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Enhanced refolding of lysozyme with imidazolium-based room temperature ionic liquids: Effect of hydrophobicity and sulfur residue
학술지 Science China, Chemistry, 55, 8, 1657-1662(2012)
저자명 Bae Sang-Woo, Chang Woo-Jin, Koo Yoon-Mo, Ha Sung Ho
The expression of recombinant proteins in microorganism frequently leads to the formation of insoluble aggregates, inclusion
bodies (IBs). Thus, the additional in vitro protein refolding process is required to convert inactive IBs into water-soluble active
proteins. This study investigated the effect of sulfur residue and hydrophobicity of imidazolium-based room temperature ionic
liquids (RTILs) on the refolding of lysozyme as a model protein in the batch dilution method which is the most commonly
used refolding method. When lysozyme was refolded in the refolding buffer containing [BF4]-based RTILs with a systematic
variety of alkyl chain on cations varying from two to eight, less hydrophobic imidazolium cations having shorter alkyl chains
were effective to facilitate lysozyme refolding. Compared to the conventional refolding buffer, 2 times higher lysozyme refolding
yield was obtained in 1-ethyl-3-methylimidazolium tetrafluoroborate ([EMIM][BF4]) containing refolding buffer. The
refolding yield of lysozyme was even more increased by 2.5 times when 1-butyl-3-methylimidazolium methylsulfate
([BMIM][MS]) containing sulfur residue on anion was used. The sulfur residue in [BMIM][MS] is supposed to improve the
refolding yield of lysozyme which has 4 intramolecular disulfide bonds. For dilution-based refolding of lysozyme, the optimum
concentrations of RTILs in refolding buffer were found to be 1.0 M [EMIM][BF4] and 0.5 M [BMIM][MS], respectively.
The optimum temperate for dilution-based refolding of lysozyme with RTILs was 4 °C.
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