Optimization of process variables for the manganese peroxidase of the white-rot fungus Schizophyllum sp. F17 by full factorial central composite design.
- Author:
Cheng ZHA
1
;
Rong JIA
;
Xianglin TAO
;
Zuliang YAO
Author Information
1. School of Life Science, Anhui Key Laboratory of Eco-engineering and Bio-technique, Anhui University, Hefei 230039, China.
- Publication Type:Journal Article
- MeSH:
Azo Compounds;
chemistry;
isolation & purification;
metabolism;
Catalysis;
Coloring Agents;
chemistry;
isolation & purification;
metabolism;
Environmental Pollutants;
chemistry;
isolation & purification;
metabolism;
Fungal Proteins;
chemistry;
isolation & purification;
metabolism;
Peroxidases;
chemistry;
isolation & purification;
metabolism;
Schizophyllum;
enzymology
- From:
Chinese Journal of Biotechnology
2010;26(3):341-349
- CountryChina
- Language:English
-
Abstract:
White-rot fungus manganese peroxidase (MnP) that has great potential in degrading azo dyes is one of the extracellular glycolsylated heme proteins. MnP from Schizophyllum sp. F17 was isolated and purified by Sephadex G-75 gel filtration chromatography followed by DEAE-cellulose anion exchange chromatography. The molecular weight of the puried enzyme was 49.2 kDa, while the half-life of the MnP in the presence of 0.1 mmol/L H2O2 was 5-6 min. The efficiency of MnP-catalyzed reactions were determined by three key factors: the concentrations of Mn2+, H2O2, and the amount of MnP. Using single factor analysis, an optimized concentration of Mn2+, H2O2 and enzyme were optimized to be 1.2 mmol/L, 0.1 mmol/L, and 0.4 mL, respectively. A response surface methodology (RSM) employing two-level-three-factor full factorial central composite design was used to optimize the catalytic conditions. The result showed that the concentration of H2O2 and the interaction between H2O2 and MnP mostly affect the MnP catalytic efficiency. Finally, we show that the azo dyes could be efficiently decolorized by the purified MnP under optimized conditions.
