Lacasa

Articulo: Pleurotus 2004.

Laccase is widespread in nature and has been found in plants, fungi,
bacteria and insects [1] . Laccase is a major enzyme in fungal ligninolytic systems
involved in lignin degradation [2]
.
Recent studies have indicated that laccases have overlapping substrate specificity, and
this substrate specificity can be extended to non-phenolic subunits using redox
mediators. Laccase plays an important role in the global carbon cycle and could help in
degrading a wide range of xenoaromatics such as textile dyes [3].
Dyes are designed to be resistant to light, water and oxidizing agents, so they are
difficult to degrade once released into aquatic systems [4]. For example, synthetic dyes
are not susceptible to decomposition by activated sludge in a conventional aerobic
process, aerobic bacterial strains screened
for dye decolorization often show a strict ability on a spe-
cific dye structure
[5]
. In recent years, white-rot fungus have
attracted increasing attention, as their ligninolytic enzymes
have the ability to degrade recalcitrant compounds and syn-
thetic dyes.
Although the molecular properties and gene sequences
of the laccase from white-rot fungi
Pleurotus ostreatus
as well as their purification have been described
articulo: Tekere
The white rot fungi are by far
the most efficient ligninolytic organisms described to date.
This capability to degrade lignin is due to the extracellular
nonspecific and nonstereoselective enzyme system. The ex-
tracellular enzyme system involved in lignin degradation is
composed of lignin peroxidases, laccases and manganese-
dependent peroxidases as well as hydrogen producing oxi-
dases [1–3]. The same unique nonspecific mechanisms that
give these fungi the ability to degrade lignin also allow them
to degrade a wide range of pollutants and they possess a
number of advantages not associated with other bioreme-
diation systems [4,5].

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