatment, 343–344 isolation of, 342 lipid oxidation, 344 milk fat globules, 344 nitrate reduction, 344 Infrared spectroscopy, 91–98 MIR, 92–95 NIR, 95–98 secondary and tertiary structures, 110–111 Insulin-like growth factor (IGF), 323–324 Intrinsically unstructured protein (IUP), 163, 164 Ion exchange, column chromatography, 102–104 Isoelectric focusing (IEF), 100–101 Isoelectric precipitation, 46–47 IUP See Intrinsically unstructured protein (IUP) K Kjeldahl method analysis, 90–91 principle, 90 L LAB See Lactic acid bacteria (LAB) Lactadherin, 415–417 a-Lactalbumin (a-La) apoptotic effects, tumor, 269–270 lactose synthase organization and regulation, 262–263 role, 261–262 vs Lysozyme Ca-binding sites, 263, 264 phylogenetic tree, 265 three-dimensional structures b4-GT-I, 268–269 binding, 268 calcium-binding site, 266–268 catalytic domain, 267 Ca/Zn complex, 266 irregular b-turns, 265, 266 whey proteins, 60–62 Lactation amniotes amniotic egg, Hylonomus, Paleothyris, amphibian skin glands, caecilians, Crocidura russula, Hadrocodium wui, hooded seal milk, 10 544 Lactation (cont.) sauropsids, synapsids diphyodonty, eggs of, 5–6 Estemmosuchus, incubating eggs, proto-lacteal glands, sequential radiations, 7–9 terrestrial vertebrates, 2–3 tetrapods proto-lacteal glands, skin secretion, 2, terrestrial eggs, parental care of, 4–5 Lactic acid bacteria (LAB), 46 Lactoferrin, 321 biochemical properties concentrations and species differences, 296 historical perspective, 295 metal-and anion-binding properties, 296–297 molecular weight and glycosylation, 296 resistant to proteolytic degradation, 297–298 tertiary structure, 296, 297 biological functions anti-adipogenic effects, 305 anticancer effects, 302–303 antiviral effects, 303 bacteriostasis/bactericidal effects, 301–302 bone homeostasis, 304–305 as growth factor, 304 immune function, 299–301 iron absorption, 305–307 multi-functionality, 299, 300 wound healing, 305 implications and significance of, 308–309 molecular biology, 298–299 receptors characteristics of, 308 monocyte/macrophage system, 308 in small intestine, 307–308 Lactoferrin (LTF), 410–411 a-Lactoglobulin bovine milk proteins, 474, 475 caprine milk proteins, 484 ovine milk proteins, 490 b-Lactoglobulin (b-Lg) amino acid environments, 225–227 binding studies EF loop, 238 fatty acids, 234 FRET study, 234 ligand-binding parameters, 235–237 macromolecule binding, 239–240 pH, 234 biosynthesis and secretion, 213–214 bovine milk proteins, 472–474 caprine milk proteins, 484 conformation and folding N↔R, 230–231 Q↔N, 229–230 Index R↔S, 231 unfolding–refolding, 231, 232 denaturation, 232–233 distribution, 214–216 evolutionary origin of, 27–31 evolutionary relationship, 241 function, 240–242 genetic variants and primary structure, 217–221 immunochemical methods, quantitation, 117–118 isolation, 216–217 ovine milk proteins, 490 solution studies molecular properties, 228 molecular size, 227–229 solubility, 227 structure, 221–225 whey proteins, 58–60 Lactoperoxidase (LPO), 322–323, 339–341 Lipoprotein lipase (LPL), 349–351 Listeria monocytogenes, 301 LPL See Lipoprotein lipase (LPL) LTF See Lactoferrin (LTF) Lysinoalanine (LAL), 528 Lysozyme, 410 Lysozyme (Lz) Ca-binding sites, 263, 264 phylogenetic tree, 265 M MALDI-MS See Matrix-assisted laser desorption/ionisation mass spectrometry (MALDI-MS) Mammary glands apocrine glands, 10–12 APSU and MPSU, 11–12 BMP signaling pathways, 12 Darwin’s theory of evolution, 1, 10 granular glands, 13 immunity heterologous transfer, 286 homologous transfer, 285–286 innate immune system, 12–13 in mid-nineteenth century, opossums, 11 oxytocin and mesotocin, 13 sweat glands, 10 Mammary secretions, immunoglobulins biological fluids, 277 classes and structure, 275–277 neonate colostrum and milk immunoglobulins, 283–285 and immunity, 283 origins of IgA and IgM, 280–281 IgG, 280 sources of, 279 transport control, 281 passive immunity transfer, 281–282 properties of, 277–279 Index Mammo-pilo-sebaceous unit (MPSU), 11–12 Mass spectrometry (MS) electrospray ionisation, 106–107 MALDI, 106 milk proteins, molecular mass determination, 107–108 peptides, 109–110 protein sequencing, 108–109 Matrix-assisted laser desorption/ionisation mass spectrometry (MALDI-MS), 106 Membrane filtration, 47–48 MFE See Molybo-flavoenzyme (MFE) MFG See Milk fat globules (MFG) MFGM proteins See Milk fat globule membranes (MFGM) proteins MG See Molten globule (MG) b2-Microglobulin, 321 Milk composition of, 43, 44 features, 43 lactose synthesis, 23–27 physiological functions, 43 production, 43 acidification, 199–202 cooling, 198–199 heating, 203–204 Milk allergy, 502 Milk and products amino acid composition bovine, 524 branched-chain amino acids, 522, 523 casein, 522 indispensible amino acids protein content, 521 methionine and cysteine, 523 sulphur-containing amino acids, 523 whey protein, 522 cheesemaking, 530–531 digestibility vand utilisation, 524–526 heat treatments D-amino acids, 529 furosine accumulation, 529 lysinoalanine, 528, 529 Maillard reaction, 527 pasteurisation, 527 protein modifications, 529 thermal denaturation, 527 UHT treatment, 527 homogenisation, 531 Milk fat globule membranes (MFGM) proteins genetic polymorphism ABCG2, 495 butyrophilin, 493–494 FABP3, 495–496 fatty acid synthase, 493 MFGE8, 494–495 MUC-1, 491, 493 protein-encoding gene, 496 glycosylation, 418–419 mucins MUC-1, 412–413 545 MUC-15, 413 non-mucin proteins adipophilin, 418 butyrophilin, 413–415 lactadherin, 415–417 Milk fat globules (MFG) adipophilin, 21 apical blebs, 21–22 apocrine secretory mechanisms, 21–22 butyrophilin, 19–20 triacylglycerols, 19 xanthine oxidoreductase, 20–21 Milk protein concentrates (MPCs), 47 Milk proteins casein-encoding genes gene cluster, 432–433 individual gene structures, 433–434 casein micelle characteristics of, 68 stability, 69–70 structure, 70–74 casein protein preparation caseinates preparation, 49 centrifugation after calcium enrichment, 47 cryoprecipitation, 48 ethanol precipitation, 48 gel filtration, 48 isoelectric precipitation, 46–47 membrane filtration, 47–48 rennet coagulation, 48 salting-out methods, 47 ultracentrifugation, 47 chromatin, 440–441 cis-regulatory elements, 436–438 classical fractions of, 45 evolution, 34–35 gel electrophoresis applications, 53–54 genetic polymorphism (see Genetic polymorphism) heterogeneity and fractionation, 50–53 hormonal regulation, 436–438 interspecies comparison, 74–75 b-lactoglobulin (see b-Lactoglobulin (BLG)) mammary epithelial amino acid transport Na+ dependent transport mechanisms, 448–449 Na+ independent transport mechanisms, 449–450 peptides, 451 transport and metabolism, 450 volume-activated amino acid transport, 450 mammary secretory epithelium biosynthetic-secretory pathway, 442 co-and post-translational modifications, 442–443 Golgi apparatus, 445–446 hormonal regulation, 447 intracellular transport, 442–443 morphological organization, 442 trans-Golgi network, 446–447 translocation, endoplasmic reticulum, 444–445 Index 546 Milk proteins (cont.) MFGM (see Milk fat globule membranes (MFGM) proteins) microheterogeneity of caseins, 54–56 molecular properties of, 65–68 mRNAs, 441 nomenclature of, 56 nutritional quality (see Nutrition) prolactin signal transduction, 439–440 quantitation of (see Quantitation) research, 44 tissue specificity and developmental regulation, 436 transcriptional control, 438–439 whey protein encoding genes a-lactalbumin gene and pseudogenes, 434 b-lactoglobulin-encoding gene and pseudogenes, 434 whey acidic protein, 435 whey proteins (see also Whey proteins) characteristics of, 58–65 comparison with casein proteins, 49–50 fractionation of, 57–58 preparation, 49, 56–57 Milk teeth, Minor proteins binding proteins FBPs, 324 riboflavin, 325 vitamin B12, 325 vitamin D, 324–325 BSA, 328 gastrointestinal tract EGF and TGFa, 324 IGF-1 and IGF-2, 323–324 immune function b2-microglobulin, 321 lactoperoxidase, 322–323 lysozyme, 323 osteopontin, 321–322 proteose peptone 3, 322 TGFb1 and 2, 323 mammary gland and maternal physiological regulatory function FIL, 326 leptin, 325–326 PTHrP, 326–327 relaxin, 327 mucins and glycoproteins, 327–328 vascular system ACE, 319–320 angiogenins, 318–319 HARP, 320 kininogen, 321 Molten globule (MG), 162–164, 269 Molybo-flavoenzyme (MFE), 20 Morganucodon, MPCs See Milk protein concentrates (MPCs) MPSU See Mammo-pilo-sebaceous unit (MPSU) MS See Mass spectrometry (MS) MUC15 See Bovine mucin 15 (MUC15) Mucin (MUC1), 327–328 Mucins MUC-1, 412–413 MUC-15, 413 Mucous secreting cells, 12 Multiple anomalous dispersions (MAD), 112 N b-N-Acetylglucosaminidase (NAGase), 368–369 Native electrophoresis, quantitation, 99 Natively unfolded (NU), 163, 164 NCN See Non-casein nitrogen (NCN) Neonatal Fc receptor (FcRn), 280 Nitric oxide synthase (NOS) activity, 318 Nitrogen fractions, quantitation, 89 NMR See Nuclear magnetic resonance (NMR) Non-casein nitrogen (NCN), 91 Non-mucin proteins adipophilin, 418 butyrophilin, 413–415 lactadherin, 415–417 Non-protein nitrogen (NPN), 64–65, 91 NOS activity See Nitric oxide synthase (NOS) activity Nuclear magnetic resonance (NMR) milk proteins application, 114 principle, 112–113 Nucleases, indigenous enzymes catalytic antibodies, oligonuclease activity, 363–364 5’-nucleotidase, 364 ribonuclease, 361–363 Nutrition bioactive peptides, 500–502 dietary proteins amino acid requirements, 517–518 protein digestibility, 519–520 protein requirements, 516–517 protein utilisation, 520–521 milk allergy, 502 milk and milk products amino acid composition, 521–524 cheesemaking, 530–531 digestibility and utilisation, 524–526 heat treatments, 526–529 homogenisation, 531 physiological activities, 531–533 O Origin of Species, Opossums, 11 Osteopontin, 321–322 Ovine milk proteins as1-casein, 484, 486–487 as2-casein, 487, 489–490 b-casein, 487 Index k-casein, 490 a-lactalbumin, 490 b-lactoglobulin, 490 P Paleothyris, Parathyroid hormone-related protein (PTHrP), 326–327 Parental care, 4–5 PAs See Plasminogen activators (PAs) Phospholipase, 351 pIgR See Polymeric immunoglobulin receptor (pIgR) Plasmin, 55–56, 119, 352–353 Plasminogen activators (PAs), 352 PLG See Plasminogen (PLG) Polymeric immunoglobulin receptor (pIgR), 281 Polyproline II conformation (PPII), 163 PPII See Polyproline II conformation (PPII) Plasminogen (PLG), 119 Pre-molten globule (PMG), 163, 164 Proteinases, indigenous enzymes cathepsin D, 353 human milk, 354 plasmin, 352–353 significance of, 354 somatic cells, 354 Proteolysis, 120 Proteose peptone (PP) 3, 63–64, 322 Proto-lacteal glands, Pseudomonas aeruginosa, 302 Pseudomonas fluorescens, 119–120 PTHrP See Parathyroid hormone-related protein (PTHrP) Q Quantitation definition and analytical performance conversion factors, 89–90 nitrogen fractions, 89 immunochemical methods antibody arrays, 117 applications, 117–123 biosensor, 116–117 ELISA, 115–116 general characteristics of, 114 immunoblotting, 116 microparticle-enhanced nephelometric immunoassay, 116 precipitation in gel, 116 significance and developments, 123 individual proteins capillary electrophoresis, 101 column chromatography, 101–105 (see also Column chromatography) isoelectric focusing, 100–101 mass spectrometry, 105–110 microfluidic “lab-on-a-chip” techniques, 101 native electrophoresis, 99 547 SDS electrophoresis, 99–100 secondary and tertiary structures, 110–114 two-dimensional electrophoresis, 101 infrared methods, 91–98 Kjeldahl method analysis, 90–91 principle, 90 R RCM See Reduced carboxymethylated (RCM) Reduced carboxymethylated (RCM), 173, 174 Relaxin, 327 Rennet coagulation, 48 Respiratory syncytial virus (RSV), 303 Riboflavin, 325 Ribonucleases (RNase), 361–363 RSV See Respiratory syncytial virus (RSV) S SAA See Sulfur-containing amino acids (SAA) Salting-out methods, 47 Sauropsids, Secondary structures, quantitation circular dichroism spectroscopy, 111–112 infrared spectroscopy, 110–111 nuclear magnetic resonance, 112–114 X-ray crystallography, 112 Secretory calcium-binding phosphoproteins (SCPP), 14–18 Sodium caseinate 3D models, 176–179 FTIR studies, 177–179 laboratory preparations, 176 Soy proteins, 123 Staphylococcus epidermis, 301 Sub-micelle model, 71–73 Sulfur-containing amino acids (SAA), 27 Sulphydryl (SH) groups, 358 Sulphydryl oxidase (SHOx), 346 Superoxide dismutase (SOD), 345–346 Supramolecule, casein acidification of milk, 199–202 calcium sequestration, 202–203 cooling of milk, 198–199 EDTA, 202, 203 ethanol, 204–205 heating of milk, 203–204 interlocked lattice, 196–198 Sweat glands, 10 Synapsids eggs of, 5–6 Estemmosuchus, sequential radiations, 7–9 T Tensegrity hypothesis, higher order structures, 179–182 Tertiary structures Index 548 lactoferrin, 296, 297 quantitation circular dichroism spectroscopy, 111–112 infrared spectroscopy, 110–111 nuclear magnetic resonance, 112–114 X-ray crystallography, 112 Tetrapods proto-lacteal glands, terrestrial eggs, parental care of, 4–5 Thrinaxodon, TOCSY See Total correlation spectroscopy (TOCSY) Total correlation spectroscopy (TOCSY), 113 Transforming growth factor (TGF)b1, 323 Transmission electron microscopy (TEM), 187–188, 192, 194, 198 Two-dimensional electrophoresis, 101 U Ultracentrifugation, 47 V Variable number of tandem repeats (VNTR), 418 Vascular system ACE, 319–320 angiogenins, 318–319 HARP, 320 kininogen, 321 Vitamin B12-binding protein, 325 Vitamin D-binding protein, 324–325 Vitellogenins, 18 VNTR See Variable number of tandem repeats (VNTR) W WAP See Whey acidic protein (WAP) Whey acidic protein (WAP), 31–34, 60, 407–408 Whey protein concentrates (WPCs), 47–48 Whey protein isolates (WPIs), 48 Whey proteins characteristics of blood serum albumin, 62 immunoglobulins, 62–63 a-lactalbumin, 60–62 b-lactoglobulin, 58–60 nonprotein nitrogen, 64–65 proteose peptones, 63–64 whey acidic protein, 60 comparison with caseins amino acid composition, 49–50 biosynthesis site, 50 heat stability, 49 physical state, 50 solubility at pH 4.6, 49 fractionation of, 57–58 immunochemical methods, quantitation, 117 preparation, 49, 56–57 WPCs See Whey protein concentrates (WPCs) X Xanthine oxidoreductase (XOR), 20–21 assay methods, 343 atherosclerosis, 344 bactericidal activity, 344 effect of processing, 343 evolution of mammals, 344–345 heat treatment, 343–344 isolation of, 342 lipid oxidation, 344 milk fat globules, 344 nitrate reduction, 344 X-ray crystallography, 112 ... (www.springer.com) Preface to the Fourth Edition Advanced Dairy Chemistry- 1A: Proteins: Basic Aspects is the first volume of the fourth edition of the series on advanced topics in dairy chemistry, which started... desired depth in one volume Hence, coverage of dairy proteins in the fourth edition of Advanced Dairy Chemistry will be split between basic (this volume) and applied aspects (Volume 1B, forthcoming)...Paul L.H McSweeney • Patrick F Fox Editors Advanced Dairy Chemistry Volume 1A: Proteins: Basic Aspects, 4th Edition Editors Paul L.H McSweeney University College Cork School