Abstract Separation and some properties of an extracellular manganese peroxidase from Phanerochaete chrysosporium grown on solid state fermentation system using rice husks as substrate

Fermentation and Enzyme Technology Laboratory
School of Biological Sciences, Universiti Sains Malaysia
11800 Minden, Penang, Malaysia

(Received 9 November 2000 / Accepted 30 June 2001)

Abstract.
The manganese peroxidase was purified by means of ammonium sulphate precipitation and gel filtration chromatography of Sephadex G 100 and agarose. The enzyme recovery of 40.9% was obtained, with about 16 folds with the specific activity of about 8.0 U/mg protein. Purification of the enzyme was pet formed using the polyacrylamide gel electrophoresis technique. The molecular weight of the enzyme was estimated to be 45,000 Dalton by SDS PAGE. The optimum temperature and pH were 30–37^oC and 4.5, respectively. The enzyme was stable at pH of 4.5 and almost 60% of the enzyme activity was retained even after 48 hour at 30^oC.

Keywords: manganese peroxidase, extracellular, Phanerochaete chrysosporium, fermentation, solid state