Purification, characterization and evaluation of extracellular peroxidase from two Coprinus species for aqueous phenol treatment.
Non-ligninolytic fungal peroxidases produced by Coprinus cinereus UAMH 4103 and Coprinus sp. UAMH 10067 were purified, characterized and evaluated as cost-effective alternatives to horseradish peroxidase for aqueous phenol treatment. Purified Coprinus peroxidases exhibited a molecular weight of 36 kDa on matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Although the catalytic properties of the two Coprinus peroxidases were nearly identical in both crude and purified forms, the stabilities were substantially different. The peroxidase from Coprinus sp. UAMH 10067 was more stable at 50 degrees C and under basic conditions (up to pH 10) than the enzyme from C. cinereus UAMH 4103. The former enzyme also performed better at pH 9 than the latter one in aqueous phenol treatment. The phenol removal efficiency of the Coprinus peroxidase was comparable to those of previously studied plant peroxidases. The broader working pH and higher thermal and alkaline stability of the peroxidase from Coprinus sp. UAMH 10067 may be advantageous for its application to industrial wastewater treatment.
Ikehata
Keisuke
K
Department of Civil and Environmental Engineering, University of Alberta, Edmonton, Alberta, Canada T6G 2W2.
Buchanan
Ian D
ID
Pickard
Michael A
MA
Smith
Daniel W
DW
D001673:Biodegradation, Environmental; D003302:Coprinus / Q000145:classification / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D045604:Extracellular Fluid / Q000737:chemistry; D009195:Peroxidase / Q000737:chemistry* / Q000302:isolation & purification*; D010636:Phenols / Q000737:chemistry*; D013045:Species Specificity; D018508:Water Purification / Q000379:methods*
D010636:Phenols; D009195:Peroxidase