Phase transitions. DSC and DTA are routinely used in the food industry to characterize phase transitions in foods, e.g. crystallization, melting, glass transitions and conformational changes. They can be used to provide information about the temperature at which transitions occur (Ttr), the enthalpy change associated with a transition (DHtr), the type of transition involved (exothermic or endothermic), and the quantify of material that undergoes a transition. As an example, we will consider the use of DSC to study the melting and crystallization of food components. When a material changes its physical state from solid-to-liquid (melting) or from liquid-to-solid (crystallization) it absorbs or gives out heat, respectively. A process that absorbs heat is an endothermic process, whereas a process that evolves heat is an exothermic process. Pure substances usually have very sharp melting or crystallization points and therefore all the heat is absorbed or evolved over a narrow range of temperatures, leading to a sharp DSC or DTA peak. Many food components are chemically complex materials and therefore the phase transitions occur over a wide range of temperatures, e.g. edible oils contain a wide variety of different triacylglycerols each with its own melting point. Peaks from food oils may also be complicated by the fact that triacylglycerols can crystallize in more than one different crystalline structure, i.e., they are polymorphic.
Molecular interactions. ITC can be used to provide valuable information about interactions between different types of molecules, e.g., binding interactions or conformational changes. As an example, we will consider the use of ITC for quantifying the binding of a ligand molecule (L) to a protein molecule (P): P + L ® PL. A solution containing the ligand is placed into the injector, while a solution containing the protein is placed into the sample cell. Small aliquots of the ligand solution are then injected into the sample solution at regular intervals (e.g., 10 mL every 300 seconds). The interval between each injection should be long enough to allow any reactions to go to completion. The instrument records the enthalpy change that occurs after each injection as a result of the interaction between the ligand and protein molecules. By measuring the change in the enthalpy with ligand concentration in the sample cell it is possible to obtain information about the number of binding sites on the protein, the strength of the binding interaction and the thermodynamics of the binding interaction.
Phase transitions. DSC and DTA are routinely used in the food industry to characterize phase transitions in foods, e.g. crystallization, melting, glass transitions and conformational changes. They can be used to provide information about the temperature at which transitions occur (Ttr), the enthalpy change associated with a transition (DHtr), the type of transition involved (exothermic or endothermic), and the quantify of material that undergoes a transition. As an example, we will consider the use of DSC to study the melting and crystallization of food components. When a material changes its physical state from solid-to-liquid (melting) or from liquid-to-solid (crystallization) it absorbs or gives out heat, respectively. A process that absorbs heat is an endothermic process, whereas a process that evolves heat is an exothermic process. Pure substances usually have very sharp melting or crystallization points and therefore all the heat is absorbed or evolved over a narrow range of temperatures, leading to a sharp DSC or DTA peak. Many food components are chemically complex materials and therefore the phase transitions occur over a wide range of temperatures, e.g. edible oils contain a wide variety of different triacylglycerols each with its own melting point. Peaks from food oils may also be complicated by the fact that triacylglycerols can crystallize in more than one different crystalline structure, i.e., they are polymorphic.Molecular interactions. ITC can be used to provide valuable information about interactions between different types of molecules, e.g., binding interactions or conformational changes. As an example, we will consider the use of ITC for quantifying the binding of a ligand molecule (L) to a protein molecule (P): P + L ® PL. A solution containing the ligand is placed into the injector, while a solution containing the protein is placed into the sample cell. Small aliquots of the ligand solution are then injected into the sample solution at regular intervals (e.g., 10 mL every 300 seconds). The interval between each injection should be long enough to allow any reactions to go to completion. The instrument records the enthalpy change that occurs after each injection as a result of the interaction between the ligand and protein molecules. By measuring the change in the enthalpy with ligand concentration in the sample cell it is possible to obtain information about the number of binding sites on the protein, the strength of the binding interaction and the thermodynamics of the binding interaction.
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