Enhanced removal of phenol from biorefinery wastewater treatment using enzymatic and Fenton process.

The valorisation of biomass has been commonly carried out in biorefineries. The environmental concerns about these processes have not been intensely considered, demanding further investigations. Particularly, phenols are founded in high concentrations in biorefinery wastewater and are considered compounds of major concern. In this study, we evaluated the bioconversion of phenols by enzymatic treatment using the enzyme Horseradish peroxidase (HRP) and the Fenton process. The results showed an enzymatic phenol conversion of 97.5% at pH 7.0, enzyme activity of 0.8 U/mL and hydrogen peroxide concentration of 1.61 g/L. So as to enhance the treatment, we evaluate the Fenton reaction as a complementary process for further remaining phenol conversion. The best conditions for Fenton process were achieved using a hydrogen peroxide concentration and [H2O2]:[Fe] ratio of 3.90 g/L and 74, respectively, and the obtained phenol concentration in the treated wastewater was 0.11 mg/L. Chromatography analysis showed that 2-methoxyphenol was the majority compound in the original wastewater, which was subsequently precipitated by the enzymatic treatment. Furthermore, many physicochemical parameters were modified due to the treatment, such as biochemical oxygen demand, chemical oxygen demand and total organic carbon, with removal efficiencies of around 97, 49 and 46%, respectively. HRP combined with Fenton can be considered as an alternative methodology for the biorefinery wastewater treatment, especially regarding the phenols conversion.

Immobilization of laccase from Aspergillus oryzae on graphene nanosheets.

Laccase enzymes of Aspergillus oryzae were immobilized on graphene nanosheets by physical adsorption and covalent bonding. Morphological features of the graphene sheets were characterized via microscopy techniques. The immobilization by adsorption was carried out through contact between graphene and solution of laccase enzyme dissolved in deionized water. The adsorption process followed a Freundlich model, showing no tendency to saturation within the range of values used. The process of immobilization by covalent bonding was carried out by nitration of graphene, followed by reduction of sodium borohydride and crosslinking with glutaraldehyde. The process of immobilization by both techniques increased the pH range of activity of the laccase enzyme compared to the free enzyme and increased its operating temperature. On operational stability, the enzyme quickly loses its activity after the second reaction cycle when immobilized via physical adsorption, while the technique by covalent bonding retained around 80% activity after six cycles.