Open AccessPurification and characterization of laccase from the rice blast fungus, Magnaporthe grisea
Author(s) -
Iyer Gopal,
Chattoo B.B
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00658-x
Subject(s) - magnaporthe grisea , laccase , enzyme , substrate (aquarium) , fungus , size exclusion chromatography , chelation , enzyme assay , chemistry , chromatography , extracellular , yield (engineering) , ion chromatography , biochemistry , biology , botany , organic chemistry , oryza sativa , materials science , ecology , metallurgy , gene
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 K m was 0.118 mM. The enzyme was strongly inhibited by Cu‐chelating agents.