Efficient one-step immobilization of CaLB lipase over MOF support NH2-MIL-53(Al)
peer-reviewed 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 pl...
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Online Access: | http://hdl.handle.net/10344/9118 https://doi.org/10.3390/catal10080918 |
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ftunivlimerick:oai:ulir.ul.ie:10344/9118 2023-05-15T14:03:30+02:00 Efficient one-step immobilization of CaLB lipase over MOF support NH2-MIL-53(Al) Gascón-Pérez, Victoria Jiménez, Mayra Belen Molina, Asunción M. Blanco, Rosa María Sánchez-Sánchez, Manuel Spanish State Research Agency IRC 2020 http://hdl.handle.net/10344/9118 https://doi.org/10.3390/catal10080918 eng eng MDPI MAT2016-77496-R Catalysts;10, 918 GOIPD/2015/287 http://hdl.handle.net/10344/9118 doi:10.3390/catal10080918 info:eu-repo/semantics/openAccess nano crystalline CaLB lipase enzyme immobilization info:eu-repo/semantics/article all_ul_research ul_published_reviewed 2020 ftunivlimerick https://doi.org/10.3390/catal10080918 2022-05-23T15:14:25Z peer-reviewed 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 NH2-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* Antarctica University of Limerick: Institutional Repository (ULIR) Catalysts 10 8 918 |
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Open Polar |
collection |
University of Limerick: Institutional Repository (ULIR) |
op_collection_id |
ftunivlimerick |
language |
English |
topic |
nano crystalline CaLB lipase enzyme immobilization |
spellingShingle |
nano crystalline CaLB lipase enzyme immobilization Gascón-Pérez, Victoria Jiménez, Mayra Belen Molina, Asunción M. Blanco, Rosa María Sánchez-Sánchez, Manuel Efficient one-step immobilization of CaLB lipase over MOF support NH2-MIL-53(Al) |
topic_facet |
nano crystalline CaLB lipase enzyme immobilization |
description |
peer-reviewed 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 NH2-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. |
author2 |
Spanish State Research Agency IRC |
format |
Article in Journal/Newspaper |
author |
Gascón-Pérez, Victoria Jiménez, Mayra Belen Molina, Asunción M. Blanco, Rosa María Sánchez-Sánchez, Manuel |
author_facet |
Gascón-Pérez, Victoria Jiménez, Mayra Belen Molina, Asunción M. Blanco, Rosa María Sánchez-Sánchez, Manuel |
author_sort |
Gascón-Pérez, Victoria |
title |
Efficient one-step immobilization of CaLB lipase over MOF support NH2-MIL-53(Al) |
title_short |
Efficient one-step immobilization of CaLB lipase over MOF support NH2-MIL-53(Al) |
title_full |
Efficient one-step immobilization of CaLB lipase over MOF support NH2-MIL-53(Al) |
title_fullStr |
Efficient one-step immobilization of CaLB lipase over MOF support NH2-MIL-53(Al) |
title_full_unstemmed |
Efficient one-step immobilization of CaLB lipase over MOF support NH2-MIL-53(Al) |
title_sort |
efficient one-step immobilization of calb lipase over mof support nh2-mil-53(al) |
publisher |
MDPI |
publishDate |
2020 |
url |
http://hdl.handle.net/10344/9118 https://doi.org/10.3390/catal10080918 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
MAT2016-77496-R Catalysts;10, 918 GOIPD/2015/287 http://hdl.handle.net/10344/9118 doi:10.3390/catal10080918 |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.3390/catal10080918 |
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Catalysts |
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10 |
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8 |
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918 |
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1766274182474104832 |