Strategies for soluble expression of recombinant protein in Escherichia coli

Many recombinant proteins fail to fold into native state with activity when expressed in Escherichia coli,instead,they often misfold and are easy to accumulate as inclusion bodies.Correctly folded recombinant proteins with activity have been obtained through many efficient strategies which include optimization of growing conditions,co-expression of folding modulators,gene fusion expression and so on.Strategies for the solution of the problems in the expression of soluble and bioactive recombinant proteins are discussed in the review.