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Proteins are biomolecules of great importance in the biochemical processes such as the med‐ ical, pharmaceutical, and food fields, since they exhibit their outstanding biological activities under mild condition. However, most of proteins dissolved in an aqueous solution are im‐ mediately denatured and inactivated at high temperatures due to the disruption of weak in‐ teractions including ionic interactions, hydrogen bonds, and hydrophobic interactions, which are prime determinants of protein tertiary structures [5-3]. In particular, protein ag‐ gregation easily occurs upon the exposure of the hydrophobic parts of proteins, which are usually located in the inside of native proteins, and this phenomenon becomes the major problem because of the fast irreversible inactivation. Thermal denaturation of proteins is a serious problem not only in the separation and storage of proteins but also in the processes of biotransformation, biosensing, drug production, and food manufacturing. Several strat‐ egies have so far been proposed in order to prevent thermal denaturation of proteins [4-14]. They include chemical modification, immobilization, genetic modification, and addition of stabilizing agents. The addition of stabilizing agents is one of the most convenient methods for minimizing thermal denaturation, compared to other methods. It has been reported that inorganic salts, polyols, sugars, amino acids, amino acid derivatives, chaotropic reagents, and water-miscible organic solvents are available for improving protein stability. However, these additives do not sufficiently prevent irreversible protein aggregation or some of them are no longer stable at high temperatures.

Increase in Thermal Stability of Proteins by Aprotic Ionic Liquids