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Non-Soluble Protein Producing in Inclusion Body

Many protein species produced in recombinant bacteria aggregate as insoluble protein clusters named inclusion bodies (IBs). Overexpression of cloned or synthetic genes in Escherichia coli often results in the formation of insoluble protein IBs. The expression of toxic proteins, such as membrane proteins (MPs), in soluble forms in vitro is a very challenging task, since high-level expression of recombinant proteins in E. coli often results in the formation of insoluble and inactive aggregates known as IBs.  However, the formation of IBs offers several advantages for the production of recombinant proteins: the recombinant protein deposited in IBs amounts to about 50% or more of the total cellular protein; IBs can be isolated from the cellular proteins by centrifugation, since they have a relatively high density. Furthermore, IBs have been found that (i) protein deposition in recombinant cells is fully reversible and (ii) a relevant fraction of IB proteins is actually functional.

Fig. 1 Electron micrograph of inclusion bodies containing recombinant adenylate kinase expressed in E. coli.