원문정보
초록
영어
Over-expressed recombinant protein produced by E. coli often creates inclusion bodies (IBs). Thus, protein refolding process is needed to convert these IBs into active forms. Recently, hydrophobic interaction chromatography (HIC) has been introduced as one of the potential methods for protein refolding since hydrophobic interaction is the dominant force in protein folding and structure stabilization. The ionic strength of mobile phase and hydrophobicity of the
adsorbent are the most important factors affecting the refolding efficiency and mass recovery of the active protein in HIC-based refolding process. This study presents the effects of salt concentrations in mobile phase and the adsorbent hydrophobicity on protein recovery and refolding yields. The butyl residue was the best among tested functional groups of the Sepharose HIC adsorbent. The optimum concentration of ammonium sulfate for adsorption and desorption of unfolded and refolded lysozyme was 1.0 mol/L and 0.4 mol/L, respectively.
Moreover, the optimum gradient strategy for refolding and desorption of bound protein was also investigated using 8 mol/L urea solution.