Abstract Characteristics of a dominant lignin peroxidase isoenzyme of Phanerochaete chrysosporium from solid state fermentation on rice husks

1. Darah, R. Burke and C. 0. Ibrahim

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

(Received 13 July 1998 / Accepted 27 October 1998)

Abstract.
The lignin peroxidase of Phanerochaete chrysosporium was purified by means of ammonium sulphate precipitation and on an anion exchange chromatography, using a prepacked Mono Q column. The resolution from Mono Q column resulted in 6 different isoenzymes with the recovery of 51 % of which peak 5 (P5) was dominant with 29% recovery. P5 was purified about 23 folds with the specific activity of about 11.7 Umg 1 protein. The molecular weight of P5 was estimated to be 42,000 Dalton by SDS PAGE and the isoelectric point was at pl l 4.2. The optimum temperature and pH were 30 – 37⁰C and 3.0, respectively. The isoenzyme was stable within the pH range of 2-4 and almost 70% of the enzyme activity was retained even after 48 h at 30⁰C.

Keywords: lignin peroxidase, Phanerochaete chrysosporium, solid state fermentation, lignin peroxidase isoenzyme