refolding of recombinant proteins
Recombinant protein expression in bacteria often results in the formation of both inactive and insoluble protein that accumulates as intracellularprotein aggregates called inclusion bodies [1]. It has beenshown that 70-80% of recombinant proteins expressed in E.coli are as inclusion bodies [2]. This is probably due to the independence of the protein type in bacterial systems. In cases of expression of eukaryotic proteins, which usually contain cysteines that are prone to form disulfide bonds in the nativestate, the bacterial system maynot support the appropriate pairing of disulfide bonds in the newly-produced protein thus leads to the presence of insoluble protein pellets [3].
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