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Laccase: new functions for an old enzyme.

Alfred M Mayer1, Richard C Staples

  • 1Department of Botany, The Hebrew University of Jerusalem, Jerusalem 91904, Israel. mayer@vms.huji.ac.il

Phytochemistry
|July 20, 2002
PubMed
Summary

Laccase enzymes, found in fungi and plants, have diverse physiological roles and industrial applications. Recent research highlights their utility in bioremediation, ethanol production, and understanding enzyme diversity.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Mycology

Background:

  • Laccases are copper-containing oxidases widely distributed in fungi, with less frequent characterization in higher plants.
  • Reports on laccase molecular weights, pH optima, and substrate specificity show significant diversity.
  • Definitive identification requires demonstrating quinol oxidation with oxygen uptake.

Purpose of the Study:

  • To review recent findings on laccase occurrence and functions in physiological development.
  • To explore the industrial utility and diverse applications of laccase enzymes.
  • To synthesize current research on laccase enzymology and its wide applicability.

Main Methods:

  • Literature review of recent reports on laccase occurrence and functions.
  • Analysis of diverse laccase characteristics including molecular weight, pH optima, and substrate specificity.
  • Examination of established and emerging industrial and bioremediation applications.

Main Results:

  • Laccase plays roles in fungal spore pigmentation, tobacco protoplast regeneration, and as fungal virulence factors.
  • Enzymes are involved in lignification of plant cell walls and delignification in wood decay.
  • Industrial uses include wood delignification, ethanol production, and drug differentiation (morphine/codeine).

Conclusions:

  • Laccases exhibit remarkable functional diversity across physiological and industrial contexts.
  • Bioremediation processes extensively utilize laccases for environmental protection against industrial effluents.
  • Intense recent research is driven by the broad diversity, utility, and intriguing enzymology of laccases.

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