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A Green Approach towards the Synthesis of Enantio Pure Diols Using Horse Radish Peroxidase Enzyme Immobilized on Magnetic Nanoparticles

机译:用辣根过氧化物酶固定在磁性纳米颗粒上的绿色方法合成对映体纯二醇

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Enantiopure epoxides and their corresponding chiral vicinal diols serve as valuable intermediates in the synthesis of biologically active pharma and agro-compounds and also value added fine chemicals. Biocatalysts are well known for their selective hydrolysis of racemic epoxides to give optically pure chiral diols. This study highlights an efficient process of synthesis of chiral vicinal diols in good yields and enantioselectiviy using horse radish peroxidase enzyme immobilized on the amine functionalized magnetic nano particles (Fe3O4 nanoparticles) as enzyme carriers. It also facilitates separation of MNP-immobilized enzymes by applying external magnetic field. The immobilization of magnetic nano particles was confirmed by transmission electron microscope (TEM) and scanning electron microscope (SEM). The MNP-immobilized peroxidase enzyme improved stability of the enzyme and has shown broader substrate specificity in enantioselective hydrolysis of racemic epoxides, under mild and environmentally friendly conditions. The methodology MNP-immobilized enzyme developed in the synthesis of chiral diols has a potential for use in large-scale applications.
机译:对映体纯环氧化合物及其相应的手性邻位二醇是生物活性药物和农用化合物合成中的有价值的中间体,还可以用作增值精细化学品。生物催化剂因其外消旋环氧化物的选择性水解而产生光学纯的手性二醇而众所周知。这项研究强调了使用固定在胺官能化磁性纳米颗粒(Fe3O4纳米颗粒)上的辣根过氧化物酶作为酶载体,可以高效,高收率和对映选择性合成手性邻位二醇的方法。通过施加外部磁场,它也有助于分离固定有MNP的酶。通过透射电子显微镜(TEM)和扫描电子显微镜(SEM)确认了磁性纳米颗粒的固定。 MNP固定的过氧化物酶提高了酶的稳定性,并且在温和且环境友好的条件下,在外消旋环氧化物的对映选择性水解中显示了更广泛的底物特异性。在手性二醇的合成中开发的固定化MNP的酶学方法具有用于大规模应用的潜力。

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