Physical, Morphological, and Rheological Properties of Agglomerated Milk Protein Isolate Powders: Effect of Binder
Yulim Jeong1, Byoungseung Yoo1
1Department of Food Science and Biotechnology, Dongguk University-Seoul, Goyang 410-820, Republic of Korea.
Abstract:
Milk protein isolate powder (MPIP), a high protein-based powder, is a common dietary ingredient but has poor physical properties due to its cohesive nature. Powder agglomeration is one of the most widely used methods to improve and modify the quality of MPIP structures. In this study, the physical, morphological, and rheological properties of MPIPs agglomerated in a fluidized-bed agglomeration process were investigated as a function of sugar binder type and concentration. The physical properties of MPIP were evaluated by their flowability, cohesiveness, porosity, particle size distribution (PSD), and water-holding properties (wettability, solubility, and water-binding capacity). The density values of the agglomerated MPIPs decreased with increasing the binder concentration, whereas the porosity, wettability, and solubility values increased. Such trends were consistent with SEM observations. The MPIP agglomerated with 10% sorbitol had the largest particle diameter (D50) and showed better physical properties compared to the other sugar binders. The viscosity values (ηa,50) of the MPIPs agglomerated with sugar binders showed lower values than the control (no sugar binder). The agglomeration process enhanced the viscoelasticity of the MPIP, but the viscoelasticity decreased with increasing the sugar binder concentration. These observations suggested that the physical, morphological, and rheological properties of MPIP can be greatly affected by the binder type and concentration in the agglomeration process.
More Related Videos
Related Concept Videos
Factors Influencing Drug Absorption: Pharmaceutical Parameters
Bonding and Strength of Aggregate
Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism
Some polymorphic crystals possess lower aqueous solubility than their amorphous counterparts, leading to incomplete absorption. For instance, the oral suspension of Chloramphenicol, which...
Factors Affecting Protein-Drug Binding: Drug-Related Factors
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In...
Factors Affecting Protein-Drug Binding: Protein-Related Factors
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...


