Laccase-conjugated thiolated chitosan-Fe3O4 hybrid composite for biocatalytic degradation of organic dyes


Ulu A., BİRHANLI E. , BORAN F. , KÖYTEPE S. , YEŞİLADA Ö. , ATEŞ B.

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, cilt.150, ss.871-884, 2020 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Cilt numarası: 150
  • Basım Tarihi: 2020
  • Doi Numarası: 10.1016/j.ijbiomac.2020.02.006
  • Dergi Adı: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
  • Sayfa Sayıları: ss.871-884

Özet

In this study, a novel immobilization support for laccase was developed to enhance enzyme stability, efficiency and reusability. Firstly, Fe3O4 magnetic particles were synthesized and modified by the co-precipitation route using thiolated chitosan (TCS). The support was characterized using several methods. Afterward, laccase was attached to the surface of functional support. The biochemical properties of the immobilized laccase were comprehensively investigated. It was observed that immobilized laccase achieved maximum activity at pH 4.0 and the optimum temperature was found to be 50 degrees C. After storage at +4 degrees C and similar to 25 degrees C for 4 weeks, the residual activity of the immobilized laccase was 87% and 80% of its initial activity, respectively. At 55 degrees C, the activity of immobilized lactase decreased to 73A% in 180 min and after reused 20 times, the relative activity of immobilized laccase still was approximately 50% of its initial activity. Moreover, the textile dye (Reactive Blue 171 and Acid Blue 74) decolorization activity of immobilized laccase was also tested and it showed long-term textile dye decolorization activity. These results are promising for the use of laccase in industrial and biotechnological applications. Therefore, this functionalized magnetic hybrid composite might be used to immobilize laccase, an industrially important enzyme. (C) 2020 Elsevier B.V. All rights reserved.