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Purification and properties of laccase from Ganoderma lucidum

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Summary

The enzyme laccase has been partially purified from the culture fluid of Ganoderma lucidum by acetone precipitation, ammonium sulphate fractionation and adsorption on alumina Cγ gel. The enzyme has been shown to be specific for ortho and para hydroxyphenolic compounds, having Km values of 5.5×10-5 M and 2.86×10-5 M for catechol and hydroquinone respectively. The optimum pH for the oxidation of catechol and hydroquinone are 5.4 and 5.0 respectively. The enzyme is inactivated above 60°C and is inhibited by enzyme inhibitors and metal chelating agents like azide, cyanide etc.

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Authors and Affiliations

  1. Microbiology and Pharmacology Laboratory, Indian Institute of Science, Bangalore 12, India

    H. Lalitha Kumari & M. Sirsi

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  1. H. Lalitha Kumari
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  2. M. Sirsi
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Kumari, H.L., Sirsi, M. Purification and properties of laccase from Ganoderma lucidum . Archiv. Mikrobiol. 84, 350–357 (1972). https://doi.org/10.1007/BF00409083

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