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Indexed/Abstracted in: EMBASE, Science Citation Index Expanded (SciSearch), Scopus
Impact Factor 0,246
Online ISSN 1827-160X
Zeinab KARIMI 1, 2, Mohammad A. MOBASHER 2, 3, 4, Soraya KHOUBANI 1, 2, Zahra PAKROUH 1, 2, Mohammad B. GHOSHOON 1, 2, Nima MONTAZERI-NAJAFABADY 1, 2, Younes GHASEMI 1, 2
1 Department of Pharmaceutical Biotechnology, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran; 2 Department of Pharmaceutical Sciences Research Center, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran; 3 Non communicable Diseases Research Center, Fasa University of Medical Sciences, Fasa, Iran; 4 Department of Medical Biotechnology, School of Medicine, Fasa University of Medical Sciences, Fasa, Iran
BACKGROUND: Superoxide dismutase enzymes (SODs) with various natural sources are metalloproteins characterized by catalyzing the dismutation of superoxide radicals to oxygen and hydrogen peroxide. These radical scavengers are responsible to therapeutic effects in treatment of oxidative stress related diseases, and have potent antioxidant properties in cosmetic and food industry against oxidative damages. Recently, biotechnology has focused on producing safer and less expensive enzymes with improvement in potency and specificity. With this concern, we aimed at producing a recombinant SOD (r-SOD) originated from Pseudomonas aeruginosa, strictly aerobic bacterium with high level of SOD activity.
METHODS: Amplified sodA was inserted into pET15b, and confirmed by molecular methods. Recombinant Mn-SOD was produced in E.coli BL21 (DE3) by using IPTG induction process. Ni-NTA spin facilitated purification of produced recombinant protein.
RESULTS: Protein BLAST with protein databases showed 92-100% identity with Mn-SOD amino acid sequences of Pseudomonas aeruginosa strains while 74-81% identity with other species. The highest nucleotide sequence identity observed with Pseudomonas aeruginosa UCBPP-PA14 (Accession NO. CP000438.1) and the lowest sequence identity observed with Rhodospirillum centenum SW (accession NO CP000613.2).
CONCLUSIONS: It seems P. aeruginosa SOD enzyme with high ability in quenching the reactive oxygen radicals in intense oxidative stress has a potent capacity for genetic engineering manipulation in the purposes of food and therapeutic applications.