多氯联苯降解酶的分离纯化及酶学性质研究

摘要

The PCB-degrading enzyme was isolated and purified from the fermentation broth of Staphylococcus epiderrnidis by ammonium sulfate precipitation, dialysis and Sephadex G-150 gel chromatography. The activity of the PCB-degrading enzymes could increase to 442.29 U/mg after purified by 30％～80％ of (NH4)2SO4 precipitations, and could increase to 480.75 U/mg after dialysis. The activity could finally increase to 6 903.57 U/mg after purified by gel chromatography, as the purification fold was 35.9; and the recovery rate was 30.56％. The optimum pH of PCB-degrading enzyme was 7.0, and it was stable at pH 6.0～9.0 and 30～45 C. Cu2+ and Fe2+ had stone inhibition to this enzyme.%采用硫酸铵盐析浓缩、透析、Sephdex G-150凝胶过滤层析,对表皮葡萄球菌产生的多氯联苯(PCBs)降解酶进行分离纯化.粗酶经30%～80%饱和度硫酸铵沉淀法纯化后比酶活可提高到442.29 U/mg;经透析后的比酶活可提高到480.75 U/mg;最后经凝胶层析法纯化后的比酶活可提高到6 903.57 U/mg,纯化倍数为35.9,回收率为30.56%.酶催化反应的最适pH值为7.0;在pH值6.0～9.0,温度为30～45℃时具有较好的稳定性;Cu2+、Fe2+对酶有一定的抑制作用.