Applied Microbiology and Biotechnology

, Volume 37, Issue 3, pp 321–323

Purification and characterization of laccase from Monocillium indicum Saxena

  • Geeta D. Thakker
  • Christine S. Evans
  • K. Koteswara Rao
Biochemical Engineering Short Contribution

DOI: 10.1007/BF00210986

Cite this article as:
Thakker, G.D., Evans, C.S. & Rao, K.K. Appl Microbiol Biotechnol (1992) 37: 321. doi:10.1007/BF00210986

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.

Copyright information

© Springer-Verlag 1992

Authors and Affiliations

  • Geeta D. Thakker
    • 1
  • Christine S. Evans
    • 2
  • K. Koteswara Rao
    • 1
  1. 1.Department of Microbiology and Biotechnology Centre, Faculty of ScienceM. S. University of BarodaBarodaIndia
  2. 2.School of Biological and Health SciencesThe Polytechnic of Central LondonLondonUK

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