Protein particles could enhance the stability of
dispersions. This review focused on the characteristics of protein particles
from different sources, their structural stability and the stability of
dispersions at different pH values. Whey protein, sodium caseinate and gelatin
particles were investigated. To create particles from these proteins,
controlled aggregation and gelation were used in several methods. As chemical
structures of these proteins are all different, their gelation properties also
vary. Whey proteins are globular, caseins have a random structure, and gelatin in
gelled form has triple helix structure. Whey proteins undergo thermal
denaturation above 68ᵒC, therefore heat-set gelatin was often used for particle
preparation. When whey protein particles were prepared at the iso-electric
point (IEP) of proteins, they became dense and small; whereas at other pH
values, particles were soft and spherical due to increased repulsive forces
between proteins. Such particles could swell when the pH of the aqueous phase
was away from the IEP. Sodium caseinate is more heat stable compared to whey
proteins; however it is pH-sensitive. When sodium caseinate particles were
prepared through acidification, particles were stable against disintegration
only around the IEP of proteins. More stable caseinate particles could be
produced using enzymatic crosslinking. On the other hand, gelatin particles,
which were prepared via cold-set gelation, were stable over a wide pH range;
however, as they were thermo-sensitive, particles disintegrated above 30ᵒC.
This review explained the chemical differences of proteins, preparation of
particles using different methods, and stability of particles and their
dispersions at different conditions.
aggregation gelatin microstructure sodium caseinate whey protein
Birincil Dil | İngilizce |
---|---|
Konular | Mühendislik |
Bölüm | Makaleler |
Yazarlar | |
Yayımlanma Tarihi | 27 Mart 2020 |
Yayımlandığı Sayı | Yıl 2020 Cilt: 16 Sayı: 1 |