A study on the effect of CspA expression on the productivity of recombinant protein at low temperature
2009
Kim, S.H., Pusan National University, Busan, Republic of Korea | Heo, M.A., Pusan National University, Busan, Republic of Korea | Lee, S.G., Pusan National University, Busan, Republic of Korea
One of the major drawbacks associated with the high-level expression of the recombinant proteins in Escherichia coli is the formation of insoluble inclusion bodies in the cytoplasm. Production of recombinant protein at reduced temperature has proven effective in improving the solubility of a number of structurally and functionally unrelated proteins, but a major limitation of using low temperatures for recombinant protein production in E. coli is the reduced rate of synthesis of the heterologous protein caused by the significant reduction of cell growth rate. Here we investigated the effect of co-expression of CspA, a cold-shock protein known to be RNA chaperone at low temperature, on the productivity of recombinant protein at various temperatures by using green fluorescence protein (GFP) as a model recombinant protein. We could observe that the co-expression of CspA enhanced the productivity of GFP at 15℃ by accelerating the growth of E. coli at the temperature. On the other hand, the CspA coexpression didn't affect the cell growth rate as well as the specific GFP production rate at other tested temperatures, 20℃, 25℃, and 37℃.
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