Purification and characterization of laccase from the rice blast fungus, Magnaporthe grisea.
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 degrees C, and its K(m) was 0.118 mM. The enzyme was strongly inhibited by Cu-chelating agents.
Plant and Microbial Biology Department, 111 Koshland Hall, University of California, Berkeley, CA 94720, USA. chattoo@giasbm01.vsnl.net.in
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Chattoo
D002851:Chromatography, High Pressure Liquid; D042845:Laccase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D020082:Magnaporthe / Q000201:enzymology* / Q000254:growth & development / Q000302:isolation & purification; D012275:Oryza / Q000382:microbiology*; D010935:Plant Diseases / Q000382:microbiology
D042845:Laccase