| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5792278 | Meat Science | 2012 | 8 Pages |
Bovine plasma proteins provide the needed amino acids for the growth and development of an organism. With the purpose of preserving the native structure, related with the protein functional properties, the oligosaccharide inulin was used as protective agent and was compared with glucose and sucrose, during freeze-drying. In the present study, the thermal stability of protein was investigated as a function of type of saccharide in a concentration range of 5-15% (w/v), and at different pHs. The effect of these variables on phase transition, thermal stability and miscibility was assessed by differential scanning calorimetry (DSC) and scanning electron microscopy (SEM). The results of thermal protein properties (denaturation temperature and enthalpy), demonstrated that endothermic transition shifted to higher temperatures, being the stabilizing effect: inulin > glucose > sucrose. The thermal behavior suggests compatibility or interactions between the components of blends. In this way, the micrographs showed a homogeneous distribution of the different phases, corroborating the miscibility in the matrix. The unfolding process was irreversible and could be adequately described by a two-state model.
⺠Different protective agents of plasma proteins during freeze-drying were compared. ⺠The study by DSC demonstrated that the stabilizing effect was inulin > glucose > sucrose. ⺠The SEM micrographs corroborates the miscibility protein-polysaccharide. ⺠The protein unfolding was irreversible and was interpreted by a theoretical model. ⺠The product can be employed as functional ingredient for food formulation.
