Properties of laccases produced by Pycnoporus sanguineus induced by 2,5-xylidine

Biotechnol Lett. 2006 May;28(9):633-6. doi: 10.1007/s10529-006-0026-3.

Abstract

Two isoforms of laccase produced from the culture supernatant of Pycnoporus sanguineus were partially purified by phenyl-Sepharose chromatography. Molecular masses of the enzymes were 80 kDa (Lac I) and 68 kDa (Lac II). Optimum activity of Lac I was at pH 4.8 and 30 degrees C, and Lac II was at pH 4.2 and 50 degrees C over 5 min reaction. The Km values of enzymes toward syringaldazine were 10 microM: (Lac I) and 8 microM: (Lac II). Sodium azide inhibited Lac I (85%) and Lac II (75%) activities.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biotechnology
  • Chromatography, Agarose
  • Enzyme Induction / drug effects
  • Enzyme Stability
  • Hydrazones / metabolism
  • Hydrogen-Ion Concentration
  • Isoenzymes / biosynthesis
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism
  • Kinetics
  • Laccase / biosynthesis*
  • Laccase / chemistry
  • Laccase / metabolism
  • Molecular Weight
  • Polyporaceae / drug effects*
  • Polyporaceae / enzymology*
  • Substrate Specificity

Substances

  • Hydrazones
  • Isoenzymes
  • syringaldazine
  • Laccase