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Biochemical characterization of laccase isozymes of Ganoderma lucidum



Biochemical characterization of laccase isozymes of Ganoderma lucidum



Phytopathology 91(6 Supplement): S115



A Ganoderma lucidum monokaryon which was isolated in Korea secreted three laccase isozymes (Galc1, 2, 3) in a complete liquid medium without any induction. We have successfully purified these isozymes through the anion exchange chromatography, preparative electrophoresis and native PAGE. These isozymes had almost same mobilities in the native- and SDS-PAGE, and even in urea-PAGE which was a mild denaturing condition of proteins. They showed quite similar biochemical properties: optimum temperature of each isozyme was 20 C, and optimum pH was 3.5. Their molecular weights were estimated 65-70 kDa by the gel filtration and SDS-PAGE analysis. Their N-terminal amino acid sequences were same as G-I-G-P-T. Km value of an isozyme (GaLc3) for o-tolidine, which showed the fastest mobility in the native-PAGE, was 0.402 mM, and Vmax value was 0.02 (OD/min/unit). When the isozymes were treated with N-glycosidase or Endoglycosidase, deglycosylated proteins moved as one band in SDS-PAGE.

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Accession: 034485124

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