Preparation of One‐Pot Immobilized Lipase with Fe3O4 Nanoparticles Into Metal‐Organic Framework For Enantioselective Hydrolysis of (R,S)‐Naproxen Methyl Ester

Abstract Immobilization of enzyme to magnetic metal‐organic frameworks (MOF) can preserve biological functionality in harsh environments to increase enzymes activity, stability, and improve reusability. The magnetic Fe 3 O 4 nanoparticles were treated with calix[4]arene tetracarboxylic acid (Calix) and Candida rugosa lipase (CRL), and then encapsulated into the zeolitic imidazole framework‐8 (Fe 3 O 4 @Calix‐ZIF‐8@CRL). The lipase activity data of Fe 3 O 4 @Calix‐ZIF‐8@CRL was 2.88 times higher than that of the Fe 3 O 4 @ZIF‐8@CRL (without Calix). The catalytic properties of immobilized lipases were studied on the enantioselective hydrolysis of R/S‐naproxen methyl ester. It was also observed that Fe 3 O 4 @Calix‐ZIF‐8@CRL has excellent enantioselectivity (E=371) compared to Fe 3 O 4 @ZIF‐8@CRL (E=131). Furthermore, Fe 3 O 4 @Calix‐ZIF‐8@CRL was seen to still retain 30 % of the conversion rate after the fifth reuse. This work may also be useful for the pharmaceutical industry due to the increased reusability and stability of enzymes, the enantiomeric selectivity exhibited by MOF‐enzyme biocomposites, and the significant differences in the biological activities of the enantiomers.