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• W2023911073 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." @default.
• W2023911073 created "2016-06-24" @default.
• W2023911073 creator A5033475196 @default.
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• W2023911073 date "2003-10-01" @default.
• W2023911073 modified "2023-10-18" @default.
• W2023911073 title "Purification and characterization of laccase from the rice blast fungus,<i>Magnaporthe grisea</i>" @default.
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• W2023911073 doi "https://doi.org/10.1016/s0378-1097(03)00658-x" @default.
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