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Environmental Science and Pollution Research

, Volume 24, Issue 8, pp 7035–7041 | Cite as

Bio-based degradation of emerging endocrine-disrupting and dye-based pollutants using cross-linked enzyme aggregates

  • Muhammad Bilal
  • Muhammad Asgher
  • Hafiz M. N. IqbalEmail author
  • Hongbo Hu
  • Xuehong Zhang
Research Article

Abstract

In this study, manganese peroxidase (MnP) from an indigenous white-rot fungus Ganoderma lucidum IBL-05 was insolubilized in the form of cross-linked enzyme aggregates (CLEAs) using various aggregating agents, i.e., acetone, ammonium sulfate, ethanol, 2-propanol, and tert-butanol, followed by glutaraldehyde (GA) cross-linking. The precipitant type, MnP, and GA concentrations affected the CLEAs activity recovery and aggregation yield. Among precipitants used, acetone appeared to be the most efficient aggregation agent, providing the highest activity recovery and aggregation yield of 31.26 and 73.46%, respectively. Optimal cross-linking was noticed using 2.0% (v/v) GA and 8:1 (v/v) MnP to GA ratio at 3.0 h cross-linking time under continuous agitation at 4 °C. The highest recovered activity and aggregation yield were determined to be 47.57 and 81.26%, respectively. The MnP-CLEAs, thus synthesized, were tested to investigate their bio-catalytic capacity for removing two known endocrine-disrupting chemicals (EDCs), e.g., nonylphenol and triclosan in a packed bed reactor system. The insolubilized MnP efficiently catalyzed the biodegradation of both EDCs, transforming over 80% in the presence of MnP-based system. A maximal of 100% decolorization was recorded for Sitara textile (SIT-based) effluent, followed by 95.5% for Crescent textile (CRT-based) effluent, 88.0% for K&N textile (KIT-based) effluent, and 84.2% for Nishat textile (NIT-based) effluent.

Keywords

Cross-linked enzyme aggregates Insolubilization Catalytic activity Endocrine disrupting chemicals Biodegradation 

Notes

Acknowledgements

The present study was a part of a research project focused on the development of ligninolytic enzymes for industrial applications. The financial support provided by the Higher Education Commission, Islamabad, Pakistan is thankfully acknowledged. The authors are also grateful to the State Key Laboratory of Microbial Metabolism, and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, 200240 Shanghai, China for providing technical and analytical help.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2017

Authors and Affiliations

  • Muhammad Bilal
    • 1
    • 2
  • Muhammad Asgher
    • 1
  • Hafiz M. N. Iqbal
    • 3
    Email author
  • Hongbo Hu
    • 2
  • Xuehong Zhang
    • 2
  1. 1.Industrial Biotechnology Laboratory, Department of BiochemistryUniversity of AgricultureFaisalabadPakistan
  2. 2.State Key Laboratory of Microbial Metabolism, and School of Life Sciences and BiotechnologyShanghai Jiao Tong UniversityShanghaiChina
  3. 3.ENCIT—Science, Engineering and Technology School, Tecnologico de MonterreyMonterreyMexico

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