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—Reactive oxygen species (ROS) have been implicated in a number of disease processes. Oxidative stress is inhibited by enzymatic defense mechanisms, such as superoxide dismutase, catalase, and glutathione peroxidase. Extracellular superoxide dismutase (EC-SOD or SOD3) is an antioxidant enzyme secreted by cells to prevent overproduction of reactive oxygen species. It could potentially be used to prevent and cure cardiovascular disease, neurological disorders, and inflammation resulting from the accumulation of superoxide anions. In this study,we expressed theEC-SOD gene isolated from a human aortic smooth muscle cDNA library in food-grade Lactobacillus caseiCCRC10679. We used an 18-aa signal peptide from human SOD3 (hSOD3) to mediate extracellular secretion. After electroporation and 20 rounds of erythromycin antibiotic selections, two clones were isolated that expressed high levels of recombinant EC-SOD. The recombinant protein was purified from L.casei/hSOD3 using fast protein liquid chromatography (FPLC) with a heparin affinity column. The purified enzyme showed two bands at 38kDa (monomer) and 76-kDa(dimer) by SDS-PAGE and western blotting. The 76-kDa band was also detected by a nitrobluetetrazolium assay. Antioxidant activity of the purified EC-SOD was determined using a water-soluble tetrazolium (WST-1) assayto demonstrate that production of recombinant EC-SOD in the food-gradeL. casei actually possessed enzymatic activity.

Cloning and Expression of the Human Extracellular Superoxide Dismutase (EC-SOD) Gene in Probiotic Lactobacillus Casei