Bioactive Egg Compounds

309 Pages·2007·5.18 MB·English

by  Marc Anton (auth.), Professor Rainer Huopalahti, Rosina López-Fandiño, Marc Anton, Rüdiger Schade (eds.)

Bioactive Egg Compounds
Rainer Huopalahti
Rosina López-Fandiño
Marc Anton
Rüdiger Schade (Eds.)
Bioactive Egg Compounds
With 30 Figures
Rainer Huopalahti Rosina López-Fandiño
Professor Isidra Recio
Food Chemistry Mercedes Ramos: Instituto de
Department of Biochemistry and Fermentaciones Industriales (CSIC)
Food Chemistry Juan de la Cierva 3
University of Turku 28006 Madrid
20014 Turku Spain
Finland e-mail:[email protected]
e-mail:[email protected]
Rüdiger Schade
Marc Anton Institut für Pharmakologie und
UR1268 Biopolymères Interactions Toxikologie
Assemblages Charité-Universitätsmedizin Berlin
INRA F-44316 Dorotheenstr. 94
NANTES 10117 Berlin
France Germany
e-mail:[email protected] e-mail:[email protected]
Library of Congress Control Number: 2006937340
ISBN-13: 978-3-540-37883-9 Springer Berlin Heidelberg New York
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Preface
The hen egg is one of the most versatile foods. It contains high-quality
proteins and lipids, as well as valuable minerals, carbohydrates, and vitamins.
Eggs are also widely used in the food industry due to their multifunctional
properties (e.g., foaming, gelling, and emulsifying). Of course, the primary
aim of the laying hen is not to produce high-value human food but to give rise
to new life. Therefore, avian eggs contain the basic elements for life, and
many of the egg compounds have so-called biological activity. For example,
almost all the albumen proteins are antimicrobial, thus protecting the devel-
oping embryo. Consequently, hen eggs are very good potential sources of raw
materials for health-promoting, so-called functional foods, as well as for the
traditional food and pharmaceutical industries.
In 2002 a COST action called “Multidisciplinary Hen Egg Research” was
founded that involves experts in different branches of egg research from 13
countries. The most important result of the COST action is the exchange of
expert knowledge between the participating countries and research groups.
Since the COST action has joined together leading European scientists in
egg research, the idea was born (in 2004) to write a book about latest
results/concepts in bioactive egg compounds and their possible use in the
food, pharmaceutical, and cosmetic industries.
The book comprises 33 chapter written by authors from 13 European and
non-European countries and is divided in three parts.
Part I contains 17 chapters concerning the composition and the extraction
of yolk, albumen, and shell compounds, respectively. We have particularly
paid attention to updating the data, notably by the contribution of our own
research results. We have opted to present, in the majority of cases, the struc-
tural aspect of the egg compounds, and of their interactions in relation to
their function. Lastly, very recent data coming from our research regarding
minor compounds are given exposure in the chapters dealing with proteases,
antiproteases, lipocalins, clusterin, etc.
In summary, this part is not an “umpteenth” presentation of the composi-
tion of the egg, but an updated document, presenting original results seen
from unique angles.
Part II, with 5 chapters, is concerned with the role of eggs in human nutri-
tion. The nutritive properties of eggs are evaluated in detail, with discussions
of the importance of the egg-contained macro and micronutrients, the
vi Preface
presence of functional substances, and the bioavailability of nutrients.
Further chapters deal with improvements in the nutritive value of eggs,
namely, by the enrichment in omega-3 fatty acids, vitamins, and selenium,
and the implications embodied therein for daily nutrient intake and human
health. The role of eggs as one of the main food allergens is also examined,
including the factors that determine the allergenic properties of egg proteins
and the possibilities for making hypoallergenic egg products.
Part III comprises 11 chapters divided in two subparts, and as in part 1 the
contents of the chapters are mainly based on the experiences of the authors
themselves. In particular, the use of specific bioactive egg compounds for
human beings is introduced. For example, possible application of egg white
compounds with antibacterial (and perhaps also antiviral) activity, or of egg-
white-derived peptides with antihypertensive activity, with the prospect that
a functional food fortified with these peptides may be produced. Further sub-
jects are the application (at present and in the future) of specific chicken
egg yolk antibodies in human and veterinary medicine, the potency of ion-
binding proteins as nutraceutical (ovoceutical), and new and interesting
fields of lecithin application.
The chapters of a second subpart are mainly focused on biotechnological
aspects of egg use: for example, new methods for egg protein fractionation, the
use of phospholipid-based liposomes/emulsions in pharmaceutics and cosmet-
ics, the use of specific yolk components for cryoprotection of spermatozoa,
and the usefulness of egg-protein-based films and coatings as biodegradable
packaging material. Finally, results are presented on nanotechnology in egg
research and news is given on avidin–biotin biotechnology.
The editors would like to express our thanks to all the authors who con-
tributed their expertise and knowhow to the success of this book. Furthermore,
we thank Springer for the patient and trustful cooperation during the process-
ing and realization of the project. Finally, we hope to present an interesting and
stimulating book that makes a contribution to understanding and disseminating
the state of art in research on bioactive egg compounds.
Turku, Madrid, Rainer Huopalahti, Rosina López-Fandiño,
Nantes, Berlin Marc Anton, Rüdiger Schade
September 2006
Contents
Part I Composition and Extraction of Egg Components
MARKANTON
Subpart Ia Egg Yolk Compounds
1 Composition and Structure of Hen Egg Yolk
MARCANTON . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1
2 Composition. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1
3 Macrostructure. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5
2 Low-density Lipoproteins (LDL) or Lipovitellenin Fraction
MARCANTON . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7
2 LDL Structure and Composition . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7
3 LDL Apoproteins. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 9
4 LDL Extraction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 11
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 12
3 High-density Lipoproteins (HDL) or Lipovitellin Fraction
MARCANTON . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 13
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 13
2 HDL Structure and Composition. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 13
3 HDL Extraction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 15
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 16
4 Phosvitin
MARCANTON, OSCARCASTELLANIANDCATHERINEGUÉRIN-DUBIARD . . . . . . . . . . 17
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 17
2 Phosvitin Composition and Structure. . . . . . . . . . . . . . . . . . . . . . . . . . . . . 17
3 Metal Chelating Properties. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 18
4 Phosvitin Extraction and Purification. . . . . . . . . . . . . . . . . . . . . . . . . . . . . 21
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 23
viii Contents
5 Livetin Fractions (IgY)
RÜDIGERSCHADEANDPABLOANIBALCHACANA . . . . . . . . . . . . . . . . . . . . . . . . . . 25
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 25
2 Alpha-Livetin. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 25
3 Beta-Livetin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 26
4 Gamma-Livetin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 26
4.1 Molecular Structure of Chicken IgY. . . . . . . . . . . . . . . . . . . . . . . . . . 26
4.2 Biological Function of IgY. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 27
4.2.1 Transfer from Maternal Blood to Egg Yolk. . . . . . . . . . . . . . . 28
4.2.2 Transfer from Yolk Sac to Embryonic Circulation. . . . . . . . . 29
4.3 IgY Extraction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 30
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 31
Subpart Ib Egg White Compounds
6 Lysozyme
GRZEGORZLESNIEROWSKIANDJACEKKIJOWSKI . . . . . . . . . . . . . . . . . . . . . . . . . . . 33
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 33
2 Characteristics of Lysozyme. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 33
3 Antimicrobial Activity of Lysozyme. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 35
4 Methods of Lysozyme Isolation. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 37
5 Lysozyme Polymeric Forms . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 38
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 40
7 Ovotransferrin
FABIANASUPERTI, MARIAGRAZIAAMMENDOLIA, FRANCESCABERLUTTI
ANDPIERAVALENTI . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 43
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 43
2 Composition. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 43
3 Purification and Structure . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 44
4 Antimicrobial and Antiviral Activity. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 46
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 48
8 Ovalbumin and Gene-Related Proteins
VALÉRIELECHEVALIER, THOMASCROGUENNEC, FRANÇOISENAU
ANDCATHERINEGUÉRIN-DUBIARD . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 51
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 51
2 Ovalbumin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 51
2.1 Amino Acid Sequence and Structure. . . . . . . . . . . . . . . . . . . . . . . . . 51
2.2 Ovalbumin Function . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 54
3 S-Ovalbumin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 55
4 Ovalbumin Gene Y. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 56
5 Ovalbumin-Related Y Protein. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 56
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 57
Contents ix
9 Ovomucin
JAAKKOHIIDENHOVI . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 61
1 Ovomucin–a Gelling Agent of Egg White . . . . . . . . . . . . . . . . . . . . . . . . . . 61
2 Chemical and Physical Properties of Ovomucin. . . . . . . . . . . . . . . . . . . . . 62
3 Isolation and Purification of Ovomucin . . . . . . . . . . . . . . . . . . . . . . . . . . . 63
3.1 Isoelectric Precipitation Method . . . . . . . . . . . . . . . . . . . . . . . . . . . . 63
3.2 Chromatographic Methods. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 64
3.3 Other Methods. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 65
4 Future Trends—Biological Roles of Ovomucin . . . . . . . . . . . . . . . . . . . . . 65
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 66
10 Riboflavin-Binding Protein (Flavoprotein)
THOMASCROGUENNEC, CATHERINEGUÉRIN-DUBIARD
ANDFRANÇOISENAU . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 69
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 69
2 Composition and Structure. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 69
3 Synthesis. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 72
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 73
11 Avidin
FRANÇOISENAU, CATHERINEGUÉRIN-DUBIARD
ANDTHOMASCROGUENNEC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 75
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 75
2 Physiochemical Characteristics . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 75
3 Structure and Interactions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 76
4 Extraction and Purification. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 77
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 78
12 Proteases
SOPHIERÉHAULT . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 81
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 81
2 Glutamyl Aminopeptidase (EAP). . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 82
3 Methionine-Preferring Broad Specificity Aminopeptidase (MAP). . . . . . 82
4 Others. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 83
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 83
13 Antiproteases
SOPHIERÉHAULT . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85
2 Ovostatin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 86
3 Ovomucoid. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 87
4 Ovoinhibitor. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 88
5 Chicken Cystatin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 89
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 89
x Contents
14 Minor Proteins
CATHERINEGUÉRIN-DUBIARDANDFRANÇOISENAU . . . . . . . . . . . . . . . . . . . . . . . . 93
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 93
2 Lipocalins. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 93
2.1 Extracellular Fatty Acid Binding Protein (Ex-FABP). . . . . . . . . . . . 94
2.2 Chondrogenesis Associated Lipocalin Gamma (CAL gamma) . . . . 94
2.3 Ovoglycoprotein. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 95
3 Clusterin. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 95
4 HEP21. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 95
5 Tenp . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 96
6 Vitelline Membrane Outer Protein 1 (VMO1) . . . . . . . . . . . . . . . . . . . . . . 96
7 Conclusion. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 97
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 97
Subpart Ic Egg Shell Compounds
15 Structure and Formation of the Eggshell
YVESNYSANDJOËLGAUTRON . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 99
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 99
2 Structure of the Eggshell. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 99
3 Eggshell Formation. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 101
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 102
16 Eggshell Matrix Proteins
JOËLGAUTRONANDYVESNYS . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 103
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 103
2 Egg White Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 104
3 Ubiquitous Proteins. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 104
4 Proteins Unique to the Eggshell. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 105
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 106
17 Function of Eggshell Matrix Proteins
JOËLGAUTRONANDYVESNYS . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 109
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 109
2 Eggshell Matrix Proteins and Calcification Process. . . . . . . . . . . . . . . . . . 109
2.1 Calcium Binding Proteins. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 110
2.2 In vitro Interaction with Mineral Phase. . . . . . . . . . . . . . . . . . . . . . . 110
2.3 In vivo Relationships Between Eggshell Matrix
and Eggshell Quality . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 111
2.4 Genomic Approach . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 112
3 Antibacterial Activities of Eggshell Matrix Proteins. . . . . . . . . . . . . . . . . . 112
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 113
Contents xi
Part II Use of Egg Compounds for Human Nutrition
ROSINALOPÉZ-FANDIN˜O
18 Nutritional Evaluation of Egg Compounds
INGRIDSEUSS-BAUM . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 117
1 The Problem with the Egg. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 117
2 Nutritional Value of Eggs. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 117
2.1 Nutrient Content per 100 g or per Portion . . . . . . . . . . . . . . . . . . . . 117
2.2 Nutrient Content Expressed as Percentage of RDI. . . . . . . . . . . . . . 125
2.3 Nutrient Profile . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 129
3 Importance of Nutrients in Eggs for Human Nutrition. . . . . . . . . . . . . . . 129
3.1 Macronutrients. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 129
3.1.1 Protein. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 129
3.1.2 Fat . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 132
3.1.3 Carbohydrates. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 134
3.2 Micronutrients. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 134
3.2.1 Vitamins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 134
3.2.2 Minerals. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 135
4 Bioavailability of Nutrients from Eggs. . . . . . . . . . . . . . . . . . . . . . . . . . . . . 136
5 Enrichment and Fortification of Nutrients in Eggs . . . . . . . . . . . . . . . . . . 137
6 Conclusions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 140
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 140
19 Concepts of Hypoallergenicity
YOSHINORIMINEANDMARIEYANG . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 145
1 Introduction. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 145
2 Food Allergy Overview . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 146
2.1 Molecular Aspects of Food Allergy. . . . . . . . . . . . . . . . . . . . . . . . . . . 146
2.2 Molecular Properties of the Major Egg Allergens. . . . . . . . . . . . . . . 146
2.3 Role of Glycosylation in Protein Allergenicity . . . . . . . . . . . . . . . . . 148
3 Concept of Hypoallergenicity. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 148
3.1 Development of Hypoallergenic Products via
Food Processing. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 148
3.1.1 Thermal Processing. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 149
3.1.2 Enzymatic Fragmentation . . . . . . . . . . . . . . . . . . . . . . . . . . . . 150
3.1.3 Other Food Processing Methods. . . . . . . . . . . . . . . . . . . . . . . . 150
3.2 Development of Hypoallergenic Products for
Immunotherapeutic Purposes. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 151
3.2.1 Full Recombinant Allergens. . . . . . . . . . . . . . . . . . . . . . . . . . . 151
3.2.2 Site-Directed Mutagenesis . . . . . . . . . . . . . . . . . . . . . . . . . . . . 152
3.2.3 Peptide-Based Immunotherapy . . . . . . . . . . . . . . . . . . . . . . . . 152
3.2.4 Production of Tolerance-Inducing Peptides . . . . . . . . . . . . . . 153
3.2.5 Blocking IgG-Inducing Peptides [Mimotope
(Mimotopes, Clayton, Australia) Immunotherapy] . . . . . . . . 153
3.2.6 Chemically Modified Allergens (Allergoids). . . . . . . . . . . . . . 154
References. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 155