Development and optimization of a silica-bound laccase biocatalyst and its application in hospital wastewater treatment.

Laccase from Trametes hirsuta was immobilized on amino-functionalized silica by adsorption and covalent binding using glutaraldehyde (GLA) and glyoxal (GLX) as cross-linkers. The immobilization process was optimized applying the Box-Behnken methodology. The immobilized biocatalysts were characterized using scanning electron microscopy, Brunauer-Emmett-Teller surface area and Barrett-Joyner-Halenda pore size analyses, and elemental analysis.

Characterization of laccases from Trametes hirsuta in the context of bioremediation of wastewater treatment plant effluent.

The bioremediation of pharmaceutical compounds contained in wastewater, in an ecological and sustainable way, is possible via the oxidative action of fungal laccases. The discovery of new fungal laccases with unique physico-chemical characteristics pushes researchers to identify suitable laccases for specific applications. The aim of this study is to purify and characterize laccase isoenzymes produced from the Trametes hirsuta IBB450 strain for the bioremediation of pharmaceutical compounds.