Thermostable Enzymes

 In general, enzyme thermostability is an intrinsic property, determined by the primary structure of the protein. However, external environmental factors including cations, substrates, co-enzymes, modulators, polyols and proteins often increase enzyme thermostability. With some exceptions, enzymes present in thermophiles are more stable than their mesophilic counterparts. Some organisms produce enzymes with different thermal stability properties when grown at lower and higher temperatures. There are commercial advantages in carrying out enzymic reactions at higher temperatures. Some industrial enzymes exhibit high thermostability. More stable forms of other industrial enzymes are eagerly being sought.   Enzyme-based processes promise a sustainable and environmentally-friendly solution to the pollution that results from industrial technologies. Thermozymes are extremely temperature-stable biocatalysts that broaden the application horizon of enzymes. Thermophiles and hyperthermophiles belonging to several genera viz. Bacillus, Clostridium, Pyrococcus, Thermus, Thermotoga, and Aquifex have been explored for thermozymes. Thermozymes, in addition to offering thermostability, are also equipped with properties such as solvent tolerance, resistance to denaturants, substrate-selectivity, and higher reaction rates; thus, making them potentially more suitable for applications as compared with mesozymes. Adaptive mechanisms of thermozymes include modifications in amino acid sequence/composition, hydrogen bonding patterns, electrostatic interactions, disulfide bonds, hydrophobic interactions, and metal binding ability, resulting in superior conformational structure. Investigation of thermostable biocatalysts could help simplify the molecular basis of stability, and may help in crafting designer enzymes via bioengineering and computational approaches. Such tailored biocatalysts may be candidates for potentially novel industrial process applications.  

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