Recombinant proteins are becoming increasingly important for industrial applications, where
Escherichia coli is the most widely used bacterial host for their production. However, the …

Formation of inclusion bodies in bacterial hosts poses a major challenge for large scale
recovery of bioactive proteins. The process of obtaining bioactive protein from inclusion …

Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

Antibodies and antibody-derived molecules are continuously developed as both therapeutic
agents and key reagents for advanced diagnostic investigations. Their application in these …

Bacterial inclusion bodies (IBs) are functional, non-toxic amyloids occurring in recombinant
bacteria showing analogies with secretory granules of the mammalian endocrine system …

Inclusion bodies (IBs) often emerge upon overexpression of recombinant proteins in E. coli.
From IBs, refolding is necessary to generate the native protein that can be further purified to …

Understanding the structure, functionalities and biology of functional amyloids is an issue of
emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria …

The expression of correctly folded and functional heterologous proteins is important in many
biotechnological production processes, whether it is enzymes, biopharmaceuticals or …

Enzymes are used as biocatalysts in a vast range of industrial applications. Immobilization of
enzymes to solid supports or their self-assembly into insoluble particles enhances their …

The formation of inclusion bodies (IBs) constitute a frequent event during the production of
heterologous proteins in bacterial hosts. Although the mechanisms leading to their formation …