Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica |
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Authors: | Sergio A. Garcí a Echauri, Manuel Gidekel, Ana Guti rrez Moraga, Leandro G. Ord ez, Juan A. Rojas Contreras, Ana P. Barba de la Rosa,Antonio De Le n Rodrí guez |
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Affiliation: | 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, |
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Abstract: | 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. |
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Keywords: | Antioxidant Plant Extremophil Psychrophilic enzyme Photo-oxidation Oxidative stress |
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