Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica
"Superoxide dismutase (SOD) catalyzes the conversion of the superoxide radical (O2−) into oxygen and hydrogen peroxide. Deschampsia antarctica is a plant that grows in Antarctica and survives to extreme low temperature and high UV radiation, thus it is an ideal model to study novel antioxidants...
Published in: | Process Biochemistry |
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Online Access: | http://hdl.handle.net/11627/3874 https://doi.org/10.1016/j.procbio.2009.04.021 |
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ftipicytsanjose:oai:repositorio.ipicyt.edu.mx:11627/3874 2023-05-15T13:54:02+02:00 Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica García Echauri, Sergio Ángel Ordoñez Acevedo, Leandro Gabriel Rojas Contreras, Juan Antonio Barba de la Rosa, Ana Paulina De León Rodríguez, Antonio 2009-09 application/pdf http://hdl.handle.net/11627/3874 https://doi.org/10.1016/j.procbio.2009.04.021 unknown Elsevier Sergio A. García Echauri, Manuel Gidekel, Ana Gutiérrez Moraga, Leandro G. Ordóñez, Juan A. Rojas Contreras, Ana P. Barba de la Rosa, Antonio De León Rodríguez, Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica, Process Biochemistry, Volume 44, Issue 9, 2009, Pages 969-974. http://hdl.handle.net/11627/3874 https://doi.org/10.1016/j.procbio.2009.04.021 Attribution-NonCommercial-NoDerivatives 4.0 Internacional http://creativecommons.org/licenses/by-nc-nd/4.0/ Acceso Abierto CC-BY-NC-ND Antioxidant Plant Extremophil Psychrophilic enzyme Photo-oxidation Oxidative stress CIENCIAS AGROPECUARIAS Y BIOTECNOLOGÍA article 2009 ftipicytsanjose https://doi.org/10.1016/j.procbio.2009.04.021 2020-05-03T16:25:54Z "Superoxide dismutase (SOD) catalyzes the conversion of the superoxide radical (O2−) into oxygen and hydrogen peroxide. Deschampsia antarctica is a plant that grows in Antarctica and survives to extreme low temperature and high UV radiation, thus it is an ideal model to study novel antioxidants. A cDNA Cu/Zn-SOD gene from D. antarctica was cloned into a pET vector and expressed in Escherichia coli BL21-SI. 112 mg/L of recombinant Cu/Zn-SOD was attained in batch cultures in bioreactor. Using Ni-affinity gel chromatography, the recombinant Cu/Zn-SOD was recovered with a purity of 90% and a specific enzyme activity of 749 at 25 °C. However, zymogram test showed that the enzyme has more activity at 4 °C. This D. antarctica SOD could be used to reduce the oxidation of refrigerated and frozen foods." Article in Journal/Newspaper Antarc* Antarctica Repository IPICYT (Instituto Potosino de Investigación Científica y Tecnológica) Process Biochemistry 44 9 969 974 |
institution |
Open Polar |
collection |
Repository IPICYT (Instituto Potosino de Investigación Científica y Tecnológica) |
op_collection_id |
ftipicytsanjose |
language |
unknown |
topic |
Antioxidant Plant Extremophil Psychrophilic enzyme Photo-oxidation Oxidative stress CIENCIAS AGROPECUARIAS Y BIOTECNOLOGÍA |
spellingShingle |
Antioxidant Plant Extremophil Psychrophilic enzyme Photo-oxidation Oxidative stress CIENCIAS AGROPECUARIAS Y BIOTECNOLOGÍA García Echauri, Sergio Ángel Ordoñez Acevedo, Leandro Gabriel Rojas Contreras, Juan Antonio Barba de la Rosa, Ana Paulina De León Rodríguez, Antonio Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica |
topic_facet |
Antioxidant Plant Extremophil Psychrophilic enzyme Photo-oxidation Oxidative stress CIENCIAS AGROPECUARIAS Y BIOTECNOLOGÍA |
description |
"Superoxide dismutase (SOD) catalyzes the conversion of the superoxide radical (O2−) into oxygen and hydrogen peroxide. Deschampsia antarctica is a plant that grows in Antarctica and survives to extreme low temperature and high UV radiation, thus it is an ideal model to study novel antioxidants. A cDNA Cu/Zn-SOD gene from D. antarctica was cloned into a pET vector and expressed in Escherichia coli BL21-SI. 112 mg/L of recombinant Cu/Zn-SOD was attained in batch cultures in bioreactor. Using Ni-affinity gel chromatography, the recombinant Cu/Zn-SOD was recovered with a purity of 90% and a specific enzyme activity of 749 at 25 °C. However, zymogram test showed that the enzyme has more activity at 4 °C. This D. antarctica SOD could be used to reduce the oxidation of refrigerated and frozen foods." |
format |
Article in Journal/Newspaper |
author |
García Echauri, Sergio Ángel Ordoñez Acevedo, Leandro Gabriel Rojas Contreras, Juan Antonio Barba de la Rosa, Ana Paulina De León Rodríguez, Antonio |
author_facet |
García Echauri, Sergio Ángel Ordoñez Acevedo, Leandro Gabriel Rojas Contreras, Juan Antonio Barba de la Rosa, Ana Paulina De León Rodríguez, Antonio |
author_sort |
García Echauri, Sergio Ángel |
title |
Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica |
title_short |
Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica |
title_full |
Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica |
title_fullStr |
Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica |
title_full_unstemmed |
Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica |
title_sort |
heterologous expression of a novel psychrophilic cu/zn superoxide dismutase from deschampsia antarctica |
publisher |
Elsevier |
publishDate |
2009 |
url |
http://hdl.handle.net/11627/3874 https://doi.org/10.1016/j.procbio.2009.04.021 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
Sergio A. García Echauri, Manuel Gidekel, Ana Gutiérrez Moraga, Leandro G. Ordóñez, Juan A. Rojas Contreras, Ana P. Barba de la Rosa, Antonio De León Rodríguez, Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica, Process Biochemistry, Volume 44, Issue 9, 2009, Pages 969-974. http://hdl.handle.net/11627/3874 https://doi.org/10.1016/j.procbio.2009.04.021 |
op_rights |
Attribution-NonCommercial-NoDerivatives 4.0 Internacional http://creativecommons.org/licenses/by-nc-nd/4.0/ Acceso Abierto |
op_rightsnorm |
CC-BY-NC-ND |
op_doi |
https://doi.org/10.1016/j.procbio.2009.04.021 |
container_title |
Process Biochemistry |
container_volume |
44 |
container_issue |
9 |
container_start_page |
969 |
op_container_end_page |
974 |
_version_ |
1766259552097927168 |