Glutaraldehyde cross-linking of immobilized thermophilic esterase on hydrophobic macroporous resin for application in poly(ε-caprolactone) synthesis.
Glutaraldehyde cross-linking of immobilized thermophilic esterase on hydrophobic macroporous resin for application in poly(ε-caprolactone) synthesis.
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DOI：
10.3390/molecules19079838
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发表时间：
2014-07-08
期刊：
影响因子：
--
通讯作者：
Li Q
中科院分区：
文献类型：
--
作者：
Wang M;Shi H;Wu D;Han H;Zhang J;Xing Z;Wang S;Li Q
利用疏水性大孔吸附树脂Sepbeads EC-OD，通过戊二醛介导的共价偶联，成功构建了固定化黄褐古细菌嗜热酯酶。通过0.05%的戊二醛处理，可以在防止酶浸的同时保持催化活性。以ε-己内酯的酶促开环聚合反应为模型，系统研究了有机溶剂和反应温度对单体转化率和产物相对分子质量的影响。通过对反应条件的优化，得到了单体转化率为100%、锰值低于1010g/mol的产物。交联型固定化嗜热酯酶具有良好的操作稳定性，12次反应单体转化率均在90%以上，16次反应后单体转化率仍在80%以上。
The immobilized thermophilic esterase from Archaeoglobus fulgidus was successfully constructed through the glutaraldehyde-mediated covalent coupling after its physical adsorption on a hydrophobic macroporous resin, Sepabeads EC-OD. Through 0.05% glutaraldehyde treatment, the prevention of enzyme leaching and the maintenance of catalytic activity could be simultaneously realized. Using the enzymatic ring-opening polymerization of ε-caprolactone as a model, effects of organic solvents and reaction temperature on the monomer conversion and product molecular weight were systematically investigated. After the optimization of reaction conditions, products were obtained with 100% monomer conversion and Mn values lower than 1010 g/mol. Furthermore, the cross‑linked immobilized thermophilic esterase exhibited an excellent operational stability, with monomer conversion values exceeding 90% over the course of 12 batch reactions, still more than 80% after 16 batch reactions.
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影响因子：
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作者：
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