Production and characterization of a novel laccase with cold adaptation and high thermal stability from an isolated fungus

Appl Biochem Biotechnol. 2010 Sep;162(1):280-94. doi: 10.1007/s12010-009-8801-y. Epub 2009 Oct 20.

Abstract

A new white-rot fungus SYBC-L1, which could produce an extracellular laccase, was isolated from a decayed Elaeocarpus sylvestris. The strain was identified as Pycnoporus sp. SYBC-L1 according to the morphological characteristics and ribosomal ITS1-5.8S-ITS2 RNA genomic sequence analysis. The highest laccase activity of 24.1 U ml(-1), which was approximately 40-fold than that in basal medium, was achieved in optimal culture medium in submerged fermentation. The laccase produced by Pycnoporus sp. SYBC-L1 was not only a cold adaptation enzyme with a relative catalytic activity of 30.2% at 0 degrees C but also a high thermostable enzyme. The half-lives at 60, 70 and 80 degrees C were 85.5, 37.2, and 2.6 h, respectively. The laccase could effectively decolorize weak acid blue AS and diamond black PV up to 88% and 74.7%, respectively, within 2 h in the absence of any redox mediators. The results suggested Pycnoporus sp. SYBC-L1 was a potential candidate for laccase production and industrial application.

MeSH terms

  • Adaptation, Physiological*
  • Animals
  • Carbon / pharmacology
  • Cold Temperature*
  • Color
  • Coloring Agents / metabolism
  • Copper / pharmacology
  • Elaeocarpaceae / microbiology
  • Enzyme Stability
  • Fermentation / drug effects
  • Hydrogen-Ion Concentration
  • Immersion
  • Laccase / biosynthesis*
  • Laccase / chemistry*
  • Laccase / metabolism
  • Nitrogen / pharmacology
  • Pycnoporus / drug effects
  • Pycnoporus / enzymology*
  • Pycnoporus / isolation & purification
  • Pycnoporus / physiology*
  • Wool

Substances

  • Coloring Agents
  • Carbon
  • Copper
  • Laccase
  • Nitrogen