Rational Design to Improve Protein Thermostability: Recent Advances and Prospects

Abstract Research on proteins is in rapid development, but the use of wild‐type proteins under industrial conditions has limitations, low thermostability in particular. Thermal stability includes three types: thermodynamic, kinetic, and process stability. Several factors (e.g., hydrophobic interactions and hydrogen bonds) affect the thermostability of proteins. The use of rational design to improve protein thermal stability is a hot topic in the field of computational biology and protein engineering. Several methods have been applied successfully to improve the thermal stability of protein, including introducing the number of disulfide bonds, optimizing protein surface charge, homologous comparison, and optimizing the free energy of unfolding. This review summarizes recent advances in our understanding of the factors influencing protein thermostability, highlights its effective improvement strategies, and discusses future prospects in this field.