Many recombinant proteins partially aggregate into inclusion bodies during production in
Escherichia coli in batch culture on defined medium. Production on complex medium …

Recombinant proteins produced in Escherichia coli hosts may appear within the cells'
cytoplasm in form of insoluble inclusion bodies (IB's) and/or as dissolved functional protein …

Production of recombinant proteins is an industrially important technique in the
biopharmaceutical sector. Many recombinant proteins are problematic to generate in a …

Escherichia coli has been most extensively used for the large-scale production of
therapeutic proteins, which do not require complex glycosylation for bioactivity. In recent …

Methyl α‐glucoside (α‐MG) is a metabolically inert glucose analog sharing the same
phosphotransferase system with glucose. The potential of using this compound, which acts …

The production of the fusion protein staphylococcal protein A/E. coli β-galactosidase in
Escherichia coli was studied in batch and fed batch cultivations. Batch cultivation of a …

The effect of changes in substrate feed rate during fedbatch cultivation was investigated with
respect to soluble protein formation and transport of product to the periplasm in Escherichia …

State of the art microbial recombinant protein production is regularly performed in fed-batch
based cultivations. However, these cultivations suffer from highly time-dependent changes …

During production in recombinant Escherichia coli, the human basic fibroblast growth factor
(hFGF-2) partly aggregates into stable cytoplasmic inclusion bodies. These inclusion bodies …

Proteins that contain disulfide bonds mainly mature in the oxidative environment of the
eukaryotic endoplasmic reticulum or the periplasm of Gram-negative bacteria. In E. coli …