Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica

• Published in: Process biochemistry (1991) Vol. 44; no. 9; pp. 969 - 974
• Main Authors: García Echauri, Sergio A., Gidekel, Manuel, Moraga, Ana Gutiérrez, Ordóñez, Leandro G., Rojas Contreras, Juan A., Barba de la Rosa, Ana P., De León Rodríguez, Antonio
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01-09-2009
• Subjects: Antioxidant; Deschampsia antarctica; Escherichia coli; Extremophil; Oxidative stress; Photo-oxidation; Plant; Psychrophilic enzyme; Oxidative stress; Plant; Photo-oxidation; Psychrophilic enzyme; Antioxidant; Extremophil
• ISSN: 1359-5113; 1873-3298
• DOI: 10.1016/j.procbio.2009.04.021

Superoxide dismutase (SOD) catalyzes the conversion of the superoxide radical (
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
°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.