[Cloning, Expression, and Characterization of Novel Laccase Enzyme from Native Bacillus subtilis Strain OH67]

Mol Biol (Mosk). 2020 Jul-Aug;54(4):680-687. doi: 10.31857/S0026898420040060.
[Article in Russian]

Abstract

Bacterial laccases are very stable at high temperature and high pH values, and have many biotechnological and industrial applications. Here we describe how we cloned, expressed and purified the laccase from Bacillus subtilis (B. subtilis). The enzyme molecular weight has been determined as 34 kDa in SDS-PAGE analysis. The activity of the recombinant enzyme has been proved by guaiacol oxidation. The KM and Vmax values of the enzyme were at 1.1077 mM and at 19.3 μmol/min/mg, respectively. The recombinant laccase was effective in the decolorization of Turquoise blue HF6, Remazol red 106, Remazol brilliant orange 3R, and Brilliant blue, thus, possessing the characteristics necessary for its possible application in textile and environmental industries.

Keywords: Bacillus subtilis; cloning; decolorization; expression; laccase.

MeSH terms

  • Bacillus subtilis / enzymology*
  • Bacillus subtilis / genetics
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cloning, Molecular
  • Coloring Agents / metabolism
  • Hydrogen-Ion Concentration
  • Laccase / genetics
  • Laccase / metabolism*
  • Temperature

Substances

  • Bacterial Proteins
  • Coloring Agents
  • Laccase