Department of Chemistry, Institute of Chemical Technology, Matunga, Mumbai, 400 019, India, India.
Department of Chemistry, Institute of Chemical Technology, Matunga, Mumbai, 400 019, India, India.
J Biotechnol. 2017 Nov 20;262:1-10. doi: 10.1016/j.jbiotec.2017.09.017. Epub 2017 Sep 25.
Kinetic resolution of rac-1,2-diols using the biocatalyst Burkholderia cepacia lipase (BCL) immobilized on a biodegradable binary blend support of hydroxypropyl methyl cellulose(HPMC)/polyvinyl alcohol (PVA) has been investigated. The immobilization technique improved enzyme activity significantly and it has excellent recyclability with good yield and enantiomeric excess values up to the studied range of nine cycles. At optimum reaction conditions, conversion of 45-50% with excellent enantiomeric excess (up to 99% ee) were obtained. It was observed that BCL shows enantio-preference to R form of primary hydroxyl group for acylation, whereas S form is preferred for diacetate formation. The resultant products were characterized with the help of different analytical techniques such as H and C NMR, chiral HPLC, IR and GC-MS. In order to understand the effect of solvent as well as various derivatives of substrates, combined molecular dynamics and docking simulations were carried out. Explanation related to experimentally observed enantio-selectivities have been provided based on transition state structures of acylated complexes.
利用固定在羟丙基甲基纤维素（HPMC）/聚乙烯醇（PVA）可生物降解二元共混载体上的生孢伯克霍尔德氏菌脂肪酶（BCL）对 rac-1,2-二醇进行动力学拆分进行了研究。固定化技术显著提高了酶的活性，并且在研究的九轮循环范围内具有极好的可回收性，收率和对映体过量值都很好。在最佳反应条件下，可获得 45-50%的转化率和极好的对映体过量值（高达 99%ee）。观察到 BCL 对酰化的伯羟基的 R 形式表现出对映体选择性，而 S 形式则优先用于二乙酸酯形成。借助不同的分析技术，如 H 和 C NMR、手性 HPLC、IR 和 GC-MS，对所得产物进行了表征。为了了解溶剂以及底物的各种衍生物的影响，进行了组合分子动力学和对接模拟。根据酰化配合物的过渡态结构，提供了对实验观察到的对映选择性的解释。
