Purification and characterization of laccase from Monocillium indicum Saxena

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 f...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 1992-06, Vol.37 (3), p.321-323
Main Authors: Thakker, G.D, Evans, C.S, Koteswara Rao, K
Format: Article
Language:English
Subjects:
activity
Ascomycota
Bacteriology
Biological and medical sciences
characterization
enzyme activity
Fundamental and applied biological sciences. Psychology
laccase
Metabolism. Enzymes
Microbiology
Monocillium indicum
purification
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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.
ISSN:0175-7598
1432-0614
DOI:10.1007/BF00210986