2026-07-20T18:21:12Zhttps://docta.ucm.es/rest/oai/request

oai:docta.ucm.es:20.500.14352/127602023-08-25T10:24:18Zcom_20.500.14352_14col_20.500.14352_15

Modulation of the Catalytic Properties of Lipase B from Candida antarctica by Immobilization on Tailor-Made Magnetic Iron Oxide Nanoparticles: The Key Role of Nanocarrier Surface Engineering Viñambres, Mario Filice, Marco Marciello, Marzia The immobilization of biocatalysts on magnetic nanomaterial surface is a very attractive alternative to achieve enzyme nanoderivatives with highly improved properties. The combination between the careful tailoring of nanocarrier surfaces and the site-specific chemical modification of biomacromolecules is a crucial parameter to finely modulate the catalytic behavior of the biocatalyst. In this work, a useful strategy to immobilize chemically aminated lipase B from Candida antárctica on magnetic iron oxide nanoparticles (IONPs) by covalent multipoint attachment or hydrophobic physical adsorption upon previous tailored engineering of nanocarriers with poly-carboxylic groups (citric acid or succinic anhydride, CALBEDA@CA-NPs and CALBEDA@SA-NPs respectively) or hydrophobic layer (oleic acid, CALBEDA@OA-NPs) is described. After full characterization, the nanocatalysts have been assessed in the enantioselective kinetic resolution of racemic methyl mandelate. Depending on the immobilization strategy, each enzymatic nanoderivative permitted to selectively improve a specific property of the biocatalyst. In general, all the immobilization protocols permitted loading from good to high lipase amount (149 < immobilized lipase < 234 mg/gFe). The hydrophobic CALBEDA@OA-NPs was the most active nanocatalyst, whereas the covalent CALBEDA@CA-NPs and CALBEDA@SA-NPs were revealed to be the most thermostable and also the most enantioselective ones in the kinetic resolution reaction (almost 90% ee R-enantiomer). A strategy to maintain all these properties in long-time storage (up to 1 month) by freeze-drying was also optimized. Therefore, the nanocarrier surface engineering is demonstrated to be a key-parameter in the design and preparation of lipase libraries with enhanced catalytic properties. 2023-06-17T12:40:41Z 2023-06-17T12:40:41Z 2023-06-17T12:40:41Z 2018-06-05 journal article https://hdl.handle.net/20.500.14352/12760 2073-4360 10.3390/polym10060615 eng SAF2014-59118-JIN (SEV-2015-0505) 2017-T1/BIO-4992 (Ref. 201760E007) https://creativecommons.org/licenses/by/3.0/es/ open access Atribución 3.0 España MDPI