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Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving
Superoxide dismutase (SOD) is a critical enzyme associated with controlling oxygen toxicity arising out of oxidative stress in any living system. A hyper-thermostable SOD isolated from a polyextremophile higher plant Potentilla atrosanguinea Lodd. var. argyrophylla (Wall. ex Lehm.) was engineered by...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3339387/ https://www.ncbi.nlm.nih.gov/pubmed/22548128 http://dx.doi.org/10.1038/srep00387 |
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author | Kumar, Arun Dutt, Som Bagler, Ganesh Ahuja, Paramvir Singh Kumar, Sanjay |
author_facet | Kumar, Arun Dutt, Som Bagler, Ganesh Ahuja, Paramvir Singh Kumar, Sanjay |
author_sort | Kumar, Arun |
collection | PubMed |
description | Superoxide dismutase (SOD) is a critical enzyme associated with controlling oxygen toxicity arising out of oxidative stress in any living system. A hyper-thermostable SOD isolated from a polyextremophile higher plant Potentilla atrosanguinea Lodd. var. argyrophylla (Wall. ex Lehm.) was engineered by mutation of a single amino acid that enhanced the thermostability of the enzyme to twofold. The engineered enzyme was functional from sub-zero temperature to >50°C, tolerated autoclaving (heating at 121°C, at a pressure of 1.1 kg per square cm for 20 min) and was resistant to proteolysis. The present work is the first example to enhance the thermostability of a hyper-thermostable protein and has potential to application to other proteins for enhancing thermostability. |
format | Online Article Text |
id | pubmed-3339387 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-33393872012-04-30 Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving Kumar, Arun Dutt, Som Bagler, Ganesh Ahuja, Paramvir Singh Kumar, Sanjay Sci Rep Article Superoxide dismutase (SOD) is a critical enzyme associated with controlling oxygen toxicity arising out of oxidative stress in any living system. A hyper-thermostable SOD isolated from a polyextremophile higher plant Potentilla atrosanguinea Lodd. var. argyrophylla (Wall. ex Lehm.) was engineered by mutation of a single amino acid that enhanced the thermostability of the enzyme to twofold. The engineered enzyme was functional from sub-zero temperature to >50°C, tolerated autoclaving (heating at 121°C, at a pressure of 1.1 kg per square cm for 20 min) and was resistant to proteolysis. The present work is the first example to enhance the thermostability of a hyper-thermostable protein and has potential to application to other proteins for enhancing thermostability. Nature Publishing Group 2012-04-30 /pmc/articles/PMC3339387/ /pubmed/22548128 http://dx.doi.org/10.1038/srep00387 Text en Copyright © 2012, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareALike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ |
spellingShingle | Article Kumar, Arun Dutt, Som Bagler, Ganesh Ahuja, Paramvir Singh Kumar, Sanjay Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving |
title | Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving |
title_full | Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving |
title_fullStr | Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving |
title_full_unstemmed | Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving |
title_short | Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving |
title_sort | engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°c, which also tolerates autoclaving |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3339387/ https://www.ncbi.nlm.nih.gov/pubmed/22548128 http://dx.doi.org/10.1038/srep00387 |
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