Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials
The use of light as an external stimulus to control the enzyme activity is an emerging strategy that enables accurate, remote, and noninvasive biotransformations. In this context, immobilization of enzymes on plasmonic nanoparticles offers an opportunity to create light-responsive biocatalytic mater...
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ftunivhelsihelda:oai:helda.helsinki.fi:10138/338157 2024-01-07T09:38:52+01:00 Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials Ribeiro de Barros, Heloise Garcia, Isabel Kuttner, Christian Zeballos, Nicoll Camargo, Pedro H. C. Cordoba de Torresi, Susana Ines Lopez-Gallego, Fernando Liz-Marzan, Luis M. Helsinki Institute of Sustainability Science (HELSUS) Department of Chemistry 2021-12-31T22:35:17Z 10 application/pdf http://hdl.handle.net/10138/338157 eng eng American Chemical Society 10.1021/acscatal.0c04919 The authors thank Brazilian agencies CNPq and São Paulo Research Foundation FAPESP (2015/26308-7 and 2018/13492-2) for financial support. H.R.B. also thanks FAPESP for the fellowships granted (2019/09668-0 and 2017/20892-4). P.H.C.C. thanks FAPESP, the University of Helsinki, and the Jane and Aatos Erkko Foundation for support. C.K. acknowledges funding from the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement No. 799393 (NANOBIOME). L.M.L-.M. and I.G. acknowledge funding from the Spanish State Research Agency (Grant MAT2017-86659-R). Funding from IKERBASQUE to L.M.L-.M. and F.L-.G. is also acknowledged. This work was performed under the Maria de Maeztu Units of Excellence Program from the Spanish State Research Agency—Grant No. MDM-2017-0720. Ribeiro de Barros , H , Garcia , I , Kuttner , C , Zeballos , N , Camargo , P H C , Cordoba de Torresi , S I , Lopez-Gallego , F & Liz-Marzan , L M 2021 , ' Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials ' , ACS catalysis , vol. 11 , no. 1 , pp. 414-423 . https://doi.org/10.1021/acscatal.0c04919 ORCID: /0000-0002-7815-7919/work/89117368 c3b6086b-7dac-49da-9dd8-1bb81e2aa13c http://hdl.handle.net/10138/338157 000606833100040 openAccess info:eu-repo/semantics/openAccess biocatalysis gold nanostructures LSPR-enhanced mechanisms nanotechnology plasmonic heating triggered bioactivity GOLD NANOPARTICLES STABILITY NANOSTARS VISCOSITY KINETICS ENZYMES SURFACE METAL CALB 116 Chemical sciences 221 Nano-technology Article acceptedVersion 2021 ftunivhelsihelda 2023-12-14T00:05:04Z The use of light as an external stimulus to control the enzyme activity is an emerging strategy that enables accurate, remote, and noninvasive biotransformations. In this context, immobilization of enzymes on plasmonic nanoparticles offers an opportunity to create light-responsive biocatalytic materials. Nevertheless, a fundamental and mechanistic understanding of the effects of localized surface plasmon resonance (LSPR) excitation on enzyme regulation remains elusive. We herein investigate the plasmonic effects on biocatalysis using Au nanospheres (AuNSp) and nanostars (AuNSt) as model plasmonic nanoparticles, lipase from Candida antarctica fraction B (CALB) as a proof-of-concept enzyme, and 808 nm as near-infrared light excitation. Our data show that LSPR excitation enables an enhancement of 58% in the enzyme activity for CALB adsorbed on AuNSt, compared with the dark conditions. This work shows how photothermal heating over the LSPR excitation enhances the CALB activity through favoring product release in the last step of the enzyme mechanism. We propose that the results reported herein shed important mechanistic and kinetic insights into the field of plasmonic biocatalysis and may inspire the rational development of plasmonic nanomaterial-enzyme hybrids with tailored activities under external light irradiation. Peer reviewed Article in Journal/Newspaper Antarc* Antarctica HELDA – University of Helsinki Open Repository ACS Catalysis 11 1 414 423 |
institution |
Open Polar |
collection |
HELDA – University of Helsinki Open Repository |
op_collection_id |
ftunivhelsihelda |
language |
English |
topic |
biocatalysis gold nanostructures LSPR-enhanced mechanisms nanotechnology plasmonic heating triggered bioactivity GOLD NANOPARTICLES STABILITY NANOSTARS VISCOSITY KINETICS ENZYMES SURFACE METAL CALB 116 Chemical sciences 221 Nano-technology |
spellingShingle |
biocatalysis gold nanostructures LSPR-enhanced mechanisms nanotechnology plasmonic heating triggered bioactivity GOLD NANOPARTICLES STABILITY NANOSTARS VISCOSITY KINETICS ENZYMES SURFACE METAL CALB 116 Chemical sciences 221 Nano-technology Ribeiro de Barros, Heloise Garcia, Isabel Kuttner, Christian Zeballos, Nicoll Camargo, Pedro H. C. Cordoba de Torresi, Susana Ines Lopez-Gallego, Fernando Liz-Marzan, Luis M. Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials |
topic_facet |
biocatalysis gold nanostructures LSPR-enhanced mechanisms nanotechnology plasmonic heating triggered bioactivity GOLD NANOPARTICLES STABILITY NANOSTARS VISCOSITY KINETICS ENZYMES SURFACE METAL CALB 116 Chemical sciences 221 Nano-technology |
description |
The use of light as an external stimulus to control the enzyme activity is an emerging strategy that enables accurate, remote, and noninvasive biotransformations. In this context, immobilization of enzymes on plasmonic nanoparticles offers an opportunity to create light-responsive biocatalytic materials. Nevertheless, a fundamental and mechanistic understanding of the effects of localized surface plasmon resonance (LSPR) excitation on enzyme regulation remains elusive. We herein investigate the plasmonic effects on biocatalysis using Au nanospheres (AuNSp) and nanostars (AuNSt) as model plasmonic nanoparticles, lipase from Candida antarctica fraction B (CALB) as a proof-of-concept enzyme, and 808 nm as near-infrared light excitation. Our data show that LSPR excitation enables an enhancement of 58% in the enzyme activity for CALB adsorbed on AuNSt, compared with the dark conditions. This work shows how photothermal heating over the LSPR excitation enhances the CALB activity through favoring product release in the last step of the enzyme mechanism. We propose that the results reported herein shed important mechanistic and kinetic insights into the field of plasmonic biocatalysis and may inspire the rational development of plasmonic nanomaterial-enzyme hybrids with tailored activities under external light irradiation. Peer reviewed |
author2 |
Helsinki Institute of Sustainability Science (HELSUS) Department of Chemistry |
format |
Article in Journal/Newspaper |
author |
Ribeiro de Barros, Heloise Garcia, Isabel Kuttner, Christian Zeballos, Nicoll Camargo, Pedro H. C. Cordoba de Torresi, Susana Ines Lopez-Gallego, Fernando Liz-Marzan, Luis M. |
author_facet |
Ribeiro de Barros, Heloise Garcia, Isabel Kuttner, Christian Zeballos, Nicoll Camargo, Pedro H. C. Cordoba de Torresi, Susana Ines Lopez-Gallego, Fernando Liz-Marzan, Luis M. |
author_sort |
Ribeiro de Barros, Heloise |
title |
Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials |
title_short |
Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials |
title_full |
Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials |
title_fullStr |
Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials |
title_full_unstemmed |
Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials |
title_sort |
mechanistic insights into the light-driven catalysis of an immobilized lipase on plasmonic nanomaterials |
publisher |
American Chemical Society |
publishDate |
2021 |
url |
http://hdl.handle.net/10138/338157 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
10.1021/acscatal.0c04919 The authors thank Brazilian agencies CNPq and São Paulo Research Foundation FAPESP (2015/26308-7 and 2018/13492-2) for financial support. H.R.B. also thanks FAPESP for the fellowships granted (2019/09668-0 and 2017/20892-4). P.H.C.C. thanks FAPESP, the University of Helsinki, and the Jane and Aatos Erkko Foundation for support. C.K. acknowledges funding from the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement No. 799393 (NANOBIOME). L.M.L-.M. and I.G. acknowledge funding from the Spanish State Research Agency (Grant MAT2017-86659-R). Funding from IKERBASQUE to L.M.L-.M. and F.L-.G. is also acknowledged. This work was performed under the Maria de Maeztu Units of Excellence Program from the Spanish State Research Agency—Grant No. MDM-2017-0720. Ribeiro de Barros , H , Garcia , I , Kuttner , C , Zeballos , N , Camargo , P H C , Cordoba de Torresi , S I , Lopez-Gallego , F & Liz-Marzan , L M 2021 , ' Mechanistic Insights into the Light-Driven Catalysis of an Immobilized Lipase on Plasmonic Nanomaterials ' , ACS catalysis , vol. 11 , no. 1 , pp. 414-423 . https://doi.org/10.1021/acscatal.0c04919 ORCID: /0000-0002-7815-7919/work/89117368 c3b6086b-7dac-49da-9dd8-1bb81e2aa13c http://hdl.handle.net/10138/338157 000606833100040 |
op_rights |
openAccess info:eu-repo/semantics/openAccess |
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ACS Catalysis |
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11 |
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414 |
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