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 …

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 …

Protein aggregation results in β-sheet–like assemblies that adopt either a variety of
amorphous morphologies or ordered amyloid-like structures. These differences in structure …

The purpose of this work was to construct a consensus prediction algorithm of 'aggregation-
prone'peptides in globular proteins, combining existing tools. This allows comparison of the …

Amyloids are highly abundant in many microbial biofilms and may play an important role in
their architecture. Nevertheless, little is known of the amyloid proteins. We report the …

Different species of microorganisms including yeasts, filamentous fungi and bacteria have
been used in the past 25 years for the controlled production of foreign proteins of scientific …

A common limitation of recombinant protein production in bacteria is the formation of
insoluble protein aggregates known as inclusion bodies. The propensity of a given protein to …

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

Protein aggregation is a major bottleneck during the bacterial production of recombinant
proteins. In general, the induction of gene expression at sub‐optimal growth temperatures …