Premium
Characterisation of laccase produced by Coniothyrium minitans
Author(s) -
Dahiya Jagroop S.,
Singh Dalel,
Nigam Poonam
Publication year - 1998
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/(sici)1521-4028(199811)38:5/6<349::aid-jobm349>3.0.co;2-b
Subject(s) - laccase , enzyme , fermentation , chromatography , mannose , specific activity , chemistry , substrate (aquarium) , enzyme assay , oxidoreductase , solid state fermentation , biochemistry , biology , ecology
A Coniothyrium minitans strain isolated from an experimental farm in Manitoba produced a substantial amount of an oxidoreductase enzyme, laccase in a 20 litre fermentation system using a simple production medium. This enzyme was purified to homogeneity by a simple procedure, the last stage of which involved hydrophobic interaction chromatography. Using this technique, over 120 mg of laccase protein was recovered per litre of fermented broth. The enzyme, with an estimated M r of 74,000 and pI of 4.0, is a monomeric glycoprotein that contains 45% carbohydrate predominantly as mannose. It exhibited pH and temperature optima of 3.5 and 60 °C, respectively. Using 2,6‐dimeth‐oxyphenol as substrate the K m value was found to be 100 μM and the purified enzyme had a specific activity of 9.9 mkat per mg of protein.