Immobilization process improves the enzyme properties, like stability, activity, selectivity or specificity. In the study, a novel cysteine-functionalized MxOy (ZrO2, SiO2) material was used as a support for the immobilization of laccase from Trametes versicolor. The proposed matrix was prepared using a simple sol-gel method. The cysteine was introduced during the synthesis of a sample. Additionally, the obtained supports were modified with glutaraldehyde. The basic properties of the prepared cysteine functionalized ZrO2 and SiO2 were determined using spectroscopic, thermal, porous, electrostatic and elemental analysis. Furthermore, the obtained biocatalytic systems were used as catalysts in the oxidation of sulfonic acid. Catalytic and kinetic parameters were determined based on the proposed model reaction. Next, laccase immobilized on ZrO2- and SiO2-based materials were, for the first time, utilized in the decolorization of Alizarin Red S. In that process, the influence of duration, pH and temperature on the efficiency of decolorization was evaluated. The results show that the proposed biocatalytic systems offer good specific activity (ca. 19 U/mg) and activity retention (ca. 77%). Importantly, they can be successfully used in the decolorization of Alizarin Red S with high efficiency (above 95%).
Efficient synthesis of butyl levulinate from furfuryl alcohol over ordered mesoporous Ti-KIT-6 catalysts for green chemistry applications