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        Production of a Thermostable Metal-tolerant Laccase from Trametes versicolor and its Application in Dye Decolorization

        Zhu Youshuang,Zhang Haibo,Cao Mingle,Wei Zhenzhen,Huang Feng,Gao Peiji 한국생물공학회 2011 Biotechnology and Bioprocess Engineering Vol.16 No.5

        Production of laccase using a submerged culture of Trametes versicolor sdu-4 was optimized using a central composite design of the Response Surface Methodology. Optimized conditions gave a laccase yield of 4,213 U/L which was approximately three times of that in basal medium. The laccase was purified to homogeneity using a three-step process. The overall yield of the purification was 58%, with a purification fold of 11.4 and a specific activity of 1320.7 U/mg protein. The molecular mass of the laccase was 60 kDa. The optimum pH values of the enzyme were 2.2, 3.7, and 7 for the oxidations of ABTS, DMP, and syringaldazine, respectively. The enzyme had adaptability to a broad pH range and high temperature and wsa stable at pH 3.0 ~ 10.0. The half-life of this laccase at 70°C was 2.2 h. Methyl red, 2-bromophenol, and 4-bromophenol were oxidized by the purified laccase in the absence of mediators. Purified laccase was effective in the decolorization of several dyes and was not inhibited by Cu^(2+), Mn^(2+), Zn^(2+), Na^+, K^+, Mg^(2+), Ba^(2+), and Ca^(2+) at 5 mM. These excellent characteristics made it a highly attractive candidate for industrial use.

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