Advanced Dairy Chemistry: Volume 1: Proteins, Parts A&B: ProteinP. F. Fox, P. L. H. McSweeney Advanced Dairy Chemistry-1. Proteins addresses the most commercially important constituents of milk in terms of their roles in nutrition and as functional components in foods. This third edition, which is the work of dairy scientists and other experts from around the world, provides detailed scientific information on all aspects of milk proteins.An extensively revised Table of Contents includes more chapter-level headings to make the material more accessible and highlights a number of key topics, such as methods for resolving and identifying proteins, biologically and physiologically active proteins, molecular genetics and functional milk proteins-all of which have assumed increased importance in recent years.All chapters from the second edition have been completely updated and coverage of the biological properties and stability of milk proteins has been enhanced greatly. The book has been expanded from 18 chapters in the second edition to 29 chapters and 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. New topics include an overview of the milk protein system, allergenicity of milk proteins, bioactive peptides, genetic engineering of milk proteins, and certain additional chapters on protein-rich dairy products.This authoritative work summarizes current knowledge on milk proteins and suggests areas for future work. |
Contents
Milk proteins general and historical aspects | 1 |
12 Preparation of casein and why proteins | 5 |
13 Comparison of key properties of casein and whey proteins | 9 |
14 Heterogeneity and fractionation of casein | 11 |
15 Application of gel electrophoresis to the study of milk proteins | 14 |
16 Microheterogeneity of the caseins | 15 |
17 Nomenclature of milk proteins | 18 |
19 Fractionation of whey proteins | 19 |
𝛼Lactalbumin | 387 |
82 OVERVIEW OF EARLIER WORK | 388 |
83 Structure | 392 |
84 Aspects of 𝛼lactalbumin function | 401 |
85 Conclusion | 410 |
Acknowledgement | 412 |
Immunoglobulins | 421 |
93 Transfer of passive immunity | 431 |
110 Some major characteristics of why proteins | 20 |
111 Molecular properties of the milk proteins | 28 |
112 Casein micelle | 31 |
113 Interspecies comparison of milk products | 39 |
114 Summary and perspective | 40 |
References | 41 |
Quantitation of proteins in milk and milk products | 49 |
21 Introduction | 51 |
22 Definitions of protein and analytical performance | 52 |
23 Reference and routine methods | 56 |
24 Separate deterimination and characterization of individual proteins in milk and dairy products | 80 |
25 Immunochemicals methods | 106 |
References | 119 |
Chemistry of caseins | 139 |
32 Protein composition of milk | 140 |
33 Isolation and identification of caseins | 145 |
34 Primary structure and chemical composition of the caseins | 154 |
35 Physicochemical characteristics of the caseins | 176 |
36 Projection of future work | 187 |
Higher orders structures of the caseins a paradox? | 203 |
42 Molecular modelling of aₓ₁ | 211 |
43 The tensegrity hypothesis and resolution | 225 |
References | 229 |
Casein micelle structure functions and interactions | 233 |
52 Biological functions of the caseins | 234 |
53 Structure of the individual caseins | 236 |
54 Size and voluminosity of the casein micelle | 241 |
55 Surface structure of the casein micelle | 244 |
56 Internal structure of the casein micelle | 246 |
57 Dissociation of casein micelles in response to environmental change | 254 |
58 Aggregation gelation and syneresis | 258 |
Acknowledgements | 270 |
Nonbovine caseins quantitative variability and molecular diversity | 277 |
62 The casein gene locus and quantitative variability | 278 |
an interspecies comparison | 281 |
interspecies variability | 289 |
65 Micelle organisation | 301 |
66 Analytical tools | 303 |
67 Concluding remarks | 308 |
References | 310 |
𝛽Lactoglobulin | 319 |
72 Biosynthesis and secretion | 320 |
73 Distribution | 321 |
74 Isolation | 324 |
75 Genetic variants and primary structure | 325 |
76 Molecular structure | 330 |
77 Solution studies | 335 |
78 Denaturation | 337 |
79 Secondary structure | 342 |
711 Amino acid environments | 345 |
712 Sitedirected mutagenesis | 347 |
713 Binding studies | 348 |
714 Homologous proteins | 358 |
715 Function | 361 |
716 Conclusion | 363 |
94 Control of transport and mammary gland immunity | 436 |
95 Interactions with other proteins in milk | 437 |
97 Conclusion | 438 |
439 | |
Lactoferrin | 449 |
103 Molecular biology of lactoferrin | 452 |
104 Biological functions of lactoferrin | 453 |
105 Lactoferrin receptors | 459 |
106 Implications and significance | 461 |
Indigenous enzymes in milk | 467 |
References | 470 |
Lipases in milk | 473 |
1122 Role of the lipoprotein lipase in metabolism of plasma lipoproteins | 474 |
1123 Structure | 475 |
1124 Catalytic properties | 479 |
1125 Apolipoprotein CII | 480 |
1126 Product inhibition | 481 |
1128 LPL in the mammary gland | 483 |
1129 SYNTHESIS AND SECRETION INTO MILK | 484 |
11210 State of LPL in milk | 486 |
11211 Lipolysis in milk | 487 |
References | 488 |
Indigenous proteinases in milk | 495 |
1132 Plasmin system in milk | 496 |
1133 Somatic cell proteinases | 505 |
References | 512 |
Indigenous phosphates in milk | 523 |
1142 Acid phosphatase | 525 |
1143 Milk alkaline phosphatase | 530 |
539 | |
Indigenous nucleases in milk | 545 |
1153 Ribonucleases | 547 |
1154 Ribonucleases in milk | 549 |
1155 Catalytic antibodiesabyzmes with oligonuclease activity | 552 |
557 | |
Lactoperoxidase | 563 |
1162 Structure of bovine lactoperoxidase bLPO | 564 |
1163 Major reactions of bovine lactoperoxidase | 566 |
1164 Components of the lactoperoxidase system in bovine milk | 567 |
1166 Conclusions | 568 |
Other enzymes 1171 Introduction | 571 |
1173 Catalase EC 11116 | 572 |
1174 Glutathione peroxidase EC 11119 | 574 |
1176 Xanthine oxidase EC 11322 | 576 |
1177 Sulphydryl oxidase | 578 |
1178 YGlutamyl transferase EC 2322 | 579 |
1179 Amylases | 580 |
11710 Lysozyme EC 32117 | 581 |
11711 NAcetyl𝛽Dglucosaminidase EC 32130 | 583 |
11712 𝛼Mannosidase EC 32124 | 584 |
11714 5Nucleotidase EC 3135 | 585 |
11715 Adenosine triphosphatase EC 3613 | 586 |
11717 Other enzymes | 591 |
Other editions - View all
Advanced Dairy Chemistry: Volume 1: Proteins, Parts A&B: Protein P. F. Fox,P. L. H. McSweeney Limited preview - 2003 |
Advanced dairy chemistry, Volume 1, Part 1 Patrick F. Fox,P. L. H. McSweeney No preview available - 2002 |
Advanced Dairy Chemistry: Volume 1: Proteins, Parts A&B: Protein P. F. Fox,P. L. H. McSweeney No preview available - 2003 |
Common terms and phrases
a-La a-lactalbumin abzymes Acta activity amino acid analysis antibodies antigen B-casein B-CN B-Lg binding Biochem Biol Biophys bovine bovine casein bovine milk C-terminal Ca2+ calcium phosphate caprine casein micelles cathepsin cathepsin D cells chain characterization cheese Chem chromatography colostrum components concentration conformation contains cows dairy products Dairy Res Dairy Sci denaturation detection determination dimer dissociation domain electrophoresis ELISA enzyme exon Farrell Figure Food fraction function gene genetic variants globule goat heat Holt human milk hydrophobic immunoglobulins interactions ionic strength isolated K-CN Kumosinski lactation lactoferrin lactose lipolysis lipoprotein lipase lysozyme mammary gland method milk proteins molecule monomer ovine oxidase P.F. Fox peptide phosphatase phosphorylation plasmin plasminogen precipitation primary structure properties proteinases proteolysis receptor region rennet retinol RNase samples secondary structure serum skim milk soluble species ẞ-CN stability studies substrate subunit Swaisgood techniques temperature urea whey proteins xanthine oxidase