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

• Published in: Process Biochemistry
• Main Authors: SERGIO ANGEL GARCIA ECHAURI, LEANDRO GABRIEL ORDONEZ ACEVEDO, JUAN ANTONIO ROJAS CONTRERAS, ANA PAULINA BARBA DE LA ROSA, ANTONIO DE LEON RODRIGUEZ
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: Elsevier Science LTD 2009
• Subjects: info:eu-repo/classification/Autor/Antioxidant; info:eu-repo/classification/Autor/Plant; info:eu-repo/classification/Autor/Extremophil; info:eu-repo/classification/Autor/Psychrophilic enzyme; info:eu-repo/classification/Autor/Photo-oxidation; info:eu-repo/classification/Autor/Oxidative stress; info:eu-repo/classification/cti/6; Antarc*; Antarctica
• Online Access: http://ipicyt.repositorioinstitucional.mx/jspui/handle/1010/1474

"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."