Purification and Characterization of Laccase from Curvularia trifol

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Electrophoretic pure lacquer enzymes were obtained from the thick enzyme of Gladiolus Curvularia trifol with grading precipitation and DEAE2-Cellulose ion exchange chromatography. The overall recycling rate of enzyme activity was 14.97% and the purification reached 2.96 times. The relative molecular mass of enzyme was 92.3Kda. The optimal temperature and pH were 40°C and 3.5, respectively. The Km of ABTS catalyzed by laccase was 1.11× 10- 5mol L-1. Alizarin red and Congo red could be degradated by purified laccase effectively without the participation of small molecule amboceptor. Alizarin red could be degradated by 80% with its being affected by 1000U/L of enzyme activity for 70h, which revealed the huge potentiality of Gladiolus Curvularia trifol and laccase in the degradation of dye.

Info:

Periodical:

Advanced Materials Research (Volumes 113-116)

Edited by:

Zhenyu Du and X.B Sun

Pages:

2215-2219

DOI:

10.4028/www.scientific.net/AMR.113-116.2215

Citation:

J. Zhang et al., "Purification and Characterization of Laccase from Curvularia trifol", Advanced Materials Research, Vols. 113-116, pp. 2215-2219, 2010

Online since:

June 2010

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Price:

$35.00

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