Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized Candida antarctica lipase B
Elongated flexuous plant viral nanoparticles (VNPs) represent an interesting platform for developing different applications in nanobiotechnology. In the case of potyviruses, the virion external surface is made up of helically-arrayed domains of the viral structural coat protein (CP), repeated over 2...
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ftdoajarticles:oai:doaj.org/article:ca7ed944274c40b89b7ecc8d1a764495 2023-05-15T13:53:48+02:00 Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized Candida antarctica lipase B Sol eCuenca Carmen eMansilla Marta eAguado Carmen eYuste-Calvo Flora eSánchez Jose María eSánchez-Montero Fernando ePonz 2016-04-01T00:00:00Z https://doi.org/10.3389/fpls.2016.00464 https://doaj.org/article/ca7ed944274c40b89b7ecc8d1a764495 EN eng Frontiers Media S.A. http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00464/full https://doaj.org/toc/1664-462X 1664-462X doi:10.3389/fpls.2016.00464 https://doaj.org/article/ca7ed944274c40b89b7ecc8d1a764495 Frontiers in Plant Science, Vol 7 (2016) turnip mosaic virus Chemical conjugation Nanobiocatalysis nanonets Enzyme Nanoimmobilization Plant culture SB1-1110 article 2016 ftdoajarticles https://doi.org/10.3389/fpls.2016.00464 2022-12-31T03:16:53Z Elongated flexuous plant viral nanoparticles (VNPs) represent an interesting platform for developing different applications in nanobiotechnology. In the case of potyviruses, the virion external surface is made up of helically-arrayed domains of the viral structural coat protein (CP), repeated over 2000 times, in which the N- and C-terminal domains of each CP are projected towards the exterior of the external virion surface. These characteristics provide a chemical environment rich in functional groups susceptible to chemical conjugations. We have conjugated Candida antarctica lipase B (CALB) onto amino groups of the external surface of the potyvirus turnip mosaic virus (TuMV) using glutaraldehyde as a conjugating agent. Using this approach, TuMV virions were transformed into scaffolds for CALB nanoimmobilization. Analysis of the resulting structures revealed the formation of TuMV nanonets onto which large CALB aggregates were deposited. The functional enzymatic characterization of the CALB-bearing TuMV nanonets showed that CALB continued to be active in the nanoimmobilized form, even gaining an increased relative specific activity, as compared to the non-immobilized form. These novel virus-based nanostructures may provide a useful new approach to enzyme nanoimmobilization susceptible to be industrially exploited. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Frontiers in Plant Science 7 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
turnip mosaic virus Chemical conjugation Nanobiocatalysis nanonets Enzyme Nanoimmobilization Plant culture SB1-1110 |
spellingShingle |
turnip mosaic virus Chemical conjugation Nanobiocatalysis nanonets Enzyme Nanoimmobilization Plant culture SB1-1110 Sol eCuenca Carmen eMansilla Marta eAguado Carmen eYuste-Calvo Flora eSánchez Jose María eSánchez-Montero Fernando ePonz Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized Candida antarctica lipase B |
topic_facet |
turnip mosaic virus Chemical conjugation Nanobiocatalysis nanonets Enzyme Nanoimmobilization Plant culture SB1-1110 |
description |
Elongated flexuous plant viral nanoparticles (VNPs) represent an interesting platform for developing different applications in nanobiotechnology. In the case of potyviruses, the virion external surface is made up of helically-arrayed domains of the viral structural coat protein (CP), repeated over 2000 times, in which the N- and C-terminal domains of each CP are projected towards the exterior of the external virion surface. These characteristics provide a chemical environment rich in functional groups susceptible to chemical conjugations. We have conjugated Candida antarctica lipase B (CALB) onto amino groups of the external surface of the potyvirus turnip mosaic virus (TuMV) using glutaraldehyde as a conjugating agent. Using this approach, TuMV virions were transformed into scaffolds for CALB nanoimmobilization. Analysis of the resulting structures revealed the formation of TuMV nanonets onto which large CALB aggregates were deposited. The functional enzymatic characterization of the CALB-bearing TuMV nanonets showed that CALB continued to be active in the nanoimmobilized form, even gaining an increased relative specific activity, as compared to the non-immobilized form. These novel virus-based nanostructures may provide a useful new approach to enzyme nanoimmobilization susceptible to be industrially exploited. |
format |
Article in Journal/Newspaper |
author |
Sol eCuenca Carmen eMansilla Marta eAguado Carmen eYuste-Calvo Flora eSánchez Jose María eSánchez-Montero Fernando ePonz |
author_facet |
Sol eCuenca Carmen eMansilla Marta eAguado Carmen eYuste-Calvo Flora eSánchez Jose María eSánchez-Montero Fernando ePonz |
author_sort |
Sol eCuenca |
title |
Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized Candida antarctica lipase B |
title_short |
Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized Candida antarctica lipase B |
title_full |
Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized Candida antarctica lipase B |
title_fullStr |
Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized Candida antarctica lipase B |
title_full_unstemmed |
Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized Candida antarctica lipase B |
title_sort |
nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized candida antarctica lipase b |
publisher |
Frontiers Media S.A. |
publishDate |
2016 |
url |
https://doi.org/10.3389/fpls.2016.00464 https://doaj.org/article/ca7ed944274c40b89b7ecc8d1a764495 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Frontiers in Plant Science, Vol 7 (2016) |
op_relation |
http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00464/full https://doaj.org/toc/1664-462X 1664-462X doi:10.3389/fpls.2016.00464 https://doaj.org/article/ca7ed944274c40b89b7ecc8d1a764495 |
op_doi |
https://doi.org/10.3389/fpls.2016.00464 |
container_title |
Frontiers in Plant Science |
container_volume |
7 |
_version_ |
1766259267363405824 |