Protein refolding is still a bottleneck for large-scale production of valuable proteins
expressed as inclusion bodies in Escherichia coli. Usually biologically active proteins …

Protein refolding at high concentrations always leads to aggregation, which limits
commercial application. An ion-exchange chromatography process with gradient changes in …

Column-based protein refolding requires a continuous processing capability if reasonable
quantities of protein are to be produced. A popular column-based method, size-exclusion …

A size-exclusion chromatography-based refolding process (SEPROS) has successfully been
used to renature lysozyme at high concentrations. This process is based on the different …

A new method to improve refolding yields and to increase the concentration of refolded
proteins in a single operation has been developed. The method uses size‐exclusion …

A refolding chromatography with immobilized molecular chaperonin GroEL was studied for
the reactivation of denatured-reduced lysozyme. The effect of denaturant concentration …

In vitro protein refolding is still a bottleneck in both structural biology and in the development
of new biopharmaceuticals, especially for commercially important polypeptides that are …

A mechanism for size-exclusion chromatography-based protein refolding is described. The
model considers the steps of loading the denatured protein onto a gel filtration column, and …

The presence of inclusion body impurities can affect the refolding yield of recombinant
proteins, thus there is a need to purify inclusion bodies prior to refolding. We have compared …

To avoid the intrinsic problem of aggregation associated with the traditional solution-phase
refolding process, we proposed a solid-phase refolding method integrated with the …