Ring-opening polymerization of ε-caprolactone catalyzed by a novel thermophilic esterase from the archaeon Archaeoglobus fulgidus
Ring-opening polymerization of ε-caprolactone catalyzed by a novel thermophilic esterase from the archaeon Archaeoglobus fulgidus
复制标题
DOI：
10.1016/j.molcatb.2008.03.012
复制
发表时间：
2009-02-01
影响因子：
--
通讯作者：
Feng, Yan
中科院分区：
文献类型：
--
作者：
Ma, Jiutong;Li, Quanshun;Feng, Yan
由古细菌Archaeoglobus fulgidus的新型嗜热酯酶催化的ε-己内酯的开环聚合在有机溶剂中成功进行。酶浓度、温度、反应时间、反应介质的影响。研究了水活性对单体转化率和产物分子量的影响。聚(ε-己内酯)的单体转化率几乎为100%，在甲苯中80℃反应72小时，数均分子量为1400。此外，Michaelis-Menten动力学分析表明，与其他报道的脂肪酶相比，该酶对ε-己内酯具有最高的亲和力，K-m值为0.093 mol/l。通过分子对接研究，研究了酶对 K-m 值可能的结构和能量影响。 (C) 2008 Elsevier B.V. 保留所有权利。
The ring-opening polymerization of epsilon-caprolactone catalyzed by a novel thermophilic esterase from the archaeon Archaeoglobus fulgidus was successfully conducted in organic solvents. The effects of enzyme concentration, temperature, reaction time, reaction medium. and water activity on monomer conversion and product molecular weight were investigated. Poly(epsilon-caprolactone) was obtained in almost 100% of the monomer conversion, with a number-average molecular weight of 1400 in toluene at 80 degrees C for 72 h. Furthermore, the Michaelis-Menten kinetic analysis showed that the enzyme had the highest affinity for epsilon-caprolactone, with a K-m value of 0.093 mol/l compared with other reported lipases. The possible structural and energetic effects of the enzyme on the K-m value were investigated, using molecular docking studies. (C) 2008 Elsevier B.V. All rights reserved.