In this study, a new biocatalyst was prepared by immobilizing Candida rugosa lipase epichlorohydrin-functionalized onto the surface of the nanoparticles. Magnetite nanoparticles were obtained by chemical co-precipitation method of Fe2+ and Fe3+, and then the prepared uncoated and coated nanoparticles were characterized by XRD, FT-IR and TGA. Lipase was covalently attached to activated nanoparticles. The catalytic properties of free and immobilized lipases were determined. It was found that the optimum temperature for free and immobilized lipases was 30 °C and 35 °C, respectively. The optimum pH values were found to be 7.0 and 8 for free and immobilized lipases, respectively. Immobilized lipase was found to retain significant activity even after the seventh use. In the final section of the study, optically pure compounds were obtained by carrying out the enantioselective hydrolysis studies of racemic esters by using immobilized lipase. Enantiomeric excesses of the products in the enantioselective hydrolysis of racemic ibuprofen and naproxen methyl ester and racemic butyl mandelate were determined to be 94.93, 77.30 and 68.15, respectively.

中文翻译：

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环氧念珠菌脂肪酶在表氯醇包覆的磁铁矿纳米粒子上的共价固定化：一些消旋酯的对映选择性水解研究和HPLC分析。

在这项研究中，通过将功能化的念珠菌脂肪酶表氯醇固定在纳米颗粒的表面上，制备了一种新的生物催化剂。通过Fe2 +和Fe3 +的化学共沉淀法获得磁铁矿纳米粒子，然后通过XRD，FT-IR和TGA对制备的未包覆和包覆的纳米粒子进行表征。脂肪酶共价附于活化的纳米颗粒。测定了游离和固定化脂肪酶的催化性能。发现游离和固定的脂肪酶的最佳温度分别为30℃和35℃。发现游离和固定脂肪酶的最佳pH值分别为7.0和8。发现固定化脂肪酶即使在第七次使用后仍保持显着活性。在研究的最后部分，通过使用固定化脂肪酶进行外消旋酯的对映选择性水解研究，获得了光学纯的化合物。测定外消旋布洛芬和萘普生甲酯和外消旋扁桃酸酯的对映选择性水解中产物的对映体过量分别为94.93、77.30和68.15。