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Rational engineering of enzyme stability.

Vincent G H Eijsink1, Alexandra Bjørk, Sigrid Gåseidnes

  • 1Department of Chemistry, Biotechnology and Food Science, Agricultural University of Norway, PO Box 5040, N-1432 As. vincent.eijsink@ikbm.nlh.no

Journal of Biotechnology
|September 24, 2004
PubMed
Summary

Protein engineering strategies, including rational design and directed evolution, enhance protein stability. Understanding thermal inactivation mechanisms is key for efficient enzyme stabilization, differentiating laboratory from industrial applications.

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Area of Science:

  • Protein Engineering and Biocatalysis
  • Molecular Biology and Biochemistry

Background:

  • Extensive research over 15 years has focused on stabilizing proteins through mutations.
  • Studies range from rational design of small enzymes to directed evolution and characterization of hyperstable proteins.

Purpose of the Study:

  • To review and synthesize strategies for rational protein stabilization.
  • To highlight recent developments in understanding protein stability, including surface contributions and the distinction between laboratory and industrial stability.

Main Methods:

  • Review of published reports on protein stabilization via mutations.
  • Analysis of rational design approaches (e.g., proline introduction, disulfide bridges).
  • Consideration of directed evolution findings and characterization of hyperstable proteins.

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Main Results:

  • Various mutational strategies can significantly increase protein stability, some defying easy rationalization.
  • Protein surface properties are increasingly recognized as critical for stability.
  • A limited number of mutations can lead to substantial stability gains.

Conclusions:

  • A fundamental difference exists between reversible laboratory stability and irreversible industrial stability (e.g., aggregation).
  • Rational enzyme stabilization is achievable with sufficient knowledge of thermal inactivation mechanisms.