Abstract
In this study, horseradish peroxidase (HRP) was covalently immobilized on the calcium-alginate support using glutaraldehyde (GA) as a cross-linking reagent for detoxification and degradation of synthetic dyes. Immobilization procedure furnished significant immobilization efficiency (86.27 ± 3.43%) along with apparent and relative activity of 24.39 ± 1.03 U/g and 84.97 ± 3.54%, respectively, for immobilized-HRP. In comparison to free-state, immobilized-HRP catalyzed the substrate oxidation reaction in a slightly acidic and wider temperature range, with an optimum at 60 °C. After 10 and 60 min of incubation at 60 °C, the immobilized-HRP displayed 99.0% and 89.0% of residual activities, whereas the free counterpart retained only 34.0% and 18.0% of residual activities, respectively. Moreover, the immobilized-HRP showed potential efficiency for the decolorization of dyes in sequential dye-decolorizing batch reactions. Cytotoxicity analysis using a plant bioassay and acute test demonstrated that the Ca-alginate immobilized-HRP may effectively be used for detoxification of dyes and has a great potential for large-scale environmental remediation.
•A novel type of horseradish peroxidase (HRP) was isolated from horseradish roots.•The enhanced biocatalytic potential of immobilized-HRP was recorded.•Maximal dye degradation and detoxification were recorded.