Purification and characterization of a laccase from the white-rot fungus Trametes multicolor |
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Authors: | Leitner Christian Hess Johann Galhaup Christiane Ludwig Roland Nidetzky Bernd Kulbe Klaus D Haltrich Dietmar |
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Institution: | (1) Division of Biochemical Engineering, Institute of Food Technology, University of Agricultural Sciences Vienna, Muthgasse 18, A-1190 Vienna, Austria;(2) Wood Composite and Chemistry Center Austria (Wood Kplus), Area 1, Muthgasse 18, A-1190 Vienna, Austria |
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Abstract: | 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. |
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Keywords: | Trametes multicolor basidiomycete laccase polyphenol oxidase lignin degradation |
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