Related Experiment Video
Updated: May 30, 2026

05:19
Optimized Production and Analysis of Recombinant Protein-Filled Vesicles from E. coli
Published on: June 30, 2023
Recombinant protein production by in vivo polymer inclusion display
Katrin Grage1, Verena Peters, Bernd H A Rehm
1Institute of Molecular BioSciences, Massey University, Palmerston North, New Zealand.
Applied and Environmental Microbiology
|August 2, 2011
Abstract:
A novel approach to produce purified recombinant proteins was established. The target protein is produced as polyhydroxyalkanoate (PHA) synthase fusion protein, which mediates intracellular formation of PHA inclusions displaying the target protein. After isolation of the PHA inclusions, the pure target protein was released by simple enterokinase digestion.
Related Concept Videos
Production of Pharmaceuticals
Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...
Recombinant DNA
Overview
Tagging and Fusion Proteins
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

