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 …

Escherichia coli has been most widely used for production of the recombinant proteins. Over-
expression of the recombinant proteins is the mainspring of the inclusion bodies formation …

Expression of heterologous proteins in E. coli often leads to the formation of protein
aggregates known as inclusion bodies (IBs). Inclusion body aggregates pose a major hurdle …

The functional analysis of individual proteins or of multiprotein complexes—since the
completion of several genome sequencing projects—is in focus of current scientific work …

Background In recent years, it has been gradually realized that bacterial inclusion bodies
(IBs) could be biologically active. In particular, several proteins including green fluorescent …

Proteome profiling of the inclusion body (IB) fraction of recombinant proteins produced in
Escherichia coli suggested that two small heat shock proteins, IbpA and IbpB, are the major …

Disulfide bonds occurred in majority of secreted protein. Formation of correct disulfide bonds
are must for achieving native conformation, solubility and activity. Production of recombinant …

The bacterium Escherichia coli is a major host for recombinant protein production of non-
glycosylated products. Depending on the expression strategy, the recombinant protein can …

High‐level expression of many recombinant proteins in Escherichia coli leads to the
formation of highly aggregated protein commonly referred to as inclusion bodies. Inclusion …

Recombinant protein production in bacteria is often accompanied by the formation of
aggregates, known as inclusion bodies (IBs). Although several strategies have been …