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Protein refolding for industrial processes.

E D Clark1

  • 1Department of Chemical and Biological Engineering, Tufts University, Medford, MA 02155, USA. eliana.clark@tufts.edu

Current Opinion in Biotechnology
|April 5, 2001
PubMed
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Inclusion body refolding is crucial for recombinant protein production. New methods using less denaturants and high hydrostatic pressure improve renaturation yields and reduce costs for industrial applications.

Area of Science:

  • Biotechnology
  • Protein Chemistry
  • Bioprocess Engineering

Background:

  • Inclusion bodies are aggregates of misfolded recombinant proteins.
  • Efficient refolding of inclusion bodies is essential for industrial protein production.
  • Current refolding methods often require high denaturant concentrations and are costly.

Purpose of the Study:

  • To explore novel strategies for improving inclusion body refolding processes.
  • To minimize protein aggregation during renaturation.
  • To reduce the chemical costs associated with recombinant protein production.

Main Methods:

  • Investigated solubilization methods avoiding high denaturant concentrations.
  • Utilized high hydrostatic pressure for simultaneous solubilization and renaturation.

Related Experiment Videos

  • Assessed refolding yields and aggregation levels.

    • Main Results:

    • Developed innovative solubilization techniques reducing reliance on high denaturants.
    • Demonstrated high hydrostatic pressure as an effective tool for combined solubilization and refolding.
    • Achieved improved renaturation yields with minimized aggregation.

    Conclusions:

    • Novel inclusion body refolding strategies show promise for industrial applications.
    • Reducing denaturant use and employing high hydrostatic pressure can enhance efficiency and lower costs.
    • These advancements are key to the successful large-scale production of recombinant proteins.