Thermostability

The thermal stability in chemistry and in particular organic and biochemistry the property of a compound to withstand relatively high temperatures (molecular heat resistance ). The opposite of the thermal stability, the thermal lability.

Properties

This thermal stability refers primarily to the structure of the molecule, but also defines application- specific about the ability to perform a particular function. The term is mainly applied to biomolecules and particularly protein structures, since proteins often lose their ability to function due to the denaturation at comparatively low temperatures. As in process technology but higher temperatures a higher metabolic rate allow ( RGT rule) and these are necessary for other reasons, in order to obtain a desired reaction product, the thermostable biomolecules here comes a high importance. An example of this is the polymerase chain reaction, can be used in the thermostable DNA polymerases from organisms such as Thermus aquaticus. Organisms which have a high temperature due to their optimum heat-stable structures are called thermophilic. Thermostable proteins have the additional stabilizing their protein folding often each other, a compact structure and increased hydrogen bonding, salt bridges, hydrolysis less sensitive amino acids and relatively high affinity of the monomers of a protein complex.

Since, in particular protein -based toxins are often heat- labile toxins are divided into heat-stable and heat- labile toxins. While thermolabile toxins as some lectins are inactivated by heating through heat-stable toxins such amatoxins this treatment without major losses. This has particular significance for the effect of cooking of toxic in the raw food ( eg potatoes, beans, lentils and some fungi).

Thermal disinfection methods are based on overcoming the heat stability of the proteins of pathogens.