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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ftpubmed:oai:pubmedcentral.nih.gov:4826883 2023-05-15T13:38:07+02:00 Nanonets Derived from Turnip Mosaic Virus as Scaffolds for Increased Enzymatic Activity of Immobilized Candida antarctica Lipase B Cuenca, Sol Mansilla, Carmen Aguado, Marta Yuste-Calvo, Carmen Sánchez, Flora Sánchez-Montero, Jose M. Ponz, Fernando 2016-04-11 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4826883/ https://doi.org/10.3389/fpls.2016.00464 en eng Frontiers Media S.A. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4826883/ http://dx.doi.org/10.3389/fpls.2016.00464 Copyright © 2016 Cuenca, Mansilla, Aguado, Yuste-Calvo, Sánchez, Sánchez-Montero and Ponz. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. CC-BY Plant Science Text 2016 ftpubmed https://doi.org/10.3389/fpls.2016.00464 2016-05-08T00:18:09Z 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 toward 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. Text Antarc* Antarctica PubMed Central (PMC) Frontiers in Plant Science 7 |
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Plant Science Cuenca, Sol Mansilla, Carmen Aguado, Marta Yuste-Calvo, Carmen Sánchez, Flora Sánchez-Montero, Jose M. Ponz, Fernando Nanonets Derived from Turnip Mosaic Virus as Scaffolds for Increased Enzymatic Activity of Immobilized Candida antarctica Lipase B |
topic_facet |
Plant Science |
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 toward 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 |
Text |
author |
Cuenca, Sol Mansilla, Carmen Aguado, Marta Yuste-Calvo, Carmen Sánchez, Flora Sánchez-Montero, Jose M. Ponz, Fernando |
author_facet |
Cuenca, Sol Mansilla, Carmen Aguado, Marta Yuste-Calvo, Carmen Sánchez, Flora Sánchez-Montero, Jose M. Ponz, Fernando |
author_sort |
Cuenca, Sol |
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 |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4826883/ https://doi.org/10.3389/fpls.2016.00464 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4826883/ http://dx.doi.org/10.3389/fpls.2016.00464 |
op_rights |
Copyright © 2016 Cuenca, Mansilla, Aguado, Yuste-Calvo, Sánchez, Sánchez-Montero and Ponz. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.3389/fpls.2016.00464 |
container_title |
Frontiers in Plant Science |
container_volume |
7 |
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1766101630948737024 |