| Literature DB >> 25531187 |
Hiroshi Yamaguchi1, Masaya Miyazaki.
Abstract
Active recombinant proteins are used for studying the biological functions of genes and for the development of therapeutic drugs. Overexpression of recombinant proteins in bacteria often results in the formation of inclusion bodies, which are protein aggregates with non-native conformations. Protein refolding is an important process for obtaining active recombinant proteins from inclusion bodies. However, the conventional refolding method of dialysis or dilution is time-consuming and recovered active protein yields are often low, and a cumbersome trial-and-error process is required to achieve success. To circumvent these difficulties, we used controllable diffusion through laminar flow in microchannels to regulate the denaturant concentration. This method largely aims at reducing protein aggregation during the refolding procedure. This Commentary introduces the principles of the protein refolding method using microfluidic chips and the advantage of our results as a tool for rapid and efficient recovery of active recombinant proteins from inclusion bodies.Entities:
Keywords: denatured protein; inclusion body; microfluidic chips; protein refolding; recombinant protein
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Year: 2015 PMID: 25531187 PMCID: PMC4601335 DOI: 10.4161/21655979.2014.987022
Source DB: PubMed Journal: Bioengineered ISSN: 2165-5979 Impact factor: 3.269