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Polymers 2018, 10(6), 615; https://doi.org/10.3390/polym10060615

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

1
Department of Biomaterials and Bioinspired Material, Materials Science Institute of Madrid (ICMM-CSIC), Sor Juana Inés de la Cruz 3, Cantoblanco, 28049 Madrid, Spain
2
Department of Chemistry in Pharmaceutical Sciences, Faculty of Pharmacy, Complutense University (UCM), Plaza Ramón y Cajal, 28040 Madrid, Spain
3
National Research Centre for Cardiovascular Disease (CNIC), C/Melchor Fernández-Almagro 3, 28029 Madrid, Spain
4
Biomedical Research Networking Center for Respiratory Diseases (CIBERES), C/Melchor Fernández-Almagro 3, 28029 Madrid, Spain
*
Authors to whom correspondence should be addressed.
Received: 5 April 2018 / Revised: 27 May 2018 / Accepted: 30 May 2018 / Published: 5 June 2018
(This article belongs to the Special Issue Selected Papers from "ECIS 2017")
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Abstract

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, 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. View Full-Text
Keywords: colloid surface engineering; magnetic iron oxide nanoparticles; oriented immobilization; lipase; catalysis; nanotechnology; nanobiocatalyst; freeze-drying colloid surface engineering; magnetic iron oxide nanoparticles; oriented immobilization; lipase; catalysis; nanotechnology; nanobiocatalyst; freeze-drying
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Viñambres, M.; Filice, M.; Marciello, M. 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. Polymers 2018, 10, 615.

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