An extracellular yellow laccase from white rot fungus Trametes sp. F1635 and its mediator systems for dye decolorization

Biochimie. 2018 May:148:46-54. doi: 10.1016/j.biochi.2018.02.015. Epub 2018 Mar 5.

Abstract

A novel extracellular laccase was purified from fermentation broth of the white rot fungus Trametes sp. F1635 by a three-step protocol including two consecutive ion-exchange chromatography steps on DEAE-Sepharose and SP-Sepharose, and a final gel-filtration on Superdex 75. The purified laccase (TsL) was a monomeric protein with the molecular mass of 64.8 kDa. It demonstrated high oxidation activity of 4.00 × 104 U/mg towards ABTS. Its N-terminal amino acid sequence was AIGPVADLTIINNAV which was unique and sharing high similarity of other fungal laccases. TsL was a yellow laccase based on absorption spectrum analysis. It demonstrated an acidic pH optimum of 2.6 and temperature optimum of 50 °C towards ABTS. The Km and Vmax values towards ABTS were estimated to 18.58 μM and 1.35 μmol/min, respectively. TsL manifested effective decolorization activity towards eriochrome black T (EBT), remazol brilliant blue R (RBBR), malachite green (MG), and eriochrome black T (EBT) (over 60%). Violuric acid (VA) and acetosyringone (AS) were the optimal mediators for the laccase in dye decolorization. Results suggest that TsL demonstrates great potential for dye decolorization and water treatment.

Keywords: Dye decolorization; Laccase; Laccase-mediator system; Purification; Trametes.

MeSH terms

  • Amino Acid Sequence
  • Color
  • Coloring Agents / metabolism*
  • Extracellular Space / enzymology*
  • Fermentation
  • Hydrogen-Ion Concentration
  • Kinetics
  • Laccase / chemistry
  • Laccase / metabolism*
  • Molecular Weight
  • Temperature
  • Trametes / cytology*
  • Trametes / enzymology

Substances

  • Coloring Agents
  • Laccase