Enhanced bio-catalytic performance and dye degradation potential of chitosan-encapsulated horseradish peroxidase in a packed bed reactor system

In this study, horseradish peroxidase (HRP) was immobilized onto chitosan beads by entrapment method and employed for the degradation of textile dyes. Stable and firm quality chitosan beads developed with 2.5% chitosan concentration exhibited maximum immobilization yield (similar to 92.54 +/- 2.53%). The pH optimum of chitosan-immobilized HRP (CTS-HRP) was marginally displaced towards alkaline region (pH 7.5) than that of F-HRP which displayed its optimum activity at pH 7.0. The free HRP (F-HRP) and CTS-HRP enzyme presented their maximum catalytic activities at 30 degrees C and 70 degrees C, respectively. Relative activities of F-HRP and CTS-HRP were decreased following pre-incubation above 30 degrees C and 50 degrees C, respectively and after 120 min at 70 degrees C, the F-HRP, and CTS-HRP retained 19.3 +/- 1.3 and 48.3 +/- 2.4% activities, accordingly. The CTS-HRP exhibited remarkably better resistance towards heavy metal induced activity inhibition. The effect of potential inhibitors on the activity of F-HRP and CTS-HRP was investigated and found that CTS-HRP was significantly less vulnerable to the denaturation caused by urea, ethylenediaminetetraacetic acid (EDTA), cysteine, 1, 4-dithiothreitol and Triton X-100. Moreover, the CTS-assisted entrapped-HRP was also employed for the decolorization of four different textile dyes i.e. Remazol Brilliant Blue R (RBBR), Reactive Black 5 (RB5), Congo Red (CR) and Crystal Violet (CV). The CTS-HRP showed considerable decolorization efficacy in six consecutive batch operations. Results suggest that CTS-HRP is an attractive choice for use as industrial biocatalyst in larger scale bioremediation of textile dyes and effluents. (C) 2016 Elsevier B.V. All rights reserved.