원문정보
초록
영어
High expression levels of recombinant protein in Escherichia coli often result in the formation of micro-scale particles of aggregated protein, called 'inclusion bodies (IBs)'. A chromatographic protein refolding technology is receiving more and more attention as a convenient technique to improve refolding yields and to increase the concentration of refolded proteins. In this study, the cyclodextrin glucanotransferase (CGTase) from Bacillus macerans was refolded from initial
high protein concentrations. The optimum washing and refolding condition from preparation of IBs to refolding of CGTase was determined. The IBs were washed by three different buffers. The addition of 1.5 M urea in refolding buffer gave 1.5 fold improved refolding yield of CGTase in batch dilution method. Moreover, the mass recovery and refolding yield of CGTase was enhanced with
increased ionic strength of refolding buffer by addition of NaCl. Then we have investigated the effect of the different pore size of size-exclusion resins on the activity and mass recovery yield.