Molecular cloning and expression of a novel laccase showing thermo- and acid-stability from the endophytic fungus Phomopsis liquidambari and its potential for growth promotion of plants

Biotechnol Lett. 2014 Jan;36(1):167-73. doi: 10.1007/s10529-013-1347-7. Epub 2013 Oct 8.

Abstract

A novel laccase (LACB3) from the endophytic fungus, Phomopsis liquidambari, was cloned and its potential to promote peanut growth was evaluated. The full-length cDNA is 1,731 bp, encoding a mature protein of 556 amino acids with a molecular mass of 60.1 kDa. Using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate), LACB3 exhibited a K m and k cat of 85 μM and 92.7 s(-1), respectively. The enzyme had maximal activity at pH 2.5 and 50 °C and retained 50 % of its activity after 20 h at 50 °C. When LACB3 was applied to soil, the peanut biomass was increased by 12 %, and the content of vanillic acid, coumaric acid and 4-hydroxybenzoic acid in soil were decreased by 21, 27 and 40 %, respectively. These results suggest substantial potential for the use of P. liquidambari or its laccase in agriculture.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arachis / drug effects
  • Ascomycota / enzymology*
  • Ascomycota / genetics
  • Bacteria / drug effects
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Endophytes / enzymology
  • Endophytes / genetics
  • Enzyme Stability
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Fungal Proteins / pharmacology
  • Hydrogen-Ion Concentration
  • Kinetics
  • Laccase / chemistry*
  • Laccase / genetics
  • Laccase / metabolism*
  • Laccase / pharmacology
  • Phylogeny
  • Recombinant Proteins / chemistry*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / pharmacology
  • Temperature

Substances

  • Fungal Proteins
  • Recombinant Proteins
  • Laccase