Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation

We present a high-yield method for the renaturation of negatively charged enzymes. The approach is based on the use of alumina nanoparticles, which after electrostatic interaction with denatured protein molecules, prevent their aggregation and make the process of refolding controllable. The method,...

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Detalles Bibliográficos
Autores principales: Volodina, Katerina V., Avnir, David, Vinogradov, Vladimir V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431136/
https://www.ncbi.nlm.nih.gov/pubmed/28469182
http://dx.doi.org/10.1038/s41598-017-01436-6
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author Volodina, Katerina V.
Avnir, David
Vinogradov, Vladimir V.
author_facet Volodina, Katerina V.
Avnir, David
Vinogradov, Vladimir V.
author_sort Volodina, Katerina V.
collection PubMed
description We present a high-yield method for the renaturation of negatively charged enzymes. The approach is based on the use of alumina nanoparticles, which after electrostatic interaction with denatured protein molecules, prevent their aggregation and make the process of refolding controllable. The method, demonstrated by the renaturation of several enzymes, is efficient, rapid, employs a minimal amount of reagents and even can be applied to renature mixture of the denatured enzymes.
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spelling pubmed-54311362017-05-16 Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation Volodina, Katerina V. Avnir, David Vinogradov, Vladimir V. Sci Rep Article We present a high-yield method for the renaturation of negatively charged enzymes. The approach is based on the use of alumina nanoparticles, which after electrostatic interaction with denatured protein molecules, prevent their aggregation and make the process of refolding controllable. The method, demonstrated by the renaturation of several enzymes, is efficient, rapid, employs a minimal amount of reagents and even can be applied to renature mixture of the denatured enzymes. Nature Publishing Group UK 2017-05-03 /pmc/articles/PMC5431136/ /pubmed/28469182 http://dx.doi.org/10.1038/s41598-017-01436-6 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Volodina, Katerina V.
Avnir, David
Vinogradov, Vladimir V.
Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation
title Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation
title_full Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation
title_fullStr Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation
title_full_unstemmed Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation
title_short Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation
title_sort alumina nanoparticle-assisted enzyme refolding: a versatile methodology for proteins renaturation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431136/
https://www.ncbi.nlm.nih.gov/pubmed/28469182
http://dx.doi.org/10.1038/s41598-017-01436-6
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