Abstract
The recombinant minichaperone sht GroEL191-345 was cultivated in a 3.7 L stirred bioreactor with the high yield of 216.2 mg / L broth. In the refolding of recombinant human interferon gamma (rhuIFN-γ) inclusion bodies, more than 2-3 fold enhancement in protein mass recovery and total activity were observed in the presence of free or immobilized minichaperone to the refolding buffer.
Keywords: minichaperone, sht groel191-345, cultivation, purification, refolding, recombinant human interferon gamma
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