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3699278 
Journal Article 
Purification and Characterization of Laccase from Ceriporiopsis subvermispora 
Wang, C; Xu, H; Yun, XueJun 
2014 
Yes 
Asian Journal of Chemistry
ISSN: 0970-7077
EISSN: 0975-427X 
26 
15 
4655-4660 
WOS:000343766300026 
Laccase from Ceriporiopsis subvermispora was purified and partially characterized using a combination of ammonium sulfate precipitation, DEAE-cellulose ion exchange chromatography and Sephadex G-100 molecular sieve column chromatography. The results demonstrated that the maximum laccase output from C. subvermispora fermentation reached 3900 U/L. The specific activity of the laccase increased from 10.28 U/mg in a crude enzyme solution to 245.27 U/mg after isolation and purification, with a purification factor of 23.86 and a yield of 24.40 %. The molecular mass of laccase was 63 kDa and the Michaelis-Menten constant value was 23.3 mu mol/L. The optimal temperature for enzyme activity was 50 degrees C. The stabilization pH range was 4-5; within a pH 4-5 range, the relative activity was higher than 70 %. 
Ceriporiopsis subvermispora; Laccase; Purification; Laccase activity; Characterization