Double Layer Immobilized Manganese Peroxidase from Effectively Enhanced the Biodecolorization of Remazol Brilliant Blue R Dye

The ability of white rot fungi to degrade lignin using relatively non-specific extracellular enzyme has encouraged the use of these fungi in decolorization processes of highly colored textile dye wastewaters. In this study, a manganese peroxidase (MnP) enzyme isolated from Pleurotus ostreatus was applied to decolorize Remazol Brilliant Blue R (RBBR), as a model of textile dye, using an immobilization form in Ca-alginate beads. The result showed that single layer immobilization of MnP decolorized only 32% of RBBR (100 ppm). However, double layer immobilized enzymes that placed the MnP in the inner layer of the bead and Mn2+, Tween80, and H2O2 as mediators in outer layer effectively enhanced the biodecolorization 2- fold compare than the single layer immobilization. MnP activity affected the decolorization yield of the RBBR with 4.5 U of MnP could decolorized the RBBR 70% in 10 h. In addition, application of the immobilized enzyme in bioreactor system improved the decolorization rate. This study is important for the further application of enzyme immobilization for decolorization of textile dye effluents. Paper Presented at The International Conference of Indonesia Forestry Researchers III. Bogor, 21-22 October 2015. Hal. 269-275