Thermal analysis thermodynamic parameters determined using

Experimental studies concerning crystallization from W/O microemulsions use thermal analysis methods to characterize the microemulsions themselves, to determine thermodynamic parameters of crystallization, and to characterize the final products. A large number of studies are concerned with the state of water in ionic [109] and nonionic [110] W/O microemulsions. It has been shown that because of the close proximity of the interface, the properties of the water molecules are quite different from those of water in the bulk, and this difference in itself may have a profound effect on the solubilization and crystallization of solutes. The problem is discussed in detail in two other chapters (by Schulz et al. and by Garti et al.) in this book and will not be reiterated here. In this presentation we describe (1) calorimetric studies of the formation of nanosized inorganic crystallites and (2) the use of TG and DSC in the characterization of a water-soluble organic compound crystallized in a W/O microemulsion. 

In brief, a DSC instrument comprises two cells fixed in an adiabatic chamber. One cell contains the sample to be tested, the second cell contains a reference solution or an empty DSC pan. The adiabatic chamber is maintained under pressure to avoid the evaporation of the sample (Plum, 2009). A DSC-thermogram represents the plot of heat capacity difference ACp (between the sample and the reference) as a function of temperature. Thermodynamic parameters, such as T, AH and AS, could be determined by the DSC curve analysis. T is the temperature at which the concentration of denatured and native forms of the protein are equal. This specific temperature is also called the midpoint of the thermal transition. AH represents the enthalpy of thermal transition determined from the integration of the DSC curve. The entropy (AS) of the thermodynamic transition of the protein may be calculated from the integrated area under the curve of AC /T vs. T. The free energy (AG), which gives an indication of the protein stability, can also be determined at any temperature from the values of AH and AS (O Brien and Haq, 2004 Plum, 2009). Thermal and thermodynamic properties of proteins analyzed by DSC are greatly affected by the experimental conditions used, such as pH, salts, alcohols, and the presence of other food components (e.g., lipids, polysaccharides) (Grinberg et al, 2009). 

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