Characterization and Cytotoxic Activity Evaluation of Superoxide Dismutase (SOD) Enzyme Purified From Escherichia coli.
Abstract
Background: Superoxide dismutases (SODs) are antioxidant metalloenzymes produced by all living cells, including E. coli. SODs enzymes have several roles in treatment of different diseases, including tumors. Its catalysing the dismutation of superoxide free radicals (O2•–) to H2O2 and H2O to protect cells against their harmful effects. This might prevent damage to tissues. Objective: Production and purification of antitumor enzyme (superoxide dismutase) from local isolate Escherichia coli. Methods: SOD was partially purified from E. coli using ammonium sulphate precipitation, DEAE-cellulose ion exchange and sephadex G-150 Gel filtration chromatography. Subsequently, the molecular weight of the purified SOD was determined using SDS-PAGE. Moreover, the activity and stability of SOD were examined under different pH and temperature values. Finally, cytotoxic potential assessed against colon cancer and normal cell lines. Results: Crude extract of SOD was partially purified using ammonium sulphate precipitation, DEAE-cellulose ion and sephadex G-150 Gel filtration chromatography, whereas specific activity of SOD was increased from 314.2 into 1357 U/mg protein with 3.5-fold and yield (52.5%). The activity and stability of SOD were examined under different pH and temperature values. The maximum SOD activity was 95 U/ml at pH 6, while the stability of enzyme (90 – 100%) at pH range (6-8). The maximum activity at 37oC. At 32-37oC, SOD enzyme was stable with remaining activity of 100%. Various agents (NaCl, CaCl2, H2O2, MnSO4 and urea) were used to estimate their effects on enzyme stability. The enzyme was maintaining its activity (100%) in presence of NaCl, CaCl2 and H2O2, while completely lose its activity in presence of urea (0.1M), and this activity was increased into 140% in presence of MnSO4 (0.1 M). Cytotoxicity of purified SOD was exanimated on primary dermal fibroblast normal (Hdfn) and a human colorectal adenocarcinoma cell-line (Caco-2) cell lines. The viability of (Caco-2) was decreased into 45% after treatment with SOD enzyme at 400 µg/ml after 24 hrs. On the other hand, the viability of HdFn was decreased into 75% after treatment with SOD enzyme at concentration of 400 µg/ml after 24 hrs. Conclusion: Lower IC₅₀ values indicate a stronger inhibition of cell viability at higher doses of SOD. Which suggesting its potential therapeutic for future applications.
Keywords:
Characterization, Cytotoxicity, E. Coli, Purification, Superoxide Dismutase
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References
Abdalah, M. E., Al-Saady, A. J., ALBahrani, M. H., Al-Obaidi, M. J., & Abd Al-Hussein, M. Y. (2018). Cleavage of mucin and salivary agglutinin by partial purified protease from a native strain of Streptococcus mutans AN67. Journal of Global Pharma Technology, 10(06), 404-410. https://jgpt.co.in/index.php/jgpt/article/view/1241
Abdel-Monsef, M. M., Darwish, D. A., Zidan, H. A., Hamed, A. A., & Ibrahim, M. A. (2023). Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii). Journal of Genetic Engineering and Biotechnology, 21(1), 21. https://doi.org/10.1186/s43141-023-00470-4
Acharya, V. V., & Chaudhuri, P. (2021). Modalities of protein denaturation and nature of denaturants. International Journal of Pharmaceutical Sciences Review and Research, 69(2), 19-24. http://dx.doi.org/10.47583/ijpsrr.2021.v69i02.002
Alateyah, N., Gupta, I., Rusyniak, R. S., &Ouhtit, A. (2022). SOD2, a potential transcriptional target underpinning CD44-promoted breast cancer progression. Molecules, 27(3), 811.https://doi.org/10.3390/molecules27030811
AL-Sa'ady, A. J. R., & Hilal, M. H. (2020). Determination of the optimum conditions for extracting polyphenol ox-idase and laccase enzymes from malva parviflora and their role in the decolorization of some dyes. Iraqi Journal of Science, 306-313. http://dx.doi.org/10.24996/ijs.2020.61.2.7
Amaal A. H., Sahar I. H, & Mohanad J. M-Ridha. (2023). Determination of the optimum conditions for urease extracted from some local plants. Iraqi Journal of Agricultural Sciences, 54(3), 647-656. https://doi.org/10.36103/ijas.v54i3.1776
Barwinska-Sendra, A., Garcia, Y. M., Sendra, K. M., Baslé, A., Mackenzie, E. S., Tarrant, E., ... & Waldron, K. J. (2020). An evolutionary path to altered cofactor specificity in a metalloenzyme. Nature Communications, 11(10), 2738. https://doi.org/10.1038/s41467-020-16478-0
Beyer Jr, W. F., &Fridovich, I. (1987). Assaying for superoxide dismutase activity: Some large consequences of minor changes in conditions. Analytical Biochemistry, 161(2), 559-566. https://doi.org/10.1016/0003-2697(87)90489-1
Bishayee, A., & Sethi, G. (2016). Bioactive natural products in cancer prevention and therapy: Progress and promise. In Seminars in Cancer Biology (Vol. 40, pp. 1-3). Academic Press. https://doi.org/10.1016/j.semcancer.2016.08.006
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72(1-2), 248-254. https://doi.org/10.1016/0003-2697(76)90527-3
Chimbekujwo, K. I., Ja'afaru, M. I., & Adeyemo, O. M. (2020). Purification, characterization and optimization conditions of protease produced by Aspergillus brasiliensis strain BCW2. Scientific African, 8, e00398.https://doi.org/10.1016/j.sciaf.2020.e00398
Dong, X., Wang, W., Li, S., Han, H., Lv, P., & Yang, C. (2021). Thermoacidophilic Alicyclobacillus superoxide dismutase: good candidate as additives in food and medicine. Frontiers in Microbiology, 12, 577001.https://doi.org/10.3389/fmicb.2021.577001
Doukyu, N., & Taguchi, K. (2021). Involvement of catalase and superoxide dismutase in hydrophobic organic solvent tolerance of Escherichia coli. AMB Express, 11(1), 97.https://doi.org/10.1186/s13568-021-01258-w
El-Mahdy, M. A., Alzarie, Y. A., Hemann, C., Badary, O. A., Nofal, S., & Zweier, J. L. (2020). The novel SOD mimetic GC4419 increases cancer cell killing with sensitization to ionizing radiation while protecting normal cells. Free Radical Biology and Medicine, 160, 630-642. https://doi.org/10.1016/j.freeradbiomed.2020.07.032
Evacuasiany, E., Ratnawati, H., Liana, L. K., Widowati, W., Maesaroh, M., Mozef, T., &Risdian, C. (2014). Cytotoxic and antioxidant activities of catechins in inhibiting the malignancy of breast cancer. Oxid Antioxid Med Sci, 3(2), 141-146. https://doi.org/10.5455/oams.240614.or.066
Fulghum, R. S., & Worthington, J. M. (1984). Superoxide dismutase in ruminal bacteria. Applied and Environmental Microbiology, 48(3), 675-677.https://doi.org/10.1128/aem.48.3.675-677.1984
Garfin, D. E. (1990). [33] One-dimensional gel electrophoresis. In Methods in Enzymology (Vol. 182, pp. 425-441). Academic Press. https://doi.org/10.1016/0076-6879(90)82035-Z
Gou, W., Zheng, P., Tian, L., Gao, M., Zhang, L., Akram, N. A., & Ashraf, M. (2017). Exogenous application of urea and a urease inhibitor improves drought stress tolerance in maize (Zea mays L.). Journal of Plant Research, 130, 599-609. https://doi.org/10.1007/s10265-017-0933-5
Guan, T., Song, J., Wang, Y., Guo, L., Yuan, L., Zhao, Y., ... & Wei, J. (2017). Expression and characterization of recombinant bifunctional enzymes with glutathione peroxidase and superoxide dismutase activities. Free Radical Biology and Medicine, 110, 188-195. https://doi.org/10.1016/j.freeradbiomed.2017.06.005
Habib, M. R., Masoud, H. M., Helmy, M. S., Hamed, A. A., Gad El-Karim, R. M., Ali, R. E., ... & Ibrahim, M. A. (2023). In vitro anticancer and antimicrobial activities of copper-zinc superoxide dismutase purified from Cellana rota snail. Egyptian Journal of Chemistry, 66(12), 1-10. https://doi.org/10.21608/ejchem.2023.200467.7736
He, Y., Li, J., Chen, J., Miao, X., Li, G., He, Q., ... & Wei, Y. (2020). Cytotoxic effects of polystyrene nanoplastics with different surface functionalization on human HepG2 cells. Science of the Total Environment, 723, 138180.https://doi.org/10.1016/j.scitotenv.2020.138180
Holdom, M. D., Lechenne, B., Hay, R. J., Hamilton, A. J., & Monod, M. (2000). Production and characterization of recombinant Aspergillus fumigatus Cu, Zn superoxide dismutase and its recognition by immune human sera. Journal of Clinical Microbiology, 38(2), 558-562. https://doi.org/10.1128/jcm.38.2.558-562.2000
Ibrahim, M. A., Mohamed, M. M., Ghazy, A. H. M., & Masoud, H. M. (2013). Superoxide dismutases from larvae of the camel tick Hyalommadromedarii. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 164(3), 221-228. https://doi.org/10.1016/j.cbpb.2013.01.002
Islam, M. N., Rauf, A., Fahad, F. I., Emran, T. B., Mitra, S., Olatunde, A., ... & Mubarak, M. S. (2022). Superoxide dismutase: an updated review on its health benefits and industrial applications. Critical Reviews in Food Science and Nutrition, 62(26), 7282-7300. https://doi.org/10.1080/10408398.2021.1913400
Krezel, A., & Maret, W. (2021). The bioinorganic chemistry of mammalian metallothioneins. Chemical reviews, 121(23), 14594-14648. https://doi.org/10.1021/acs.chemrev.1c00371?urlappend=%3Fref%3DPDF&jav=VoR&rel=cite-as
Kumar, A., Sharma, M., Bhardwaj, P. K., Vats, S. K., Singh, D., & Kumar, S. (2016). Copper, zinc superoxide dismutase from Caragana jubata: A thermostable enzyme that functions under a broad pH and temperature window. Process Biochemistry, 51(10), 1434-1444. https://doi.org/10.1016/j.procbio.2016.06.025
Law, J. W. F., Ser, H. L., Duangjai, A., Saokaew, S., Bukhari, S. I., Khan, T. M., ... & Lee, L. H. (2017). Streptomyces colonosanans sp. nov., a novel actinobacterium isolated from Malaysia mangrove soil exhibiting antioxidative activity and cytotoxic potential against human colon cancer cell lines. Frontiers in Microbiology, 8, 877.https://doi.org/10.3389/fmicb.2017.00877
Lefebre, M. D., & Valvano, M. A. (2001). In vitro resistance of Burkholderiacepacia complex isolates to reactive oxygen species in relation to catalase and superoxide dismutase production. Microbiology, 147(1), 97-109. https://doi.org/10.1099/00221287-147-1-97
Longoni, S. S., Marín, C., & Sánchez-Moreno, M. (2014). Excreted Leishmania peruviana and Leishmania amazonensis iron–superoxide dismutase purification: Specific antibody detection in Colombian patients with cutaneous leishmaniasis. Free Radical Biology and Medicine, 69, 26-34. https://doi.org/10.1016/j.freeradbiomed.2014.01.012
Matsumoto, H., Haniu, H., & Komori, N. (2019). Determination of protein molecular weights on SDS-PAGE. Electrophoretic Separation of Proteins: Methods and Protocols, 101-105. https://doi.org/10.1007/978-1-4939-8793-1_10
Ozdemir, C., Gulesci, N., & Bilgin, R. (2021). Purification and Characterization of Superoxide Dismutase Enzyme from Punica granatum L. Asian Journal of Research in Biochemistry, 9(3), 30-35. https://doi.org/10.9734/ajrb/2021/v9i330203
Park, A., Joo, M., Kim, K., Son, W. J., Lim, G., Lee, J., ... & Nam, S. (2022). A comprehensive evaluation of regression-based drug responsiveness prediction models, using cell viability inhibitory concentrations (IC50 values). Bioinformatics, 38(10), 2810-2817. https://doi.org/10.1093/bioinformatics/btac177
Pokharel, P., Ma, Z., & Chang, S. X. (2020). Biochar increases soil microbial biomass with changes in extra-and intracellular enzyme activities: A global meta-analysis. Biochar, 2, 65-79. https://doi.org/10.1007/s42773-020-00039-1
Rady, M. M., El-Shewy, A. A., Seif El-Yazal, M. A., & Abd El-Gawwad, A. F. M. (2022). Integrative application of soil P-solubilizing bacteria and foliar nano-P improves antioxidant, hormonal, and nutrient contents and phosphatase activity in Phaseolus vulgaris plants grown under calcareous soil conditions. Journal of Agricultural Research Pesticides and Biofertilizers, 3(2). https://doi.org/10.1007/s42729-019-00168-Y
Rosa, A. C., Corsi, D., Cavi, N., Bruni, N., & Dosio, F. (2021). Superoxide dismutase administration: A review of proposed human uses. Molecules, 26(7), 1844.https://doi.org/10.3390/molecules26071844
Saqib, U., Kelley, T. T., Panguluri, S. K., Liu, D., Savai, R., Baig, M. S., &Schürer, S. C. (2018). Polypharmacology or promiscuity? Structural interactions of resveratrol with its bandwagon of targets. Frontiers in Pharmacology, 9, 1201.https://doi.org/10.3389/fphar.2018.01201
Stephenie, S., Chang, Y. P., Gnanasekaran, A., Esa, N. M., &Gnanaraj, C. (2020). An insight on superoxide dismutase (SOD) from plants for mammalian health enhancement. Journal of Functional Foods, 68, 103917.https://doi.org/10.1016/j.jff.2020.103917
Tuteja, N., Mishra, P., Yadav, S., Tajrishi, M., Baral, S., & Sabat, S. C. (2015). Heterologous expression and biochemical characterization of a highly active and stable chloroplasticCuZn-superoxide dismutase from Pisum sativum. BMC biotechnology, 15, 1-14. https://doi.org/10.1186/s12896-015-0117-0
Valderas, M. W., & Hart, M. E. (2001). Identification and characterization of a second superoxide dismutase gene (sodM) from Staphylococcus aureus. Journal of Bacteriology, 183(11), 3399-3407. https://doi.org/10.1128/JB.183.11.3399-3407.2001
Wang, B. R., Zhi, W. X., Han, S. Y., Zhao, H. F., Liu, Y. X., Xu, S. Y., ... & Mu, Z. S. (2024). Adaptability to the environment of protease by secondary structure changes and application to enzyme-selective hydrolysis. International Journal of Biological Macromolecules, 278(Pt 3), 134969.https://doi.org/10.1016/j.ijbiomac.2024.134969
Wang, J., Luo, B., Li, X., Lu, W., Yang, J., Hu, Y., ... & Wen, S. (2017). Inhibition of cancer growth in vitro and in vivo by a novel ROS-modulating agent with ability to eliminate stem-like cancer cells. Cell Death & Disease, 8(6), e2887-e2887. https://doi.org/10.1038/cddis.2017.272
Wang, M., Wang, L., Yi, Q., Gai, Y., & Song, L. (2015). Molecular cloning and characterization of a cytoplasmic manganese superoxide dismutase and a mitochondrial manganese superoxide dismutase from Chinese mitten crab Eriocheir sinensis. Fish & Shellfish Immunology, 47(1), 407-417. https://doi.org/10.1016/j.fsi.2015.09.035
Wang, Q. F., Wang, Y. F., Hou, Y. H., Shi, Y. L., Han, H., Miao, M., ... & Li, Y. J. (2016). Cloning, expression and biochemical characterization of recombinant superoxide dismutase from Antarctic psychrophilic bacterium Pseudoalteromonas sp. ANT506. Journal of Basic Microbiology, 56(7), 753-761. https://doi.org/10.1002/jobm.201500444
Whitaker, J. R., & Bernhard, R. A. (1972). Experiments for: An introduction to enzymology.
World Health Organization. (2018). Global Health Estimates 2016: Deaths by cause, age, sex, by country and by region, 2000–2016. Geneva: World Health Organization. Available at: https://www.who.int/data/gho/data/themes/mortality-and-global-health-estimates
Zeinali, F., Homaei, A., & Kamrani, E. (2017). Identification and kinetic characterization of a novel superoxide dismutase from Avicennia marina: An antioxidant enzyme with unique features. International Journal of Biological Macromolecules, 105(Pt 3), 1556-1562. https://doi.org/10.1016/j.ijbiomac.2017.07.054
Zheng, M., Liu, Y., Zhang, G., Yang, Z., Xu, W., & Chen, Q. (2023). The applications and mechanisms of superoxide dismutase in medicine, food, and cosmetics. Antioxidants, 12(9), 1675.https://doi.org/10.3390/antiox12091675
Abdel-Monsef, M. M., Darwish, D. A., Zidan, H. A., Hamed, A. A., & Ibrahim, M. A. (2023). Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii). Journal of Genetic Engineering and Biotechnology, 21(1), 21. https://doi.org/10.1186/s43141-023-00470-4
Acharya, V. V., & Chaudhuri, P. (2021). Modalities of protein denaturation and nature of denaturants. International Journal of Pharmaceutical Sciences Review and Research, 69(2), 19-24. http://dx.doi.org/10.47583/ijpsrr.2021.v69i02.002
Alateyah, N., Gupta, I., Rusyniak, R. S., &Ouhtit, A. (2022). SOD2, a potential transcriptional target underpinning CD44-promoted breast cancer progression. Molecules, 27(3), 811.https://doi.org/10.3390/molecules27030811
AL-Sa'ady, A. J. R., & Hilal, M. H. (2020). Determination of the optimum conditions for extracting polyphenol ox-idase and laccase enzymes from malva parviflora and their role in the decolorization of some dyes. Iraqi Journal of Science, 306-313. http://dx.doi.org/10.24996/ijs.2020.61.2.7
Amaal A. H., Sahar I. H, & Mohanad J. M-Ridha. (2023). Determination of the optimum conditions for urease extracted from some local plants. Iraqi Journal of Agricultural Sciences, 54(3), 647-656. https://doi.org/10.36103/ijas.v54i3.1776
Barwinska-Sendra, A., Garcia, Y. M., Sendra, K. M., Baslé, A., Mackenzie, E. S., Tarrant, E., ... & Waldron, K. J. (2020). An evolutionary path to altered cofactor specificity in a metalloenzyme. Nature Communications, 11(10), 2738. https://doi.org/10.1038/s41467-020-16478-0
Beyer Jr, W. F., &Fridovich, I. (1987). Assaying for superoxide dismutase activity: Some large consequences of minor changes in conditions. Analytical Biochemistry, 161(2), 559-566. https://doi.org/10.1016/0003-2697(87)90489-1
Bishayee, A., & Sethi, G. (2016). Bioactive natural products in cancer prevention and therapy: Progress and promise. In Seminars in Cancer Biology (Vol. 40, pp. 1-3). Academic Press. https://doi.org/10.1016/j.semcancer.2016.08.006
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72(1-2), 248-254. https://doi.org/10.1016/0003-2697(76)90527-3
Chimbekujwo, K. I., Ja'afaru, M. I., & Adeyemo, O. M. (2020). Purification, characterization and optimization conditions of protease produced by Aspergillus brasiliensis strain BCW2. Scientific African, 8, e00398.https://doi.org/10.1016/j.sciaf.2020.e00398
Dong, X., Wang, W., Li, S., Han, H., Lv, P., & Yang, C. (2021). Thermoacidophilic Alicyclobacillus superoxide dismutase: good candidate as additives in food and medicine. Frontiers in Microbiology, 12, 577001.https://doi.org/10.3389/fmicb.2021.577001
Doukyu, N., & Taguchi, K. (2021). Involvement of catalase and superoxide dismutase in hydrophobic organic solvent tolerance of Escherichia coli. AMB Express, 11(1), 97.https://doi.org/10.1186/s13568-021-01258-w
El-Mahdy, M. A., Alzarie, Y. A., Hemann, C., Badary, O. A., Nofal, S., & Zweier, J. L. (2020). The novel SOD mimetic GC4419 increases cancer cell killing with sensitization to ionizing radiation while protecting normal cells. Free Radical Biology and Medicine, 160, 630-642. https://doi.org/10.1016/j.freeradbiomed.2020.07.032
Evacuasiany, E., Ratnawati, H., Liana, L. K., Widowati, W., Maesaroh, M., Mozef, T., &Risdian, C. (2014). Cytotoxic and antioxidant activities of catechins in inhibiting the malignancy of breast cancer. Oxid Antioxid Med Sci, 3(2), 141-146. https://doi.org/10.5455/oams.240614.or.066
Fulghum, R. S., & Worthington, J. M. (1984). Superoxide dismutase in ruminal bacteria. Applied and Environmental Microbiology, 48(3), 675-677.https://doi.org/10.1128/aem.48.3.675-677.1984
Garfin, D. E. (1990). [33] One-dimensional gel electrophoresis. In Methods in Enzymology (Vol. 182, pp. 425-441). Academic Press. https://doi.org/10.1016/0076-6879(90)82035-Z
Gou, W., Zheng, P., Tian, L., Gao, M., Zhang, L., Akram, N. A., & Ashraf, M. (2017). Exogenous application of urea and a urease inhibitor improves drought stress tolerance in maize (Zea mays L.). Journal of Plant Research, 130, 599-609. https://doi.org/10.1007/s10265-017-0933-5
Guan, T., Song, J., Wang, Y., Guo, L., Yuan, L., Zhao, Y., ... & Wei, J. (2017). Expression and characterization of recombinant bifunctional enzymes with glutathione peroxidase and superoxide dismutase activities. Free Radical Biology and Medicine, 110, 188-195. https://doi.org/10.1016/j.freeradbiomed.2017.06.005
Habib, M. R., Masoud, H. M., Helmy, M. S., Hamed, A. A., Gad El-Karim, R. M., Ali, R. E., ... & Ibrahim, M. A. (2023). In vitro anticancer and antimicrobial activities of copper-zinc superoxide dismutase purified from Cellana rota snail. Egyptian Journal of Chemistry, 66(12), 1-10. https://doi.org/10.21608/ejchem.2023.200467.7736
He, Y., Li, J., Chen, J., Miao, X., Li, G., He, Q., ... & Wei, Y. (2020). Cytotoxic effects of polystyrene nanoplastics with different surface functionalization on human HepG2 cells. Science of the Total Environment, 723, 138180.https://doi.org/10.1016/j.scitotenv.2020.138180
Holdom, M. D., Lechenne, B., Hay, R. J., Hamilton, A. J., & Monod, M. (2000). Production and characterization of recombinant Aspergillus fumigatus Cu, Zn superoxide dismutase and its recognition by immune human sera. Journal of Clinical Microbiology, 38(2), 558-562. https://doi.org/10.1128/jcm.38.2.558-562.2000
Ibrahim, M. A., Mohamed, M. M., Ghazy, A. H. M., & Masoud, H. M. (2013). Superoxide dismutases from larvae of the camel tick Hyalommadromedarii. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 164(3), 221-228. https://doi.org/10.1016/j.cbpb.2013.01.002
Islam, M. N., Rauf, A., Fahad, F. I., Emran, T. B., Mitra, S., Olatunde, A., ... & Mubarak, M. S. (2022). Superoxide dismutase: an updated review on its health benefits and industrial applications. Critical Reviews in Food Science and Nutrition, 62(26), 7282-7300. https://doi.org/10.1080/10408398.2021.1913400
Krezel, A., & Maret, W. (2021). The bioinorganic chemistry of mammalian metallothioneins. Chemical reviews, 121(23), 14594-14648. https://doi.org/10.1021/acs.chemrev.1c00371?urlappend=%3Fref%3DPDF&jav=VoR&rel=cite-as
Kumar, A., Sharma, M., Bhardwaj, P. K., Vats, S. K., Singh, D., & Kumar, S. (2016). Copper, zinc superoxide dismutase from Caragana jubata: A thermostable enzyme that functions under a broad pH and temperature window. Process Biochemistry, 51(10), 1434-1444. https://doi.org/10.1016/j.procbio.2016.06.025
Law, J. W. F., Ser, H. L., Duangjai, A., Saokaew, S., Bukhari, S. I., Khan, T. M., ... & Lee, L. H. (2017). Streptomyces colonosanans sp. nov., a novel actinobacterium isolated from Malaysia mangrove soil exhibiting antioxidative activity and cytotoxic potential against human colon cancer cell lines. Frontiers in Microbiology, 8, 877.https://doi.org/10.3389/fmicb.2017.00877
Lefebre, M. D., & Valvano, M. A. (2001). In vitro resistance of Burkholderiacepacia complex isolates to reactive oxygen species in relation to catalase and superoxide dismutase production. Microbiology, 147(1), 97-109. https://doi.org/10.1099/00221287-147-1-97
Longoni, S. S., Marín, C., & Sánchez-Moreno, M. (2014). Excreted Leishmania peruviana and Leishmania amazonensis iron–superoxide dismutase purification: Specific antibody detection in Colombian patients with cutaneous leishmaniasis. Free Radical Biology and Medicine, 69, 26-34. https://doi.org/10.1016/j.freeradbiomed.2014.01.012
Matsumoto, H., Haniu, H., & Komori, N. (2019). Determination of protein molecular weights on SDS-PAGE. Electrophoretic Separation of Proteins: Methods and Protocols, 101-105. https://doi.org/10.1007/978-1-4939-8793-1_10
Ozdemir, C., Gulesci, N., & Bilgin, R. (2021). Purification and Characterization of Superoxide Dismutase Enzyme from Punica granatum L. Asian Journal of Research in Biochemistry, 9(3), 30-35. https://doi.org/10.9734/ajrb/2021/v9i330203
Park, A., Joo, M., Kim, K., Son, W. J., Lim, G., Lee, J., ... & Nam, S. (2022). A comprehensive evaluation of regression-based drug responsiveness prediction models, using cell viability inhibitory concentrations (IC50 values). Bioinformatics, 38(10), 2810-2817. https://doi.org/10.1093/bioinformatics/btac177
Pokharel, P., Ma, Z., & Chang, S. X. (2020). Biochar increases soil microbial biomass with changes in extra-and intracellular enzyme activities: A global meta-analysis. Biochar, 2, 65-79. https://doi.org/10.1007/s42773-020-00039-1
Rady, M. M., El-Shewy, A. A., Seif El-Yazal, M. A., & Abd El-Gawwad, A. F. M. (2022). Integrative application of soil P-solubilizing bacteria and foliar nano-P improves antioxidant, hormonal, and nutrient contents and phosphatase activity in Phaseolus vulgaris plants grown under calcareous soil conditions. Journal of Agricultural Research Pesticides and Biofertilizers, 3(2). https://doi.org/10.1007/s42729-019-00168-Y
Rosa, A. C., Corsi, D., Cavi, N., Bruni, N., & Dosio, F. (2021). Superoxide dismutase administration: A review of proposed human uses. Molecules, 26(7), 1844.https://doi.org/10.3390/molecules26071844
Saqib, U., Kelley, T. T., Panguluri, S. K., Liu, D., Savai, R., Baig, M. S., &Schürer, S. C. (2018). Polypharmacology or promiscuity? Structural interactions of resveratrol with its bandwagon of targets. Frontiers in Pharmacology, 9, 1201.https://doi.org/10.3389/fphar.2018.01201
Stephenie, S., Chang, Y. P., Gnanasekaran, A., Esa, N. M., &Gnanaraj, C. (2020). An insight on superoxide dismutase (SOD) from plants for mammalian health enhancement. Journal of Functional Foods, 68, 103917.https://doi.org/10.1016/j.jff.2020.103917
Tuteja, N., Mishra, P., Yadav, S., Tajrishi, M., Baral, S., & Sabat, S. C. (2015). Heterologous expression and biochemical characterization of a highly active and stable chloroplasticCuZn-superoxide dismutase from Pisum sativum. BMC biotechnology, 15, 1-14. https://doi.org/10.1186/s12896-015-0117-0
Valderas, M. W., & Hart, M. E. (2001). Identification and characterization of a second superoxide dismutase gene (sodM) from Staphylococcus aureus. Journal of Bacteriology, 183(11), 3399-3407. https://doi.org/10.1128/JB.183.11.3399-3407.2001
Wang, B. R., Zhi, W. X., Han, S. Y., Zhao, H. F., Liu, Y. X., Xu, S. Y., ... & Mu, Z. S. (2024). Adaptability to the environment of protease by secondary structure changes and application to enzyme-selective hydrolysis. International Journal of Biological Macromolecules, 278(Pt 3), 134969.https://doi.org/10.1016/j.ijbiomac.2024.134969
Wang, J., Luo, B., Li, X., Lu, W., Yang, J., Hu, Y., ... & Wen, S. (2017). Inhibition of cancer growth in vitro and in vivo by a novel ROS-modulating agent with ability to eliminate stem-like cancer cells. Cell Death & Disease, 8(6), e2887-e2887. https://doi.org/10.1038/cddis.2017.272
Wang, M., Wang, L., Yi, Q., Gai, Y., & Song, L. (2015). Molecular cloning and characterization of a cytoplasmic manganese superoxide dismutase and a mitochondrial manganese superoxide dismutase from Chinese mitten crab Eriocheir sinensis. Fish & Shellfish Immunology, 47(1), 407-417. https://doi.org/10.1016/j.fsi.2015.09.035
Wang, Q. F., Wang, Y. F., Hou, Y. H., Shi, Y. L., Han, H., Miao, M., ... & Li, Y. J. (2016). Cloning, expression and biochemical characterization of recombinant superoxide dismutase from Antarctic psychrophilic bacterium Pseudoalteromonas sp. ANT506. Journal of Basic Microbiology, 56(7), 753-761. https://doi.org/10.1002/jobm.201500444
Whitaker, J. R., & Bernhard, R. A. (1972). Experiments for: An introduction to enzymology.
World Health Organization. (2018). Global Health Estimates 2016: Deaths by cause, age, sex, by country and by region, 2000–2016. Geneva: World Health Organization. Available at: https://www.who.int/data/gho/data/themes/mortality-and-global-health-estimates
Zeinali, F., Homaei, A., & Kamrani, E. (2017). Identification and kinetic characterization of a novel superoxide dismutase from Avicennia marina: An antioxidant enzyme with unique features. International Journal of Biological Macromolecules, 105(Pt 3), 1556-1562. https://doi.org/10.1016/j.ijbiomac.2017.07.054
Zheng, M., Liu, Y., Zhang, G., Yang, Z., Xu, W., & Chen, Q. (2023). The applications and mechanisms of superoxide dismutase in medicine, food, and cosmetics. Antioxidants, 12(9), 1675.https://doi.org/10.3390/antiox12091675
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How to Cite
Mhmood, W., & Hussein, A. (2025). Characterization and Cytotoxic Activity Evaluation of Superoxide Dismutase (SOD) Enzyme Purified From Escherichia coli. International Journal of Advancement in Life Sciences Research, 8(3), 60-72. https://doi.org/https://doi.org/10.31632/ijalsr.2025.v08i03.005
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