Thermostabilization of proteins
1991
Gupta, M.N.
Enhancement of thermal stability is beneficial for most of the applications of enzymes/proteins. Whereas, heating at moderate temperatures for short duration may lead to reversible unfolding of the protein molecule, higher temperatures and longer time period ultimately lead to irreversible inactivation. The latter may involve a number of processes such as aggregation, peptide bond hydrolysis, deamidation of asparagine residues, formation of "scrambled" structures with or without disulfide exchange reactions and dissociation of prosthetic group. High thermal stability of enzymes from thermophilic organisms cannot be attributed to a single factor. Formation of more ion pairs, metal binding, glycosylation, increase in surface arginine residues, decrease in aspartic and asparagine residues and a stronger hydrophobic core are some of the important features which distinguish these enzymes. Various approaches which may be tried for thermostabilization of enzymes are: Addition of substances, chemical modification and cross-linking, immobilization, protein engineering, and change of medium to anhydrous organic solvents.
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