Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario, Canada.
Water Environ Res. 2010 Nov;82(11):2285-9. doi: 10.2175/106143010x12681059116617.
This paper demonstrates, for the first time, the capability of soybean peroxidase (SBP), an enzyme, for catalyzing the removal of an aromatic thiol, 2-mercaptobenzothiazole (MBT), from aqueous solution. The optimum pH for enzymatic conversion of MBT in aqueous buffer was found to be in the range 6.0 to 9.0. The optimum hydrogen peroxide (H2O2): MBT stoichiometry was 0.6. In terms of standard units (U) of catalytic activity, the minimum SBP concentration required for 95% conversion of 1.0 mM MBT in 3 hours was found to be 0.9 U/mL. The presence of polyethylene glycol at 50 mg/L can reduce the enzyme concentration required for the same conversion by 3-fold. It is proposed that these findings should be the basis for viable and cost-effective treatment of MBT in industrial wastewater and/or process water.
本文首次证明了大豆过氧化物酶(SBP)作为一种酶,能够催化从水溶液中去除芳香族硫醇 2-巯基苯并噻唑(MBT)。发现酶促转化 MBT 的最佳 pH 值范围在 6.0 到 9.0 之间。最佳的过氧化氢(H2O2):MBT 计量比为 0.6。就催化活性的标准单位(U)而言,在 3 小时内将 1.0 mM MBT 转化 95%所需的最小 SBP 浓度为 0.9 U/mL。在 50 mg/L 的聚乙二醇存在下,可以将相同转化率所需的酶浓度降低 3 倍。据推测,这些发现应该是在工业废水和/或工艺水中处理 MBT 的可行且具有成本效益的方法的基础。