Purification, biochemical characterization and dye decolorization capacity of an alkali-resistant and metal-tolerant laccase from Trametes pubescens.

@article{Si2013PurificationBC,
  title={Purification, biochemical characterization and dye decolorization capacity of an alkali-resistant and metal-tolerant laccase from Trametes pubescens.},
  author={Jing Si and Feng Peng and Baokai Cui},
  journal={Bioresource technology},
  year={2013},
  volume={128},
  pages={49-57}
}
Extracellular laccase (Tplac) from Trametes pubescens was purified to homogeneity by a three-step method, which resulted in a high specific activity of 18.543 Umg(-1), 16.016-fold greater than that of crude enzyme at the same level. Tplac is a monomeric protein that has a molecular mass of 68 kDa. The enzyme demonstrated high activity toward 1.0mM ABTS at an optimum pH of 5.0 and temperature of 50 °C, and under these conditions, the catalytic efficiency (k(cat)/K(m)) is 8.34 s(-1) μM(-1). Tplac… CONTINUE READING
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