Purification and characterization of laccase from curvularia trifol
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 ℃ and 3.5,respectively.The Km of ABTS catalyzed by laccase was 1.11×10-5 mol 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.
Curvularia trifol laccase purification of enzyme enzymological properties
Jie Zhang Jing Ren Yang Yu Binsong Wang
School of Life Sciences,Northeast Forestry University,Harbin 150040,China School of chemistry chemical engneering and material,Heilongjiang University,Harbin 150080,China
国际会议
哈尔滨
英文
2215-2219
2010-07-24（万方平台首次上网日期，不代表论文的发表时间）