Purification of pyranose oxidase from the white rot fungus Irpex lacteus and its cooperation with laccase in lignin degradation》.pdf

Process Biochemistry 49 (2014) 2191–2198 Contents lists available at ScienceDirect Process Biochemistry j o u r n a l h o m e p a g e: w w w. elsev /locate/proc bio Purification of pyranose oxidase from the white rot fungus Irpex lacteus and its cooperation with laccase in lignin degradation Ming-Qiang Ai, Fang-Fang Wang, Yu-Zhong Zhang, Feng Huang ∗ State Key Laboratory of Microbial Technology, Shandong University,Jinan 250100, China a r t i c l e i n f o a b s t r a c t Article history: Laccase and peroxidases mainly cause polymerization of lignin in vitro due to the random coupling of the Received 30 April 2014 phenoxy radicals or quinoid intermediates. White rot fungi may avoid polymerization in vivo by reduction Received in revised form 8 August 2014 of these intermediates. Pyranose oxidase is suggested to play such a role based on its quinone-reducing Accepted 1 October 2014 activity, but direct evidence has been lacking. In this study, a pyranose oxidase was purified from the Available online 13 October 2014 white rot fungus Irpex lacteus and partially characterized. The enzyme is composed of four subunits of 71 kDa as determined by SDS. It exhibits maximum activity at pH 6.5 and 55 ◦ C and is rather stable. Keywords: d-glucose is the preferred substrate, but d-galactose, l-sorbose and d-xylose are also readily oxidized. In Pyranose oxidase