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Cited by 251

The DOI matches its Crossref record; 67 of the 67 references it cites were found in a registry or an index.

Refolding Techniques for Recovering Biologically Active Recombinant Proteins from Inclusion Bodies

Yamaguchi, Hiroshi, Miyazaki, Masaya·2014·Biomolecules
DOI 10.3390/biom4010235
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Abstract

Biologically active proteins are useful for studying the biological functions of genes and for the development of therapeutic drugs and biomaterials in a biotechnology industry. Overexpression of recombinant proteins in bacteria, such as Escherichia coli, often results in the formation of inclusion bodies, which are protein aggregates with non-native conformations. As inclusion bodies contain relatively pure and intact proteins, protein refolding is an important process to obtain active recombinant proteins from inclusion bodies. However, conventional refolding methods, such as dialysis and dilution, are time consuming and, often, recovered yields of active proteins are low, and a trial-and-error process is required to achieve success. Recently, several approaches have been reported to refold these aggregated proteins into an active form. The strategies largely aim at reducing protein aggregation during the refolding procedure. This review focuses on protein refolding techniques using chemical additives and laminar flow in microfluidic chips for the efficient recovery of active proteins from inclusion bodies.

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Cites

Research works printed but not linked: 2

  1. Zhi, 1992, Renaturation of citrate synthase: Influence of denaturant and folding assistants, Protein Sci., 1, 522, 10.1002/pro.5560010407 · DOI
  2. Nian, 2009, Synergistic coordination of polyethylene glycol with ClpB/DnaKJE bichaperone for refolding of heat-denatured malate dehydrogenase, Biotechnol. Prog., 25, 1078, 10.1002/btpr.175 · DOI

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Metadata

Authors
Yamaguchi, H., & Miyazaki, M.
Venue
Biomolecules
Publisher
MDPI AG
Published
2014-02-20
Volume
4
Issue
1
Pages
235-251
ISSN
2218-273X
DOI
10.3390/biom4010235
Cited by
251
References
67
Language
en
Licence
creativecommons.org/licenses/by/3.0/ (vor)

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