10.1007/s40089-017-0215-1

Laccase-conjugated amino-functionalized nanosilica for efficient degradation of Reactive Violet 1 dye

Show Details XML HTML PDF
  • Mayur Gahlout1,
  • Darshan M. Rudakiya1,
  • Shilpa Gupte2,
  • Akshaya Gupte*1,
  1. Department of Microbiology, Natubhai V. Patel College of Pure and Applied Sciences, Anand, Gujarat, 388 120, IN
  2. Ashok and Rita Patel Institute of Integrated Study and Research in Biotechnology and Allied Sciences, Anand, Gujarat, 388 121, IN
Cover Image

Published in Issue 2017-08-08

How to Cite

Gahlout, M., Rudakiya, D. M., Gupte, S., & Gupte, A. (2017). Laccase-conjugated amino-functionalized nanosilica for efficient degradation of Reactive Violet 1 dye. International Nano Letters, 7(3 (September 2017). https://doi.org/10.1007/s40089-017-0215-1
Crossref
Scopus
Google Scholar
Europe PMC

HTML views: 31

PDF views: 123

Abstract

Abstract Immobilization of enzyme with nanostructures enhances its ideal characteristics, which may allow the enzyme to become more stable and resistant. The present investigation deals with the formulation of laccase nanosilica conjugates to overcome the problems associated with its stability and reusability. Synthesized nanosilica and laccase nanoparticles were spherical shaped, with the mean size of 220 and 615 nm, respectively. Laccase nanoparticles had an optimum temperature of 55 °C and pH 4.0 for the oxidation of ABTS. Laccase nanoparticle retained 79% of residual activity till 20th cycle. It also showed 91% of its initial activity at lower temperatures even after 60 days. Laccase nanoparticles were applied for Reactive Violet 1 degradation wherein 96.76% of decolourization was obtained at pH 5.0 and 30 °C within 12 h. Toxicity studies on microbes and plants suggested that the degraded metabolites were less toxic than control dye. Thus, the method applied for immobilization increased storage stability and reusability of laccase, and therefore, it can be utilized for efficient degradation of azo dyes. Graphical Abstract

Keywords

  • Biocatalyst,
  • Ganoderma cupreum AG-1,
  • Laccase nanoparticle,
  • Nano-immobilization,
  • Reactive Violet 1
HTML PDF

References

  1. Rao et al. (2014) Enzymes as useful tools for environmental purposes (pp. 145-162) https://doi.org/10.1016/j.chemosphere.2013.12.059
  2. Avvakumova et al. (2014) Biotechnological approaches toward nanoparticle biofunctionalization (pp. 11-20) https://doi.org/10.1016/j.tibtech.2013.09.006
  3. Mukhopadhyay et al. (2015) Enhanced functionality and stabilization of a cold active laccase using nanotechnology based activation-immobilization (pp. 573-584) https://doi.org/10.1016/j.biortech.2014.12.070
  4. Lettera et al. (2016) Efficient immobilization of a fungal laccase and its exploitation in fruit juice clarification (pp. 1272-1278) https://doi.org/10.1016/j.foodchem.2015.10.074
  5. Cipolatti et al. (2014) Current status and trends in enzymatic nanoimmobilization (pp. 56-67) https://doi.org/10.1016/j.molcatb.2013.10.019
  6. da Costa et al. (2014) Bionanoconjugation for proteomics applications-an overview (pp. 952-970) https://doi.org/10.1016/j.biotechadv.2014.04.013
  7. Min and Yoo (2014) Recent progress in nanobiocatalysis for enzyme immobilization and its application (pp. 553-567) https://doi.org/10.1007/s12257-014-0173-7
  8. Yang et al. (2013) Reusable sensor based on high magnetization carboxyl-modified graphene oxide with intrinsic hydrogen peroxide catalytic activity for hydrogen peroxide and glucose detection (pp. 172-179) https://doi.org/10.1016/j.bios.2012.08.008
  9. Hou et al. (2014) Laccase immobilization on titania nanoparticles and titania-functionalized membranes (pp. 229-240) https://doi.org/10.1016/j.memsci.2013.10.019
  10. Ding et al. (2015) Increasing the activity of immobilized enzymes with nanoparticle conjugation (pp. 242-250) https://doi.org/10.1016/j.copbio.2015.04.005
  11. Kües (2015) Fungal enzymes for environmental management (pp. 268-278) https://doi.org/10.1016/j.copbio.2015.03.006
  12. Senthivelan et al. (2016) Recent trends in fungal laccase for various industrial applications: an eco-friendly approach—A review (pp. 19-38) https://doi.org/10.1007/s12257-015-0278-7
  13. Asif et al. (2017) Degradation of pharmaceuticals and personal care products by white-rot fungi—a critical review 3(2) (pp. 88-103) https://doi.org/10.1007/s40726-017-0049-5
  14. Fernández-Fernández et al. (2013) Recent developments and applications of immobilized laccase (pp. 1808-1825) https://doi.org/10.1016/j.biotechadv.2012.02.013
  15. Catherine et al. (2016) Product formation from phenolic compounds removal by laccases: a review (pp. 250-266) https://doi.org/10.1016/j.eti.2016.04.001
  16. Pang et al. (2015) Degradation of phenolic compounds by laccase immobilized on carbon nanomaterials: diffusional limitation investigation (pp. 38-45) https://doi.org/10.1016/j.talanta.2014.07.045
  17. Richter et al. (2015) Novel materials through nature’s catalysts (pp. 459-467) https://doi.org/10.1016/j.mattod.2015.04.002
  18. Li et al. (2016) A magnetic mesoporous SiO2/Fe3O4 hollow microsphere with a novel network-like composite shell: synthesis and application on laccase immobilization (pp. 523-530) https://doi.org/10.1007/s10971-016-3967-6
  19. Asther et al. (1988) Phospholipid and fatty acid enrichment of Phanerochaete chrysosporium INA-12 in relation to ligninase production (pp. 393-398) https://doi.org/10.1007/BF00251775
  20. Rudakiya and Gupte (2017) Degradation of hardwoods by treatment of white rot fungi and its pyrolysis kinetics studies (pp. 21-35) https://doi.org/10.1016/j.ibiod.2017.02.004
  21. Stöber et al. (1968) Controlled growth of monodisperse silica spheres in the micron size range (pp. 62-69) https://doi.org/10.1016/0021-9797(68)90272-5
  22. Huang et al. (2006) Immobilization of Pycnoporus sanguineus laccase on copper tetra-aminophthalocyanine–Fe3O4 nanoparticle composite (pp. 93-100) https://doi.org/10.1042/BA20050213
  23. Lowry et al. (1951) Protein measurement with the Folin phenol reagent (pp. 265-275)
  24. Kalme et al. (2010) Biodegradation of Green HE4B: co-substrate effect, biotransformation enzymes and metabolite toxicity analysis (pp. 156-164) https://doi.org/10.1007/s12088-010-0001-5
  25. Al-Adhami et al. (2002) Immobilization of wood-rotting fungi laccases on modified cellulose and acrylic carriers (pp. 1387-1394) https://doi.org/10.1016/S0032-9592(02)00023-7
  26. Bayramoglu et al. (2012) Immobilization of laccase on itaconic acid grafted and Cu (II) ion chelated chitosan membrane for bioremediation of hazardous materials (pp. 530-539) https://doi.org/10.1002/jctb.2743
  27. Beganskienė et al. (2004) FTIR, TEM and NMR investigations of Stöber silica nanoparticles (pp. 287-290)
  28. Rudakiya and Pawar (2017) Bactericidal potential of silver nanoparticles synthesized using cell-free extract of Comamonas acidovorans: in vitro and in silico approaches 7(2) https://doi.org/10.1007/s13205-017-0728-3
  29. Kalkan et al. (2012) Preparation of chitosan-coated magnetite nanoparticles and application for immobilization of laccase (pp. 707-716) https://doi.org/10.1002/app.34504
  30. Wang et al. (2010) Magnetic mesoporous silica nanoparticles: fabrication and their laccase immobilization performance (pp. 8931-8935) https://doi.org/10.1016/j.biortech.2010.06.115
  31. Cabana et al. (2011) Conjugation of laccase from the white rot fungus Trametes versicolour to chitosan and its utilization for the elimination of triclosan (pp. 1656-1662) https://doi.org/10.1016/j.biortech.2010.09.080
  32. Hu et al. (2007) Comparative study of immobilized Trametes versicolour laccase on nanoparticles and kaolinite (pp. 1618-1626) https://doi.org/10.1016/j.chemosphere.2006.08.004
  33. Irshad et al. (2012) Decolorization applicability of sol–gel matrix-immobilized laccase produced from Ganoderma leucidum using agro-industrial waste (pp. 4249-4261)
  34. Liu et al. (2012) Immobilization of laccase on magnetic bimodal mesoporous carbon and the application in the removal of phenolic compounds (pp. 21-26) https://doi.org/10.1016/j.biortech.2011.11.015
  35. Roy et al. (2005) Biosensor for the determination of phenols based on cross-linked enzyme crystals (CLEC) of laccase (pp. 206-211) https://doi.org/10.1016/j.bios.2004.08.024
  36. Valle-Vigón and Fuertes (2011) Magnetically separable carbon capsules loaded with laccase and their application to dye degradation (pp. 1756-1762) https://doi.org/10.1039/c1ra00333j
  37. Makas et al. (2010) Immobilization of laccase in κ-carrageenan based semi-interpenetrating polymer networks (pp. 216-220) https://doi.org/10.1016/j.jbiotec.2010.05.011
  38. Usluoglu and Arabaci (2013) Dye decolourization by Dandelion (Taraxacum officinale) polyphenol oxidase immobilized into alginate beads (pp. 16-20)
  39. Mogharabi, M., Nassiri-Koopaei, N., Bozorgi-Koushalshahi, M., Nafissi-Varcheh, N., Bagherzadeh, G., Faramarzi, M.A.: Immobilization of laccase in alginate-gelatin mixed gel and decolourization of synthetic dyes. Bioinorg. Chem. Appl. 1–6 (2012). doi:
  40. 10.1155/2012/823830
  41. Zille et al. (2005) Degradation of azo dyes by Trametes villosa laccase over long periods of oxidative conditions (pp. 6711-6718) https://doi.org/10.1128/AEM.71.11.6711-6718.2005
  42. Jadhav et al. (2011) Biochemical degradation pathway of textile dye Remazol red and subsequent toxicological evaluation by cytotoxicity, genotoxicity and oxidative stress studies (pp. 733-743) https://doi.org/10.1016/j.ibiod.2011.04.003
  43. Ilyas and Rehman (2013) Decolourization and detoxification of Synozol red HF-6BN azo dye, by Aspergillus niger and Nigrospora sp 10(1) https://doi.org/10.1186/1735-2746-10-12
  44. Lade et al. (2012) Enhanced biodegradation and detoxification of disperse azo dye Rubine GFL and textile industry effluent by defined fungal–bacterial consortium (pp. 94-107) https://doi.org/10.1016/j.ibiod.2012.06.001