Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH 2 -MIL-53(Al)

Metal-organic framework (MOF) materials possess the widest versatility in structure, composition, and synthesis procedures amongst the known families of materials. On the other hand, the extraordinary affinity between MOFs and enzymes has led to widely investigating these materials as platforms to s...

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Published in:Catalysts
Main Authors: Victoria Gascón-Pérez, Mayra Belen Jiménez, Asunción Molina, Rosa María Blanco, Manuel Sánchez-Sánchez
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2020
Subjects:
Online Access:https://doi.org/10.3390/catal10080918
https://doaj.org/article/bbd4d768afa8415c8446d49af433ccb6
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spelling ftdoajarticles:oai:doaj.org/article:bbd4d768afa8415c8446d49af433ccb6 2024-10-29T17:41:08+00:00 Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH 2 -MIL-53(Al) Victoria Gascón-Pérez Mayra Belen Jiménez Asunción Molina Rosa María Blanco Manuel Sánchez-Sánchez 2020-08-01T00:00:00Z https://doi.org/10.3390/catal10080918 https://doaj.org/article/bbd4d768afa8415c8446d49af433ccb6 EN eng MDPI AG https://www.mdpi.com/2073-4344/10/8/918 https://doaj.org/toc/2073-4344 doi:10.3390/catal10080918 https://doaj.org/article/bbd4d768afa8415c8446d49af433ccb6 Catalysts, Vol 10, Iss 8, p 918 (2020) CaLB lipase enzyme immobilization in situ MOF support nanocrystalline NH 2 -MIL-53(Al) Chemical technology TP1-1185 Chemistry QD1-999 article 2020 ftdoajarticles https://doi.org/10.3390/catal10080918 2024-10-09T17:27:43Z Metal-organic framework (MOF) materials possess the widest versatility in structure, composition, and synthesis procedures amongst the known families of materials. On the other hand, the extraordinary affinity between MOFs and enzymes has led to widely investigating these materials as platforms to support these catalytic proteins in recent years. In this work, the MOF material NH 2 -MIL-53(Al) has been tested as a support to immobilize by one-step methodology (in situ) the enzyme lipase CaLB from Candida antarctica by employing conditions that are compatible with its enzymatic activity (room temperature, aqueous solution, and moderate pH values). Once the nature of the linker deprotonating agent or the synthesis time were optimized, the MOF material resulted in quite efficient entrapping of the lipase CaLB through this in situ approach (>85% of the present enzyme in the synthesis media) while the supported enzyme retained acceptable activity (29% compared to the free enzyme) and had scarce enzyme leaching. The equivalent post-synthetic method led to biocatalysts with lower enzyme loading values. These results make clear that the formation of MOF support in the presence of the enzyme to be immobilized substantially improves the efficiency of the biocatalysts support for retaining the enzyme and limits their leaching. Article in Journal/Newspaper Antarc* Directory of Open Access Journals: DOAJ Articles Catalysts 10 8 918
institution Open Polar
collection Directory of Open Access Journals: DOAJ Articles
op_collection_id ftdoajarticles
language English
topic CaLB lipase
enzyme immobilization
in situ
MOF support
nanocrystalline
NH 2 -MIL-53(Al)
Chemical technology
TP1-1185
Chemistry
QD1-999
spellingShingle CaLB lipase
enzyme immobilization
in situ
MOF support
nanocrystalline
NH 2 -MIL-53(Al)
Chemical technology
TP1-1185
Chemistry
QD1-999
Victoria Gascón-Pérez
Mayra Belen Jiménez
Asunción Molina
Rosa María Blanco
Manuel Sánchez-Sánchez
Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH 2 -MIL-53(Al)
topic_facet CaLB lipase
enzyme immobilization
in situ
MOF support
nanocrystalline
NH 2 -MIL-53(Al)
Chemical technology
TP1-1185
Chemistry
QD1-999
description Metal-organic framework (MOF) materials possess the widest versatility in structure, composition, and synthesis procedures amongst the known families of materials. On the other hand, the extraordinary affinity between MOFs and enzymes has led to widely investigating these materials as platforms to support these catalytic proteins in recent years. In this work, the MOF material NH 2 -MIL-53(Al) has been tested as a support to immobilize by one-step methodology (in situ) the enzyme lipase CaLB from Candida antarctica by employing conditions that are compatible with its enzymatic activity (room temperature, aqueous solution, and moderate pH values). Once the nature of the linker deprotonating agent or the synthesis time were optimized, the MOF material resulted in quite efficient entrapping of the lipase CaLB through this in situ approach (>85% of the present enzyme in the synthesis media) while the supported enzyme retained acceptable activity (29% compared to the free enzyme) and had scarce enzyme leaching. The equivalent post-synthetic method led to biocatalysts with lower enzyme loading values. These results make clear that the formation of MOF support in the presence of the enzyme to be immobilized substantially improves the efficiency of the biocatalysts support for retaining the enzyme and limits their leaching.
format Article in Journal/Newspaper
author Victoria Gascón-Pérez
Mayra Belen Jiménez
Asunción Molina
Rosa María Blanco
Manuel Sánchez-Sánchez
author_facet Victoria Gascón-Pérez
Mayra Belen Jiménez
Asunción Molina
Rosa María Blanco
Manuel Sánchez-Sánchez
author_sort Victoria Gascón-Pérez
title Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH 2 -MIL-53(Al)
title_short Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH 2 -MIL-53(Al)
title_full Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH 2 -MIL-53(Al)
title_fullStr Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH 2 -MIL-53(Al)
title_full_unstemmed Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH 2 -MIL-53(Al)
title_sort efficient one-step immobilization of calb lipase over mof support nh 2 -mil-53(al)
publisher MDPI AG
publishDate 2020
url https://doi.org/10.3390/catal10080918
https://doaj.org/article/bbd4d768afa8415c8446d49af433ccb6
genre Antarc*
genre_facet Antarc*
op_source Catalysts, Vol 10, Iss 8, p 918 (2020)
op_relation https://www.mdpi.com/2073-4344/10/8/918
https://doaj.org/toc/2073-4344
doi:10.3390/catal10080918
https://doaj.org/article/bbd4d768afa8415c8446d49af433ccb6
op_doi https://doi.org/10.3390/catal10080918
container_title Catalysts
container_volume 10
container_issue 8
container_start_page 918
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