Iyer, Gopal ; Chattoo, B. B. (2003) Purification and characterization of laccase from the rice blast fungus, Magnaporthe grisea FEMS Microbiology Letters, 227 (1). pp. 121-126. ISSN 0378-1097
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Official URL: http://onlinelibrary.wiley.com/doi/10.1016/S0378-1...
Related URL: http://dx.doi.org/10.1016/S0378-1097(03)00658-X
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 Kmwas 0.118 mM. The enzyme was strongly inhibited by Cu-chelating agents.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to John Wiley and Sons. |
| Keywords: | Magnaporthe grisea; Laccase; Syringaldazine |
| ID Code: | 60101 |
| Deposited On: | 08 Sep 2011 09:59 |
| Last Modified: | 08 Sep 2011 09:59 |
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