earticle

영어

Recombinant protein is often produce by E.coli in the form of inclusion bodies (IBs). IBs are densed particle of proteins and do not have activity as protein. To convert IBs into water-soluble active protein, the refolding process is required. Ionic liquids (ILs) are organic salts composed of anion and cation, and the salts that do not crystallize at room temperature are called room temperature ionic liquids (RTILs) in particular. Tunable hydrophobicity and polarity of RTILs leads the expansion of its application in chemical and biological processes. In this study, we investigated how the hydrophobicity of RTILs affects protein refolding efficiency. Especially
the effect of N-alkyl-N’-methylimidazolium methylsulfate having sulfur in anion part of ILs on target protein having the disulfide bond during refolding process. As the alkyl chain length increased the refolding efficiency generally decreased. In addition, we found that N-alkyl-N’-
methylimidazolium methylsulfate is only effective as refolding additive when the target protein contain disulfide bond.