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Rational design toward developing a more efficient laccase: Catalytic efficiency and selectivity.

Atefeh Khodakarami1, Negar Goodarzi1, Mahshideh Hoseinzadehdehkordi2

  • 1Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.

International Journal of Biological Macromolecules
|February 10, 2018
PubMed
Summary

Site-directed mutagenesis of Bacillus HR03 laccase improved enzyme efficiency and specificity. Key mutations enhanced catalytic efficiency for ABTS and increased thermal stability, demonstrating potential for improved biocatalysts.

Keywords:
Catalytic efficiencyLaccaseSpecificityThermal stability

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Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Engineering

Background:

  • Laccases are multicopper oxidases with diverse substrate oxidation capabilities.
  • Enzyme specificity and efficiency are critical for laccase applications.
  • Improving biocatalysts requires targeted modifications of enzyme structure.

Purpose of the Study:

  • To enhance the catalytic efficiency and specificity of laccase from Bacillus HR03 through site-directed mutagenesis.
  • To investigate the impact of mutations near the type 1 copper site on laccase activity and stability.
  • To characterize the kinetic and structural properties of engineered laccase variants.

Main Methods:

  • Site-directed mutagenesis was performed on Bacillus HR03 laccase, focusing on residues T415 and T418.
  • Kinetic parameters were determined using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and syringaldazine (SGZ) as substrates.
  • Circular dichroism (CD) and fluorescence spectroscopy were used to analyze secondary and tertiary structures of mutants.

Main Results:

  • Mutant T415I showed a 4-fold increase in catalytic efficiency for ABTS compared to the wild-type.
  • Variants T415I and T418I exhibited significantly enhanced specificity for ABTS over SGZ.
  • The T415I mutant demonstrated improved thermal stability, with a half-life of 60 minutes at 80°C.

Conclusions:

  • Targeted mutations in the substrate-binding pocket can effectively alter laccase specificity and efficiency.
  • Engineered laccase variants possess enhanced catalytic properties and thermal stability.
  • These findings provide a basis for developing improved laccase biocatalysts for industrial applications.