2026-07-21T11:48:45Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/65792024-09-27T10:15:24Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19607
Repisalud
author
Vinambres, Mario
author
Filice, Marco
author
Marciello, Marzia
funder
Ministerio de Economía y Competitividad (España)
funder
Fundación ProCNIC
funder
Unión Europea. Fondo Europeo de Desarrollo Regional (FEDER/ERDF)
funder
Complutense University of Madrid (España)
funder
Comunidad de Madrid (España)
2018-11-05T11:58:22Z
2018-11-05T11:58:22Z
2018
Polymers. 2018; 10(6):615
10.3390/polym10060615
2073-4360
Polymers
http://hdl.handle.net/20.500.12105/6579
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 antarctica 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, CALB(EDA)@CA-NPs and CALB(EDA)@SA-NPs respectively) or hydrophobic layer (oleic acid, CALB(EDA)@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/g(Fe)). The hydrophobic CALB(EDA)@OA-NPs was the most active nanocatalyst, whereas the covalent CALB(EDA)@CA-NPs and CALB(EDA)@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.
eng
Colloid surface engineering
Magnetic iron oxide nanoparticles
Oriented immobilization
Lipase
Catalysis
Nanotechnology
Nanobiocatalyst
Freeze-drying
GAMMA-FE2O3 NANOPARTICLES
BIOMEDICAL APPLICATIONS
ENZYME IMMOBILIZATION
CHEMICAL-MODIFICATION
HYDROPHOBIC SUPPORTS
SOLID-PHASE
STRATEGIES
STABILIZATION
BIOCATALYSTS
HYPERTHERMIA
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
journal article
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ModulationCatalyticPropertiesLipase_2018.pdf
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ModulationCatalyticPropertiesLipase_2018_SUPPL.pdf
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ModulationCatalyticPropertiesLipase_2018.pdf.txt
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ModulationCatalyticPropertiesLipase_2018_SUPPL.pdf.txt