Concepedia

Publication | Closed Access

Laccases: A Useful Group of Oxidoreductive Enzymes

814

Citations

182

References

1999

Year

TLDR

Laccases, oxidoreductive enzymes mainly produced by wood‑rotting fungi but also by plants and bacteria, are widely employed to decontaminate phenol‑polluted environments, transform lignin, and in diverse applications such as beverage processing, analytical tools, and biosensors, owing to their broad substrate specificity and variable kinetic properties. Production of laccases is enhanced by protein‑synthesis inducers and recent advances in fungal molecular and cellular engineering, which have markedly increased industrial recombinant yields.

Abstract

Using enzymes as decontaminating agents has received great attention. One of the most promising groups of enzymes, laccases, are used to decontaminate phenol-polluted systems and for bio technological applications. Higher plants and fungi, mostly wood-rotting fungi, are the main producers of laccases, but bacterial laccases also have been found. Belonging to the class of phenoloxidases, laccases catalyze the polymerization of several phenolic substances to polymeric products. In addition, they have transformed lignin and lignin-related compounds, showing a very broad substrate specificity. Specific compounds acting as protein-synthesis inducers historically have been used to improve the production of the enzyme. Recent success in fungal molecular and cellular engineering technology has contributed to significantly increase the industrial production of recombinant laccase. Kinetic (Michaelis-Menten parameters, optimum pH, kcat) and stability properties of laccases may vary according to the source of the enzymes. Laccases are used in a variety of applications, such as to remove toxic compounds from aquatic and terrestrial systems, to produce and treat beverages, as analytical tools, and as biosensors to estimate the quantity of phenols in natural juices or the presence of other enzymes. Laccases have been used successfully in immobilized form as well as dissolved in organic solvents.

References

YearCitations

Page 1