Purification and characterization of laccase from the rice blast fungus, Magnaporthe grisea

Authors

  • Gopal Iyer,

    1. Plant and Microbial Biology Department, 111 Koshland Hall, University of California, Berkeley, CA 94720, USA
    2. Department of Microbiology and Biotechnology Centre, Faculty of Science, M. S. University of Baroda, Baroda 390 002, India
    Search for more papers by this author
  • B.B Chattoo

    Corresponding author
    1. Plant and Microbial Biology Department, 111 Koshland Hall, University of California, Berkeley, CA 94720, USA
    Search for more papers by this author

*Corresponding author. Tel.: +91 (265) 794396; Fax: +91 (265) 792508, E-mail address: chattoo@giasbm01.vsnl.net.in

Abstract

A 70-kDa extracellular laccase was purified from the rice blast fungus Magnaporthe grisea using gel filtration and ion exchange chromatography The procedure provided 282-fold purification with a specific enzyme activity of 225.91 U mg−1 and a yield of 11.92%. The enzyme oxidized a wide range of substrates. The highest level of oxidation was detected with syringaldazine as the substrate. Using syringaldazine as the substrate, the enzyme exhibited a pH optimum of 6 and temperature optimum of 30°C, and its Km was 0.118 mM. The enzyme was strongly inhibited by Cu-chelating agents.

Ancillary