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A new kinetic scheme for lysozyme refolding and aggregation.

A Mark Buswell1, Anton P J Middelberg

  • 1Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA United Kingdom. antonm@cheng.cam.ac.uk

Biotechnology and Bioengineering
|June 27, 2003
PubMed
Summary

A new kinetic model accurately predicts lysozyme refolding in fed-batch processes by accounting for rapid aggregation and sequential mechanisms, improving protein production yields.

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Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Protein Science

Background:

  • Traditional kinetic models fail to predict lysozyme refolding in fed-batch cultures.
  • Existing models do not account for complex aggregation pathways or variations in chemical composition.

Purpose of the Study:

  • To develop and validate a new kinetic model for lysozyme refolding in fed-batch processes.
  • To improve the prediction accuracy of protein refolding yields.

Main Methods:

  • Proposed a novel kinetic scheme incorporating rapid partitioning and sequential aggregation.
  • Utilized stopped-flow light-scattering to measure aggregation rates.
  • Determined refolding rate constants via batch experiments as "snapshots" of fed-batch conditions.

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Main Results:

  • The new kinetic scheme accurately predicted fed-batch lysozyme refolding performance.
  • The model accounts for monomeric lysozyme aggregation in various states, including native.
  • Experimental evidence supports native protein incorporation into aggregates, explaining yield reduction.

Conclusions:

  • The proposed kinetic model offers a superior approach for predicting fed-batch protein refolding.
  • Understanding aggregation mechanisms is crucial for optimizing recombinant protein production.
  • This work provides a framework for enhancing bioprocess yields through improved kinetic modeling.