Summary
An ascomycete Monocillium indicum Saxena producing extracellular laccase was isolated. The culture filtrate on native polyacrylamide gel electrophoresis (PAGE) revealed four bands of activity, one of which was a major one. The major laccase band, a glycoprotein, was purified and characterized. Gel filtration chromatography showed that the relative molecular weight (Mr) of laccase was 100 000. On sodium dodecyl sulphate (SDS)-PAGE the major laccase band further resolved into three proteins of Mr 72 000, 56 000 and 24 000. The enzyme had a pH optimum of 3.0 and was active on a number of o-phenols and aromatic acids. The 72 000 Mr protein was found to share common immunological properties with laccases of Coriolus versicolor, Agaricus bisporus and lignin peroxidase of Phanerochaete chrysosporium.
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Correspondence to: K. Koteswara Rao
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Thakker, G.D., Evans, C.S. & Rao, K.K. Purification and characterization of laccase from Monocillium indicum Saxena. Appl Microbiol Biotechnol 37, 321–323 (1992). https://doi.org/10.1007/BF00210986
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DOI: https://doi.org/10.1007/BF00210986