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
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 biomacromolecul...
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ftmdpi:oai:mdpi.com:/2073-4360/10/6/615/ 2023-08-20T04:02:31+02:00 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 Mario Viñambres Marco Filice Marzia Marciello 2018-06-05 application/pdf https://doi.org/10.3390/polym10060615 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/polym10060615 https://creativecommons.org/licenses/by/4.0/ Polymers; Volume 10; Issue 6; Pages: 615 colloid surface engineering magnetic iron oxide nanoparticles oriented immobilization lipase catalysis nanotechnology nanobiocatalyst freeze-drying Text 2018 ftmdpi https://doi.org/10.3390/polym10060615 2023-07-31T21:33:39Z 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. Text Antarc* Antarctica MDPI Open Access Publishing Polymers 10 6 615 |
institution |
Open Polar |
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MDPI Open Access Publishing |
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language |
English |
topic |
colloid surface engineering magnetic iron oxide nanoparticles oriented immobilization lipase catalysis nanotechnology nanobiocatalyst freeze-drying |
spellingShingle |
colloid surface engineering magnetic iron oxide nanoparticles oriented immobilization lipase catalysis nanotechnology nanobiocatalyst freeze-drying Mario Viñambres Marco Filice Marzia Marciello 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 |
topic_facet |
colloid surface engineering magnetic iron oxide nanoparticles oriented immobilization lipase catalysis nanotechnology nanobiocatalyst freeze-drying |
description |
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. |
format |
Text |
author |
Mario Viñambres Marco Filice Marzia Marciello |
author_facet |
Mario Viñambres Marco Filice Marzia Marciello |
author_sort |
Mario Viñambres |
title |
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 |
title_short |
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 |
title_full |
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 |
title_fullStr |
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 |
title_full_unstemmed |
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 |
title_sort |
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 |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2018 |
url |
https://doi.org/10.3390/polym10060615 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Polymers; Volume 10; Issue 6; Pages: 615 |
op_relation |
https://dx.doi.org/10.3390/polym10060615 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/polym10060615 |
container_title |
Polymers |
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10 |
container_issue |
6 |
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615 |
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1774713015599366144 |