Salgin, SemaCakal, MustafaSalgin, Ugur2024-10-262024-10-2620201082-60681532-2297https://doi.org/10.1080/10826068.2019.1679178https://hdl.handle.net/20.500.12418/28274In this study, the non-magnetic and the magnetic cross-linked enzyme aggregates (CLEAs) from Candida rugosa lipase were synthesized to catalyze the kinetic resolution reaction of naproxen methyl ester (NME). Magnetic iron oxide nanoparticles (MIONPs) were produced through co-precipitation method and their surfaces were modified by silanization reaction. The MIONPs were used as a platform to synthesize the magnetic CLEAs (M-CLEAs). The biocatalysts and MIONPs synthesized were characterized by FTIR spectroscopy and SEM analysis. The kinetic resolution of racemic NME was studied in aqueous buffer solution/isooctane biphasic system to compare the performance of M-CLEAs and CLEAs. The effects of reaction parameters such as temperature, pH, stirring rate on the enantiomeric excess of the substrate (ee(s)%) were investigated in a batch reactor system. The activity recovery of CRL enzyme in CLEAs was higher than M-CLEAs. Compared with M-CLEAs, CLEAs biocatalysts had previously reached ee(s)% values. Although both biocatalysts showed similar cavity structure from SEM analysis, the lower performance of M-CLEAs may be due to the different microenvironments of M-CLEAs from CLEAs. However, the reusability performance of M-CLEAs was higher than that of CLEAs. The optimal reaction conditions for M-CLEAs and CLEAs were found to be 37 degrees C, pH 7.5, and 300 rpm.en10.1080/10826068.2019.1679178info:eu-repo/semantics/closedAccessCLEAskinetic resolutionlipasemagnetic CLEAsnaproxen methyl esterKinetic resolution of racemic naproxen methyl ester by magnetic and non-magnetic cross-linked lipase aggregatesArticle502155148316473662-s2.0-85074462152Q3WOS:000492310300001Q4