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: Vinambres, Mario, Filice, Marco, Marciello, Marzia
• Other Authors: Ministerio de Economía y Competitividad (España), Fundación ProCNIC, Unión Europea. Fondo Europeo de Desarrollo Regional (FEDER/ERDF), Complutense University of Madrid (España), Comunidad de Madrid (España)
• Format: Article in Journal/Newspaper
• Language: English
• Published: Multidisciplinary Digital Publishing Institute (MDPI) 2018
• Subjects: 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; Antarc*; Antarctica
• Online Access: https://hdl.handle.net/20.500.12105/6579; https://doi.org/10.3390/polym10060615

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 ...