Purification and characterization of a novel manganese peroxidase from white-rot fungus Cerrena unicolor BBP6 and its application in dye decolorization and denim bleaching

2018 ◽  
Vol 66 ◽  
pp. 222-229 ◽  
Author(s):  
Hao Zhang ◽  
Ji Zhang ◽  
Xiaoyu Zhang ◽  
Anli Geng
2013 ◽  
Vol 442 ◽  
pp. 120-124
Author(s):  
Bei Bei Zhang ◽  
Yong Jian Shen ◽  
Chang Xu ◽  
Ying Li ◽  
Ming Hu Jiang

Dyes are usually difficult to be decolorized due to their complex chemical structures. In this work, laccase was purified from the white rot fungus Cerrena unicolor to evaluate its application in dye decolorization. SDS-PAGE analysis showed the purified laccase to be a monomeric protein of 63.7 kDa. The optimum pH for the oxidation of 2,2-azinobis-(3-ethylbenzthiaoline-6-sufonic acid) (ABTS) was 2.2 and the optimum temperature was 50°C. The activity of the purified enzyme was strongly inhibited by sodium azide and partially inhibited by cysteine, dithiothreitol. The Km values of the purified laccase for the substrate ABTS, syringaldazine and 2,6-dimethoxyphenol were 0.217, 0.306 and 0.199 mmol/L.


2010 ◽  
Vol 27 (3) ◽  
pp. 731-735 ◽  
Author(s):  
Li-Qiong Guo ◽  
Shuo-Xin Lin ◽  
Xiao-Bing Zheng ◽  
Zi-Rou Huang ◽  
Jun-Fang Lin

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