Abstract

Escherichia coli has been most widely used for the production of various recombinant proteins and asit has been far better characterized than any other microorganism in every aspects. Overexpressionof recombinant proteins results in a rapid stress response and changes in the metabolism of E. coli[3]. These cellular responses may lead to plasmid instability, ribosome destruction, growth inhibitionor even cell lysis, all of which negatively a ect recombinant protein production. The yield of arecombinant protein is generally proportional to both the nal cell density and the speci c proteinproductivity. Therefore, various strategies have been developed for cultivating E. coli to high densitiesand/or optimizing expression systems for increased speci c protein productivity.Proteome pro ling is a systematic and powerful tool for understanding physiological changes andfor developing metabolic and cellular engineering strategies. In this study, we studied overexpressionof a human leptin in E. coli and used proteomics to design a better bioprocess to achieve increasedleptin yield.

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