Decolorization of Textile Dyes by Extracellular Enzymes Produced from Trametes sanguinea and Perenniporia taephropora Immobilized on Natural Media

Siriorn Boonyawanich, Nipon Pisutpaisal and Saowaluck Haosagul

Decolorization of Textile Dyes by Extracellular Enzymes Produced from Trametes sanguinea and Perenniporia taephropora Immobilized on Natural Media

2024

Siriorn Boonyawanich, Nipon Pisutpaisal and Saowaluck Haosagul

The color of textile wastewater is still a main problem in wastewater treatment by biological processes. The colored effluents from textile factories usually exceed effluent standards. Therefore, various innovations were developed to treat textile wastewater for decolorization in the effluents. This research aims to decolorize textile wastewater by immobilizing white rot fungi degradation. At first, the 11 fungal stains were tested to find the decolorized efficiency then the high decolorized efficiency fungal stains were immobilized on four material media, namely water hyacinth stalks, coconut husk, corn cob, and loofah. After that, the immobilized fungi were cultivated in the culture media at 30, 60, and 120 C/N ratios, respectively. The results showed that Trametes sanguinea and Perenniporia tephropora were two stains with a high decolorized efficiency of 68.8% and 67.5% respectively, and the decolorized efficiency was increased when immobilized on loofahs and fed with 120 C/N ratio medium. In a comparison of two fungal stains, P. tephropora was found more suitable for the decolorization of textile wastewater than T. sanguinea because T. sanguinea could produce red-orange pigments that induced the colored enhancement in wastewater over time. Finally, immobilized P. tephropora was cultivated in a 120 C/N ratio medium within a 10 L continuous stirred tank reactor (8 L working volume) to investigate the decolorized efficiency, enzymatic activity, and repeated batch. It was found that three repeated cycles were carried out by reusing the immobilized P. tephropora and the highest decolorized efficiency was 63.4%. The enzymatic activity of laccase, manganese peroxidase, and lignin peroxidase was 15.5 U/L, 85.9 U/L, and 0 U/L, respectively

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