pH-Dependent Behavior and Stability of Protein-Based Particles in Aqueous Media
Makaleler > Tam Makale · 2019
Yazarlar: İnce Coşkun, Alev Emine, Özgül ÖZDESTAN OCAK, Buğra OCAK, Semih ÖTLEŞ
DergiPark (Istanbul University), Uluslararası, 2019
Özet
This review focused on the characteristics of protein particles from different sources, namely whey proteins, sodium caseinate and gelatin, their structural stability and the stability of dispersions at different pH values.To create particles, controlled aggregation and gelation were used in several methods.Different chemical structures of the proteins provide different gelation properties.Whey proteins undergo thermal denaturation above 68 ᵒ C, 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 pHsensitive.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 30 ᵒ C.This review explained the chemical differences of proteins, preparation of particles using different methods, and stability of particles and their dispersions at different conditions.Such differences in protein particles should be carefully investigated before they are used in food products, which could have complex matrix.