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 degrees C, respectively. Using 2,6-dimethoxyphenol as substrate the K-m value was found to be 100 mu M and the purified enzyme had a specific activity of 9.9 mkat per mg of protein.
|Journal||JOURNAL OF BASIC MICROBIOLOGY|
|Publication status||Published (in print/issue) - 1998|