Zhang Hong, Xun Erna, Wang Jiaxin, Chen Ge, Cheng Tiexin, Wang Zhi, Ji Tengfei, Wang Lei
College of Chemistry, Jilin University, Changchun 130023, China.
Key Laboratory of Molecular Enzymology and Engineering of Ministry of Education, College of Life Sciences, Jilin University, Changchun 130023, China.
Int J Mol Sci. 2012;13(5):5998-6008. doi: 10.3390/ijms13055998. Epub 2012 May 18.
Trametes Villosa Laccase (TVL) was immobilized through physical adsorption on SBA-15 mesoporous silica and the immobilized TVL was used in the oxidative coupling of trans-resveratrol. Higher loading and activity of the immobilized enzyme on SBA-15 were obtained when compared with the free enzyme. The effects of reaction conditions, such as buffer type, pH, temperature and substrate concentration were investigated, and the optimum conditions were screened and resulted in enzyme activity of up to 10.3 μmol/g·h. Furthermore, the oxidative couplings of the derivatives of trans-resveratrol were also catalyzed by immobilized TVL. The immobilized TVL was recyclable and could maintain 78% of its initial activity after reusing it four times.
通过物理吸附将绒毛栓菌漆酶（TVL）固定在SBA - 15介孔二氧化硅上，并将固定化的TVL用于反式白藜芦醇的氧化偶联反应。与游离酶相比，固定化酶在SBA - 15上具有更高的负载量和活性。研究了反应条件如缓冲液类型、pH、温度和底物浓度的影响，筛选出了最佳条件，酶活性高达10.3 μmol/g·h。此外，固定化的TVL还催化了反式白藜芦醇衍生物的氧化偶联反应。固定化的TVL可循环使用，重复使用四次后可保持其初始活性的78%。
