Kim Yunjung, Yeo Sumin, Kim Myung K, Choi Hyoung T
Molecular Microbiology Laboratory, Department of Biochemistry, Division of Life Sciences, and Research Institute of Life Sciences, Kangwon National University, Chunchon, Korea.
FEMS Microbiol Lett. 2008 Jul;284(2):172-5. doi: 10.1111/j.1574-6968.2008.01189.x. Epub 2008 May 23.
A white-rot basidiomycete, Phlebia tremellosa, produced a laccase that showed increased activity during degradation of phthalates. A laccase was purified through the ion exchange chromatography and preparative gel electrophoresis, and the estimated molecular weight was 75 kDa. The optimum pH and temperature of the purified laccase was pH 4.0 and 20 degrees C, respectively. The K(m) value of the enzyme was 55.7 microM, and the V(max) was 0.0541 OD min(-1) U(-1) for o-tolidine. Purified laccase reduced the estrogenic activity of four different endocrine-disrupting chemicals. However, this effect was reduced by a laccase inhibitor, kojic acid, which confirmed that the laccase was involved in the removal of estrogenic activity.
一种白腐担子菌，即淡黄韧革菌（Phlebia tremellosa），产生了一种漆酶，该漆酶在邻苯二甲酸酯降解过程中活性增加。通过离子交换色谱法和制备性凝胶电泳对漆酶进行了纯化，估计其分子量为75 kDa。纯化漆酶的最适pH值和温度分别为pH 4.0和20℃。该酶的K(m)值为55.7 microM，对邻联甲苯胺的V(max)为0.0541 OD min(-1) U(-1)。纯化的漆酶降低了四种不同内分泌干扰化学物质的雌激素活性。然而，漆酶抑制剂曲酸降低了这种效果，这证实了漆酶参与了雌激素活性的去除。
