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Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins

Vallejo, Luis Felipe, Rinas, Ursula·2004·Microbial Cell Factories
DOI 10.1186/1475-2859-3-11
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Abstract

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 and solubilization procedures. In particular, the pros and cons of well-established robust refolding techniques such as direct dilution as well as less common ones such as diafiltration or chromatographic processes including size exclusion chromatography, matrix- or affinity-based techniques and hydrophobic interaction chromatography are discussed. Moreover, the effect of physical variables (temperature and pressure) as well as the presence of buffer additives on the refolding process is elucidated. In particular, the impact of protein stabilizing or destabilizing low- and high-molecular weight additives as well as micellar and liposomal systems on protein refolding is illustrated. Also, techniques mimicking the principles encountered during in vivo folding such as processes based on natural and artificial chaperones and propeptide-assisted protein refolding are presented. Moreover, the special requirements for the generation of disulfide bonded proteins and the specific problems and solutions, which arise during process integration are discussed. Finally, the different strategies are examined regarding their applicability for large-scale production processes or high-throughput screening procedures.

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Metadata

Authors
Vallejo, L. F., & Rinas, U.
Venue
Microbial Cell Factories
Publisher
Springer Science and Business Media LLC
Published
2004-09-02
Volume
3
Issue
1
ISSN
1475-2859
DOI
10.1186/1475-2859-3-11
Cited by
311
References
1
Language
en

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