Inclusion bodies produced in Escherichia coli are composed of densely packed denatured
protein molecules in the form of particles. Refolding of inclusion body proteins into bioactive …

Among the various expression systems employed for the over-production of proteins,
bacteria still remains the favorite choice of a Protein Biochemist. However, even today, due …

Recent advances in generating active proteins through refolding of bacterial inclusion body
proteins are summarized in conjunction with a short overview on inclusion body isolation …

Ever since lysozyme was discovered by Fleming in 1922, this protein has emerged as a
model for investigations on protein structure and function. Over the years, several high …

The rapid provision of purified native protein underpins both structural biology and the
development of new biopharmaceuticals. The dominance of Escherichia coli as a cellular …

Bioseparation processes are dominated by chromatographic steps. Even primary recovery is
sometimes accomplished by chromatographic separation, using a fluidized bed instead of a …

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 …

In laboratories and manufacturing settings, a rapid and inexpensive method for the
preparation of a target protein is crucial for promoting resesrach in protein science and …

Monomethoxypoly (ethylene glycol)-b-poly (dl-lactide) copolymer (PELA) microparticles
loading lysozyme were prepared through a modified W/O/W double emulsion-solvent …

The release of sequence data, particularly from a number of medically and
biotechnologically important genomes, is increasing in an exponential fashion. In light of …