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Recombinant Expression of Archaeal Superoxide Dismutases in Plant Cell Cultures: A Sustainable Solution with Potential Application in the Food Industry
Superoxide dismutase (SOD) is a fundamental antioxidant enzyme that neutralises superoxide ions, one of the main reactive oxygen species (ROS). Extremophile organisms possess enzymes that offer high stability and catalytic performances under a wide range of conditions, thus representing an exception...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9495943/ https://www.ncbi.nlm.nih.gov/pubmed/36139805 http://dx.doi.org/10.3390/antiox11091731 |
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author | Gogliettino, Marta Arciello, Stefania Cillo, Fabrizio Carluccio, Anna Vittoria Palmieri, Gianna Apone, Fabio Ambrosio, Rosa Luisa Anastasio, Aniello Gratino, Lorena Carola, Antonietta Cocca, Ennio |
author_facet | Gogliettino, Marta Arciello, Stefania Cillo, Fabrizio Carluccio, Anna Vittoria Palmieri, Gianna Apone, Fabio Ambrosio, Rosa Luisa Anastasio, Aniello Gratino, Lorena Carola, Antonietta Cocca, Ennio |
author_sort | Gogliettino, Marta |
collection | PubMed |
description | Superoxide dismutase (SOD) is a fundamental antioxidant enzyme that neutralises superoxide ions, one of the main reactive oxygen species (ROS). Extremophile organisms possess enzymes that offer high stability and catalytic performances under a wide range of conditions, thus representing an exceptional source of biocatalysts useful for industrial processes. In this study, SODs from the thermo-halophilic Aeropyrum pernix (SOD(Ap)) and the thermo-acidophilic Saccharolobus solfataricus (SOD(Ss)) were heterologously expressed in transgenic tomato cell cultures. Cell extracts enriched with SOD(Ap) and SOD(Ss) showed a remarkable resistance to salt and low pHs, respectively, together with optimal activity at high temperatures. Moreover, the treatment of tuna fillets with SOD(Ap)-extracts induced an extension of the shelf-life of this product without resorting to the use of illicit substances. The results suggested that the recombinant plant extracts enriched with the extremozymes could find potential applications as dietary supplements in the nutrition sector or as additives in the food preservation area, representing a more natural and appealing alternative to chemical preservatives for the market. |
format | Online Article Text |
id | pubmed-9495943 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-94959432022-09-23 Recombinant Expression of Archaeal Superoxide Dismutases in Plant Cell Cultures: A Sustainable Solution with Potential Application in the Food Industry Gogliettino, Marta Arciello, Stefania Cillo, Fabrizio Carluccio, Anna Vittoria Palmieri, Gianna Apone, Fabio Ambrosio, Rosa Luisa Anastasio, Aniello Gratino, Lorena Carola, Antonietta Cocca, Ennio Antioxidants (Basel) Article Superoxide dismutase (SOD) is a fundamental antioxidant enzyme that neutralises superoxide ions, one of the main reactive oxygen species (ROS). Extremophile organisms possess enzymes that offer high stability and catalytic performances under a wide range of conditions, thus representing an exceptional source of biocatalysts useful for industrial processes. In this study, SODs from the thermo-halophilic Aeropyrum pernix (SOD(Ap)) and the thermo-acidophilic Saccharolobus solfataricus (SOD(Ss)) were heterologously expressed in transgenic tomato cell cultures. Cell extracts enriched with SOD(Ap) and SOD(Ss) showed a remarkable resistance to salt and low pHs, respectively, together with optimal activity at high temperatures. Moreover, the treatment of tuna fillets with SOD(Ap)-extracts induced an extension of the shelf-life of this product without resorting to the use of illicit substances. The results suggested that the recombinant plant extracts enriched with the extremozymes could find potential applications as dietary supplements in the nutrition sector or as additives in the food preservation area, representing a more natural and appealing alternative to chemical preservatives for the market. MDPI 2022-08-31 /pmc/articles/PMC9495943/ /pubmed/36139805 http://dx.doi.org/10.3390/antiox11091731 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Gogliettino, Marta Arciello, Stefania Cillo, Fabrizio Carluccio, Anna Vittoria Palmieri, Gianna Apone, Fabio Ambrosio, Rosa Luisa Anastasio, Aniello Gratino, Lorena Carola, Antonietta Cocca, Ennio Recombinant Expression of Archaeal Superoxide Dismutases in Plant Cell Cultures: A Sustainable Solution with Potential Application in the Food Industry |
title | Recombinant Expression of Archaeal Superoxide Dismutases in Plant Cell Cultures: A Sustainable Solution with Potential Application in the Food Industry |
title_full | Recombinant Expression of Archaeal Superoxide Dismutases in Plant Cell Cultures: A Sustainable Solution with Potential Application in the Food Industry |
title_fullStr | Recombinant Expression of Archaeal Superoxide Dismutases in Plant Cell Cultures: A Sustainable Solution with Potential Application in the Food Industry |
title_full_unstemmed | Recombinant Expression of Archaeal Superoxide Dismutases in Plant Cell Cultures: A Sustainable Solution with Potential Application in the Food Industry |
title_short | Recombinant Expression of Archaeal Superoxide Dismutases in Plant Cell Cultures: A Sustainable Solution with Potential Application in the Food Industry |
title_sort | recombinant expression of archaeal superoxide dismutases in plant cell cultures: a sustainable solution with potential application in the food industry |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9495943/ https://www.ncbi.nlm.nih.gov/pubmed/36139805 http://dx.doi.org/10.3390/antiox11091731 |
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