egg-white and milk whey, respectively [128, 129]. They suggest liquid–liquid phase
separation throughout cross-protein aggregation. Howell et al. [129] underlined the
strong dependence of such assembly between mixed native proteins on the physicochemical conditions of the medium. Assembly between LYS and β-Lg, but also
between LYS and α-La, were shown to be modulated by several physicochemical
parameters such as protein molar ratio, pH and ionic strength of the solution,
suggesting the involvement of electrostatic interactions between these proteins.
Working on egg-white proteins, Matsudomi et al. [128] showed that pre-denaturation
Individual
molecules
(2-3 nm)
Clusters
Aggregates
(0,1 – 10 µm)
Mix of two proteins with opposite charge
One protein or a mix of two proteins with the
same sign of net charge
1 M
0 M
0 M
1 M
Fig. 5 Illustration of how an increase in ionic strength affects protein self-assembly according to
the net charge of proteins at a given pH
Table 3 Self-assembly between oppositely charged food proteins and the shape of formed
supramolecular objects
Acidic, negatively
charged protein
Basic, positively
charged protein
Shape of formed
supramolecular structures References
Pre-denatured
ovalbumin
Lysozyme
Undetermined
[128]
Ovalbumin
Lysozyme
No self-assembly
[128]
Holo α-lactalbumin
Lysozyme
Undetermined
[129]
β-Lactoglobulin
Lysozyme
Undetermined
[129]
Succinylated
lysozyme
Native lysozyme
Undetermined
[130, 131]
Caseins
Lactoferrin
Coacervates
[132]
Gelatin B
Gelatin A
Coacervates
[133]
Holo α-lactalbumin
Lysozyme
No self-assembly
[3, 12, 134, 135]
Apo α-lactalbumin
Lysozyme
Amorphous aggregates
[3, 12, 134, 135]
Apo α-lactalbumin
Lysozyme
Microspheres
[3, 12, 134, 135]
Ovalbumin
Lysozyme
Microspheres
[5]
Ovalbumin
Avidin
Microspheres
[5]
BSA
Lysozyme
Microspheres
[5]
β-Lactoglobulin
Lactoferrin
Microspheres or
aggregates
Bouhallab et al.
(unpublished data)
β-Lactoglobulin
Lysozyme
Apo α-lactalbumin
Lactoferrin
86
S. Bouhallab and T. Croguennec