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Purification and characterization of a laccase from the white-rot fungus Trametes multicolor

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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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Correspondence to Dietmar Haltrich.

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Leitner, C., Hess, J., Galhaup, C. et al. Purification and characterization of a laccase from the white-rot fungus Trametes multicolor . Appl Biochem Biotechnol 98, 497–507 (2002). https://doi.org/10.1385/ABAB:98-100:1-9:497

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