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

Echauri, SAG; Gidekel, M.; Moraga, AG; Ordonez, LG; Contreras, JAR; de la Rosa, APB; Rodriguez, AD

Abstract

Superoxide dismutase (SOD) catalyzes the conversion of the superoxide radical ({radical dot}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. © 2009 Elsevier Ltd. All rights reserved.

Más información

Título según WOS: Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica
Título según SCOPUS: Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica
Título de la Revista: PROCESS BIOCHEMISTRY
Volumen: 44
Número: 9
Editorial: ELSEVIER SCI LTD
Fecha de publicación: 2009
Página de inicio: 969
Página final: 974
Idioma: English
URL: http://linkinghub.elsevier.com/retrieve/pii/S1359511309001445
DOI:

10.1016/j.procbio.2009.04.021

Notas: ISI, SCOPUS