Enhanced refolding of lysozyme with imidazolium-based room temperature ionic liquids: Effect of hydrophobicity and sulfur residue

摘要: The expression of recombinant proteins in microorganism frequently leads to the formation insoluble aggregates, inclusion bodies (IBs). Thus, additional vitro protein refolding process is required convert inactive IBs into water-soluble active proteins. This study investigated effect sulfur residue and hydrophobicity imidazolium-based room temperature ionic liquids (RTILs) on lysozyme as a model batch dilution method which most commonly used method. When was refolded buffer containing [BF4]-based RTILs with systematic variety alkyl chain cations varying from two eight, less hydrophobic imidazolium having shorter chains were effective facilitate refolding. Compared conventional buffer, 2 times higher yield obtained 1-ethyl-3-methylimidazolium tetrafluoroborate ([EMIM][BF4]) buffer. even more increased by 2.5 when 1-butyl-3-methylimidazolium methylsulfate ([BMIM][MS]) anion used. [BMIM][MS] supposed improve has 4 intramolecular disulfide bonds. For dilution-based lysozyme, optimum concentrations found be 1.0 M [EMIM][BF4] 0.5 [BMIM][MS], respectively. temperate for °C.