Fast and high-level expression of heterologous proteins in bacterial hosts often results in the
accumulation of almost pure aggregates (inclusion bodies, IBs) of the target protein …

Overexpression of recombinant proteins in E. coli often results in formation of insoluble,
inactive inclusion bodies. These inclusion bodies, which contain the recombinant proteins in …

The overexpression of recombinant proteins in Escherichia coli leads in most cases to their
accumulation in the form of insoluble aggregates referred to as inclusion bodies (IBs). To …

The vast majority of protein purification is now done with cloned, recombinant proteins
expressed in a suitable host. The predominant host is Escherichia coli. Many, if not most …

Escherichia coli is widely used for the expression of recombinant proteins that do not require
glycosylation for their bioactivity (1, 2). Many commercially available recombinant hormones …

The production of recombinant proteins in a large scale is important for protein functional
and structural studies, particularly by using Escherichia coli over-expression systems; …

Inclusion bodies produced in Escherichia coli are composed of densely packed denatured
protein molecules in the form of particles. Refolding of inclusion body proteins into bioactive …

Recombinant proteins are widely used in industry (pharmaceutical, chemical, food,
cosmetics…), research and diagnostics; therefore, interest in their production is increasing …

Throughout the twenty-first century, the view on inclusion bodies (IBs) has shifted from
undesired by-products towards a targeted production strategy for recombinant proteins …

Since inclusion bodies (IBs) contain an important amount of properly folded and active
proteins, their solubilization using nondenaturing conditions to obtain aggregation-prone …