2.6 Caseins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 74
2.7 Lactoferrin . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . .. . . . . . . . . . . . . . .. . . . . . . . . . . . . . . .. . . . . . . . . . . . . . .. 75
2.8 Lysozyme . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 75
3 Induced Assemblies of Food Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 76
3.1 Fibrils . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 76
3.2 Multistranded Ribbons and Spherulites . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 77
3.3 Particulate Aggregates . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 78
3.4 Nanotubes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 80
4 Spontaneous Assemblies of Food Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 81
4.1 Oppositely Charged Proteins and Polyelectrolytes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 82
4.2 Oppositely Charged Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85
5 Conclusion . . . . . . . . . . . . . . . . .. . . . . . . . . . . . . . .. . . . . . . . . . . . . . . .. . . . . . . . . . . . . . .. . . . . . . . . . . . . . . .. . . . . 93
References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 95
Abbreviations
α-La α-Lactalbumin
β-Lg β-Lactoglobulin
BSA Bovine serum albumin
Lf
Lactoferrin
LYS Lysozyme
Ova Ovalbumin
1 Introduction
Protein assembly in food science has been studied for long time because it contributes
to the characteristics and specific sensory properties of food. In the past decades,
improving knowledge on the mechanism of protein assembly has been responsible
for the design of specific but still limited numbers of supramolecular structures
(fibres, spheres, nanotubes, etc.) [1–5]. These structures could extend the functional
properties of proteins by the development of new sensory properties in food or the
encapsulation, protection and delivery of bioactives. Anyway, obtaining such
supramolecular structures from protein solutions tightens the evidence that proteins
constitute ideal building blocks for obtaining assemblies of various size and
architectures [6]. These supramolecular structures are not specific to one (or a
group of) protein(s) but are obtained from very distinct proteins, indicating that the
way that proteins assemble into supramolecular structures is a generic property of
proteins that is, de facto, independent of the amino acid composition of proteins [7].
In addition, one selected protein will self-assemble into various different supramolecular structures only by modifying the physicochemical conditions of the medium.
Hence, even if protein assembly follows universal mechanisms, the selection of the
physicochemical conditions of the medium, by affecting the rate of the different steps
occurring during protein assembly, influences the size, shape and characteristics
of the supramolecular structure formed (reactivity, internal structure, etc.); these
physicochemical conditions being specific to each protein system [8].
68
S. Bouhallab and T. Croguennec
2.7 Lactoferrin . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . .. . . . . . . . . . . . . . .. . . . . . . . . . . . . . . .. . . . . . . . . . . . . . .. 75
2.8 Lysozyme . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 75
3 Induced Assemblies of Food Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 76
3.1 Fibrils . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 76
3.2 Multistranded Ribbons and Spherulites . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 77
3.3 Particulate Aggregates . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 78
3.4 Nanotubes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 80
4 Spontaneous Assemblies of Food Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 81
4.1 Oppositely Charged Proteins and Polyelectrolytes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 82
4.2 Oppositely Charged Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 85
5 Conclusion . . . . . . . . . . . . . . . . .. . . . . . . . . . . . . . .. . . . . . . . . . . . . . . .. . . . . . . . . . . . . . .. . . . . . . . . . . . . . . .. . . . . 93
References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 95
Abbreviations
α-La α-Lactalbumin
β-Lg β-Lactoglobulin
BSA Bovine serum albumin
Lf
Lactoferrin
LYS Lysozyme
Ova Ovalbumin
1 Introduction
Protein assembly in food science has been studied for long time because it contributes
to the characteristics and specific sensory properties of food. In the past decades,
improving knowledge on the mechanism of protein assembly has been responsible
for the design of specific but still limited numbers of supramolecular structures
(fibres, spheres, nanotubes, etc.) [1–5]. These structures could extend the functional
properties of proteins by the development of new sensory properties in food or the
encapsulation, protection and delivery of bioactives. Anyway, obtaining such
supramolecular structures from protein solutions tightens the evidence that proteins
constitute ideal building blocks for obtaining assemblies of various size and
architectures [6]. These supramolecular structures are not specific to one (or a
group of) protein(s) but are obtained from very distinct proteins, indicating that the
way that proteins assemble into supramolecular structures is a generic property of
proteins that is, de facto, independent of the amino acid composition of proteins [7].
In addition, one selected protein will self-assemble into various different supramolecular structures only by modifying the physicochemical conditions of the medium.
Hence, even if protein assembly follows universal mechanisms, the selection of the
physicochemical conditions of the medium, by affecting the rate of the different steps
occurring during protein assembly, influences the size, shape and characteristics
of the supramolecular structure formed (reactivity, internal structure, etc.); these
physicochemical conditions being specific to each protein system [8].
68
S. Bouhallab and T. Croguennec