Antioxidant activity in vitro of the selenium-contained protein from the Se-enriched Bifidobacterium animalis 01 |
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| Authors: | Qian Shen Bowen Zhang Rihua Xu Yang Wang Xuelong Ding Pinglan Li |
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| Institution: | 1. Institute for Biochemistry and Molecular Biology I, Heinrich-Heine-University, Düsseldorf, Germany;2. Leibniz-Institut für Umweltmedizinische Forschung (IUF) Heinrich-Heine-University, Düsseldorf, Germany;3. College of Science, King Saud University, Riyadh, Saudi Arabia;1. Instituto de Productos Lácteos de Asturias-Consejo Superior de Investigaciones Científicas (IPLA-CSIC), Paseo Río Linares s/n 33300 Villaviciosa, Asturias, Spain;2. Department of Biomedical and Biotechnological Sciences, University of Catania, Via Santa Sofia 97, 95123 Catania, Italy;3. Department of Chemical Sciences, University of Naples Federico II, Via Cintia 4, 80126 Napoli, Italy;4. Department of Drug Science, Biochemistry Section, University of Catania. Viale Andrea Doria 6, 95123 Catania, Italy;5. Department of Agricultural Sciences, University of Naples Federico II, Via Università 100, 80055 Portici, NA, Italy;1. School of Nutrition and Food Sciences, Louisiana State University Agricultural Center, Baton Rouge, LA, 70803, USA;2. College of Enology, Northwest A&F University, Yangling, China;1. Department of Medical Biotechnology, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran;2. Nanotechnology Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran;1. Life and Medical Sciences (LIMES) Institute, University of Bonn, Germany;2. Institute of Medical Immunology, Charité, Universitätsmedizin Berlin, Berlin, Germany;3. BIH Center for Regenerative Therapies, Charité, Universitätsmedizin Berlin, and Berlin Institute of Health (BIH) Berlin, Germany;4. Centre for Individualised Infection Medicine (CiiM) and TWINCORE, joint ventures between the Helmholtz-Centre for Infection Research (HZI) and the Hannover Medical School (MHH), Hannover, Germany;5. Department of Internal Medicine I, University Hospital Bonn, Bonn, Germany;6. Helmholtz Institute for RNA-based Infection Research (HIRI), Helmholtz-Center for Infection Research (HZI), Würzburg, Germany;7. Department of Infectious Diseases and Respiratory Medicine, Charité, Universitätsmedizin Berlin, Berlin, Germany;8. German Center for Neurodegenerative Diseases (DZNE), PRECISE Platform for Genomics and Epigenomics at DZNE, and University of Bonn, Bonn, Germany;9. Mass Cytometry Lab, DRFZ Berlin, a Leibniz Institute, Berlin, Germany;10. Flow and Mass Cytometry Core Facility, Charité, Universitätsmedizin Berlin, and Berlin Institute of Health (BIH), Berlin, Germany;11. Department of Internal Medicine and Radboud Center for Infectious Diseases, Radboud University Medical Center, Nijmegen, the Netherlands;12. German Center for Lung Research (DZL);13. Department of Immunology, Labor Berlin-Charité Vivantes, Berlin, Germany;14. Institute of Virology, Charité Universitätsmedizin Berlin, Berlin, Germany;15. Berlin Institute of Health (BIH), Berlin, Germany;16. Berlin Institute for Medical Systems Biology, Max-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany;17. Clinical Study Center (CSC), Charité, Universitätsmedizin Berlin, and Berlin Institute of Health, Berlin, Germany;18. Institute of Laboratory Medicine, Clinical Chemistry, and Pathobiochemistry, Charité, Universitätsmedizin Berlin, Berlin, Germany;19. Genome Analytics, Helmholtz-Center for Infection Research (HZI), Braunschweig, Germany;20. German Center for Infection Research (DZIF);21. Department of Tropical Medicine, Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany;22. I. Department of Medicine, University Medical Center, Hamburg-Eppendorf, Hamburg, Germany |
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| Abstract: | Several studies indicated that bifidobacteria possessed strong antioxidant activity. In present study, the antioxidant activities of Bifidobacterium animalis 01 proteins were evaluated using six assays, namely, linoleic acid preoxidation assay, erythrocyte hemolysis assay, 1,1-diphenyl-2-picrylhydrazyl (DPPH) assay, reducing power assay, hydroxyl ( OH) and superoxide radicals (O2?) assays, in which the last two assays were measured by electron spin resonance (ESR). There were two kinds of B. animalis 01 proteins in this study, the regular B. animalis 01 protein (Pro-CK) and the B. animalis 01 selenium-contained protein (Pro-Se). Both Pro-CK and Pro-Se showed concentration dependent antioxidant activity in DPPH assay, reducing power assay and erythrocyte hemolysis assay. All results of six assays indicated that the antioxidant activity of the B. animalis 01 protein was improved remarkably after selenium was incorporated. The antioxidant activity of Pro-Se increased with the increase of selenium content in Pro-Se suggesting selenium played a positive role in enhancing the antioxidant activity of B. animalis 01 protein. Moreover, organic selenium was more effective than inorganic selenium on enhancing the hydroxyl radical scavenging ability of B. animalis 01 protein. |
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