Heterologous expression of a novel psychrophilic cu/zn superoxide dismutase from deschampsia antarctica
Superoxide dismutase (SOD) catalyzes the conversion of the superoxide radical ((center dot)O(2)(-)) 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 an...
| Published in: | Process Biochemistry |
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| Main Authors: | , , , , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
ELSEVIER SCI LTD
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| Subjects: | |
| Online Access: | http://hdl.handle.net/10533/197736 https://doi.org/10.1016/j.procbio.2009.04.021 |
| Summary: | Superoxide dismutase (SOD) catalyzes the conversion of the superoxide radical ((center dot)O(2)(-)) 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 degrees C. However, zymogram test showed that the enzyme has more activity at 4 degrees C. This D. antarctica SOD could be used to reduce the oxidation of refrigerated and frozen foods. (C) 2009 Elsevier Ltd. All rights reserved. |
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