Strategies for Expression of Soluble Heterologous Proteins in Escherichia coli

Escherichia coli has long been the primary expression system for the synthesis of heterologous proteins, but its utility is limited because many heterologous proteins are either prone to be degraded by the cellular proteases or to accumulate in insoluble form, typically as inclusion bodies. This paper reviews recent advances in the strategies for expression soluble heterologous proteins in Escherichia coli so as to improve the recovery yield of heterologous gene products in a biologically active form.