Abstract
The interaction between urea and guanidinium chloride (GuHCl) on lysozyme refolding was investigated in this work. Live micrococcus lysodeikticus was successfully introduced into a refolding system. Lysozyme can be refolded from the GuHCl-denatured, DTT-reduced state in a good yield of 96.54% at final protein concentration as high as 0.2 mg·mL−1. A model could be employed to elucidate refolding kinetics behavior and the kinetics constants were studied. In the coexistence of GuHCl and urea, the aggregation rate decreased by increasing urea concentration to a proper value. The cooperation of GuHCl and urea not only suppressed the competition of the aggregation reaction but also increased the yield of refolding efficiently.
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