Abstract
We have succeeded in the efficient refolding of denatured carbonic anhydrase B (CAB) using reversed micelles formulated with nonionic surfactant. The reversed micelles with nonionic tetraethylene glycol dodecyl ether prevented denatured CAB from aggregation in the refolding process, allowing a refolding yield of over 70% in 20 h, while the refolding yield of CAB with AOT/isooctane reversed micelle was only about 5%. These results demonstrated that the reversed micelles-mediated protein refolding technique could be extended to the protein which has strong interaction with AOT by simply altering the type of surfactant.
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