Purification and characterization of a laccase from the white-rot fungus Trametes multicolor.
The wood-degrading fungus Trametes multicolor secretes several laccase isoforms when grown on a simple medium containing copper in the millimolar range for stimulating laccase synthesis. The main isoenzyme laccase II was purified to apparent homogeneity from the culture supernatant by using anion-exchange chromatography and gel filtration. Laccase II is a monomeric glycoprotein with a molecular mass of 63 kDa as determined by sodium dodecylsulfate polyacrylamide gel electrophoresis, contains 18% glycosylation, and has a pI of 3.0. It oxidizes a variety of phenolic substrates as well as ferrocyanide and iodide. The pH optimum depends on the substrate employed and shows a bell-shaped pH activity profile with an optimum of 4.0 to 5.0 for the phenolic substrates, while the nonphenolic substrates ferrocyanide and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate) show a monotonic pH profile with a rate decreasing with increasing pH.
Leitner
Christian
C
Division of Biochemical Engineering, Institute of Food Technology, University of Agricultural Sciences Vienna, Austria.
Hess
Johann
J
Galhaup
Christiane
C
Ludwig
Roland
R
Nidetzky
Bernd
B
Kulbe
Klaus D
KD
Haltrich
Dietmar
D
D001487:Basidiomycota / Q000201:enzymology* / Q000254:growth & development; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D042845:Laccase; D008970:Molecular Weight; D010088:Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism*; D013379:Substrate Specificity; D013816:Thermodynamics
D007527:Isoenzymes; D010088:Oxidoreductases; D042845:Laccase