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

• Published in: Polymers
• Main Authors: Viñambres, Mario, Filice, Marco, Marciello, Marzia
• Other Authors: Ministerio de Economía y Competitividad (España), European Commission, Comunidad de Madrid, Universidad Complutense de Madrid, Consejo Superior de Investigaciones Científicas (España), Fundación Severo Ochoa, Fundación Pro CNIC
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: Multidisciplinary Digital Publishing Institute 2018
• Subjects: Antarc*; Antarctica
• Online Access: http://hdl.handle.net/10261/166925; https://doi.org/10.3390/polym10060615; https://doi.org/10.13039/501100003329; https://doi.org/10.13039/501100000780; https://doi.org/10.13039/501100002911; https://doi.org/10.13039/501100003339; https://doi.org/10.13039/100012818

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. The CNIC is supported by Spanish Ministry for Economy and Competitiveness (MEyC) and the Pro-CNIC Foundation and is a Severo Ochoa Center of Excellence (SEV-2015-0505). M.F. would like to thank MEyC for the research grant ...