Refolding of recombinant proteins

Department of Chemical Engineering, Tufts University, Medford, MA 02155, USA
Current Opinion in Biotechnology (Impact Factor: 8.04). 05/1998; DOI: 10.1016/S0958-1669(98)80109-2

ABSTRACT Expression of recombinant proteins as inclusion bodies in bacteria is one of the most efficient ways to produce cloned proteins, as long as the inclusion body protein can be successfully refolded. Aggregation is the leading cause of decreased refolding yields. Developments during the past year have advanced our understanding of the mechanism of aggregation in in vitro protein folding. New additives to prevent aggregation have been added to a growing list. A wealth of literature on the role of chaperones and foldases in in vivo protein folding has triggered the development of new additives and processes that mimic chaperone activity vitro.

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    ABSTRACT: Despite the importance of recombinant protein production in academy and industrial fields, many issues concerning the expression of soluble and homogeneous product are still unsolved. Although several strategies were developed to overcome these obstacles, at present there is no magic bullet that can be applied for all cases. Indeed, several key expression parameters need to be evaluated for each protein. Among the different hosts for protein expression, Escherichia coli is by far the most widely used. In this chapter, we review many of the different tools employed to circumvent protein insolubility problems.
    Methods in molecular biology (Clifton, N.J.) 01/2015; 1258:27-44. · 1.29 Impact Factor
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    The Scientific World Journal 07/2014; Received 24 April 2014; Accepted 9 July 2014. · 1.73 Impact Factor
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    14th Asia Pacific Confederation of Chemical Engineering Congress; 01/2012


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