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Directed Evolution Method in Saccharomyces cerevisiae: Mutant Library Creation and Screening
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Published on: April 1, 2016

Development of new laccases by directed evolution: functional and computational analyses.

Giovanna Festa1, Flavia Autore, Franca Fraternali

  • 1Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Complesso Universitario Monte S. Angelo, via Cintia, 80126 Napoli, Italy.

Proteins
|January 12, 2008
PubMed
Summary

Researchers engineered fungal laccase enzymes using random mutagenesis. The best mutant, 3M7C, shows significantly increased activity and stability due to specific amino acid substitutions, advancing enzyme engineering for various applications.

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Area of Science:

  • Biotechnology
  • Enzyme Engineering
  • Molecular Biology

Background:

  • Laccases are multicopper oxidases with broad applications in industry.
  • Heterologous expression of Pleurotus ostreatus laccases in yeast is established.
  • Molecular evolution enables the creation of improved enzyme variants.

Purpose of the Study:

  • To generate and characterize improved fungal laccase variants through random mutagenesis.
  • To identify mutations enhancing both activity and stability.
  • To investigate structure-function relationships of engineered laccases.

Main Methods:

  • Random mutagenesis using error-prone PCR (EP-PCR) on poxc and poxa1b cDNAs.
  • Screening of large mutant libraries (1100 and 1200 clones).
  • Characterization of enzyme properties, including activity and stability.
  • Molecular dynamics simulations of wild-type and mutant enzyme models.

Main Results:

  • A single mutation (L112F) in mutant 1M9B increased activity but decreased stability.
  • A second-generation mutant, 3M7C, with mutations L112F and P494T, exhibited significantly enhanced stability and activity.
  • Molecular dynamics simulations provided insights into the structural basis for improved enzyme performance.

Conclusions:

  • Directed evolution can yield fungal laccase variants with superior properties.
  • Specific mutations, like P494T, can simultaneously enhance laccase activity and stability.
  • Understanding structure-function relationships guides the rational design of industrial enzymes.