Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes

PLoS One. 2020 Jun 4;15(6):e0229968. doi: 10.1371/journal.pone.0229968. eCollection 2020.

Abstract

Although laccase has been recognized as a wonder molecule and green enzyme, the use of low yielding fungal strains, poor production, purification, and low enzyme kinetics have hampered its large-scale application. Thus,this study aims to select high yielding fungal strains and optimize the production, purification, and kinetics of laccase of Aspergillus sp. HB_RZ4. The results obtained indicated that Aspergillus sp. HB_RZ4 produced a significantly large amount of laccase under meso-acidophilic shaking conditions in a medium containing glucose and yeast extract. A 25 μM CuSO4 was observed to enhance the enzyme yield. The enzyme was best purified on a Sephadex G-100 column. The purified enzyme resembled laccase of A. flavus. The kinetics of the purified enzyme revealed high substrate specificity and good velocity of reaction,using ABTS as a substrate. The enzyme was observed to be stable over various pH values and temperatures. The peptide structure of the purified enzyme was found to resemble laccase of A. kawachii IFO 4308. The fungus was observed to decolorize various dyes independent of the requirement of a laccase mediator system.Aspergillus sp. HB_RZ4 was observed to be a potent natural producer of laccase, and it decolorized the dyes even in the absence of a laccase mediator system. Thus, it can be used for bioremediation of effluent that contains non-textile dyes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus / enzymology*
  • Biodegradation, Environmental
  • Biotechnology / methods*
  • Coloring Agents / isolation & purification
  • Coloring Agents / metabolism*
  • Enzyme Activation
  • Enzyme Inhibitors / pharmacology
  • Enzyme Stability
  • Enzymes, Immobilized / antagonists & inhibitors
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism
  • Hydrogen-Ion Concentration
  • Laccase / antagonists & inhibitors
  • Laccase / chemistry
  • Laccase / metabolism*
  • Plant Bark / microbiology*

Substances

  • Coloring Agents
  • Enzyme Inhibitors
  • Enzymes, Immobilized
  • Laccase

Grants and funding

The authors extend their sincere appreciation to the Deanship of Scientific Research at King Saud University and MOE, UTM-RMC, and MOHE-HICOE fund, Malaysia for supporting this research through the Research Group Project NO RG-1436-025 and No.R.J130000.7846.4J262, respectively.