The thermal behavior ofΒ-lactoglobulin (Β-lg) disperesed in distilled water (pH=3.2) is studied dy differential scanning calorimetry (DSC) in the temperature range 20‡C–120‡C and within a concentration region of 3.5% to 24%.
Crystallization of fat droplets in complex emulsions, which differed only by the initial structure of proteins, was studied by differential scanning calorimetry, before and after application of a whipping process. Upon cooling at 5 or 1°C min–1, the temperature needed to initiate fat crystallization was lower, and one more distinguishable crystallization peak was detected in emulsions containing caseins, in comparison with the emulsion containing pure whey proteins. Furthermore, the whipping process was accompanied by more protein depletion from the fat droplet surface, less resistance to coalescence, and a lower supercooling effect in the emulsion based on pure whey proteins.
Three types of wheat were submitted to two different milling procedures, giving rise to six flours which differed by some physico-chemical characteristics such as particle size, level of damaged starch and protein content. Differential scanning calorimetry was used for monitoring heat-induced structural changes in flour aqueous dispersions 80% water and in doughs 45% water. Differences between the thermal behaviour of the flour dispersions and doughs were explained mainly by differences in protein content. This result was confirmed after partial substitution of flour by gluten. Dynamic mechanical analysis performed at 20°C on the flour doughs indicated, as expected, a linear increase in the elastic modulus with increasing protein content. The results did not bring any evidence that, under these experimental conditions, starch damage might affect gluten hydration.
Authors:A. Kamyshny, P. Relkin, S. Lagerge, S. Partyka, and S. Magdassi
Differential scanning calorimetry (DSC) and isothermal calorimetric batch technique were used to monitor the heat-induced structural changes and adsorption properties of human immunoglobulin G (IgG), in native and hydrophobized states. The transition temperature (Tmax) and enthalpy of heat-induced conformational changes (
calH) of IgG in solution as well as the enthalpy change accompanying the adsorption of IgG onto hydrophilic silica (
adsH), were shown to depend on the degree of the protein hydrophobicity (number of covalently attached alkyl chains). The adsorption enthalpy for all forms of IgG at all surface concentrations was found to be endothermic, that is the process is entropy driven. Factors affecting the IgG adsorption onto silica are discussed.