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...
Published in: | Polymers |
---|---|
Main Authors: | , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
MDPI AG
2018
|
Subjects: | |
Online Access: | https://doi.org/10.3390/polym10060615 https://doaj.org/article/bd15bed5007143f1bc5825c343af2d12 |
id |
ftdoajarticles:oai:doaj.org/article:bd15bed5007143f1bc5825c343af2d12 |
---|---|
record_format |
openpolar |
spelling |
ftdoajarticles:oai:doaj.org/article:bd15bed5007143f1bc5825c343af2d12 2023-05-15T14:02:45+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 2018-06-01T00:00:00Z https://doi.org/10.3390/polym10060615 https://doaj.org/article/bd15bed5007143f1bc5825c343af2d12 EN eng MDPI AG http://www.mdpi.com/2073-4360/10/6/615 https://doaj.org/toc/2073-4360 2073-4360 doi:10.3390/polym10060615 https://doaj.org/article/bd15bed5007143f1bc5825c343af2d12 Polymers, Vol 10, Iss 6, p 615 (2018) colloid surface engineering magnetic iron oxide nanoparticles oriented immobilization lipase catalysis nanotechnology nanobiocatalyst freeze-drying Organic chemistry QD241-441 article 2018 ftdoajarticles https://doi.org/10.3390/polym10060615 2023-01-08T01:31:37Z 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. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Polymers 10 6 615 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
colloid surface engineering magnetic iron oxide nanoparticles oriented immobilization lipase catalysis nanotechnology nanobiocatalyst freeze-drying Organic chemistry QD241-441 |
spellingShingle |
colloid surface engineering magnetic iron oxide nanoparticles oriented immobilization lipase catalysis nanotechnology nanobiocatalyst freeze-drying Organic chemistry QD241-441 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 Organic chemistry QD241-441 |
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 |
Article in Journal/Newspaper |
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 |
MDPI AG |
publishDate |
2018 |
url |
https://doi.org/10.3390/polym10060615 https://doaj.org/article/bd15bed5007143f1bc5825c343af2d12 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Polymers, Vol 10, Iss 6, p 615 (2018) |
op_relation |
http://www.mdpi.com/2073-4360/10/6/615 https://doaj.org/toc/2073-4360 2073-4360 doi:10.3390/polym10060615 https://doaj.org/article/bd15bed5007143f1bc5825c343af2d12 |
op_doi |
https://doi.org/10.3390/polym10060615 |
container_title |
Polymers |
container_volume |
10 |
container_issue |
6 |
container_start_page |
615 |
_version_ |
1766273169501454336 |