Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/10189
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dc.contributor.authorGüneş, Seda-
dc.contributor.authorTamburacı, Sedef-
dc.contributor.authorİmamoğlu, Esra-
dc.contributor.authorDalay, Meltem Conk-
dc.date.accessioned2021-01-24T18:32:50Z-
dc.date.available2021-01-24T18:32:50Z-
dc.date.issued2015-
dc.identifier.issn2231-1866-
dc.identifier.urihttps://doi.org/10.1080/22311866.2014.983973-
dc.identifier.urihttps://hdl.handle.net/10189-
dc.description.abstractThere is considerable interest in cyanobacteria as sources of antioxidant pigments, antiinflammatory substances, enzymes such as superoxide dismutase (SOD) and vitamins. Antioxidant enzymes have significant role in the removal of reactive oxygen species produced during visible and ultraviolet irradiance stress in cyanobacteria. One of the most ubiquitous protective enzyme is superoxide dismutase (SOD). Most of cyanobacteria are known to have both FeSOD and MnSOD which are associated with photosystem I and II. These enzymes are responsible for scavenging superoxide radicals.Spirulina platensis and Synechococcus nidulans are widely used cyanobacteria as food supplement and cosmetic due to their bioactive compounds. Although the chemical composition of S.platensis has been investigated by many researchers, research on the relationship between protein content and comparison of SOD activity with other cyanobacteria is limited.Among several SOD producing cyanobacteria, the most promising organisms were investigate in terms of SOD activities in this study. The aim of the present work was to investigate and compare the SOD activities of different cyanobacteria including S. platensis, Pseudanabeana sp., S. nidulans and associate with protein contents. SOD activities of these cyanobacteria were determined by xanthine/xanthineoxidase method.Modified Lowry method was used for protein determination. The analysis results showed that the maximum specific SOD activity obtained was 50.4 U/mg from S.nidulans and the minimum specific SOD activity was 18.4 U/mg from Pseudanabeana sp. Total protein amount of S. nidulans, S. platensis, Pseudanabeana sp. was determined as 0.25 mg/ml, 0.27 mg/ml and 0.43 mg/ml respectively. As a result, Synechococcus nidulans was more efficient at scavenging peroxide radicals than Pseudanabeana sp. © 2015, © 2015 Har Krishan Bhalla & Sons.en_US
dc.description.sponsorshipThe authors would like to thank Ege University Scientific Research Fund for financial support and Prof. Dr. Sibel Konyalioglu for technical support.en_US
dc.language.isoenen_US
dc.publisherTaylor and Francis Ltd.en_US
dc.relation.ispartofJournal of Biologically Active Products from Natureen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectPseudanabeanaen_US
dc.subjectSOD activityen_US
dc.subjectSpirulina platensisen_US
dc.subjectSynechococcus nidulansen_US
dc.titleDetermination of superoxide dismutase activities in different cyanobacteria for scavenging of reactive oxygen speciesen_US
dc.typeArticleen_US
dc.institutionauthorGüneş, Seda-
dc.institutionauthorTamburacı, Sedef-
dc.departmentİzmir Institute of Technology. Bioengineeringen_US
dc.identifier.volume5en_US
dc.identifier.issue1en_US
dc.identifier.startpage25en_US
dc.identifier.endpage32en_US
dc.identifier.scopus2-s2.0-85019122672en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1080/22311866.2014.983973-
dc.relation.doi10.1080/22311866.2014.983973en_US
dc.coverage.doi10.1080/22311866.2014.983973en_US
local.message.claim2022-06-13T11:28:59.603+0300|||rp00694|||submit_approve|||dc_contributor_author|||None*
dc.identifier.scopusquality--
item.grantfulltextopen-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.openairetypeArticle-
item.languageiso639-1en-
item.fulltextWith Fulltext-
crisitem.author.dept03.02. Department of Chemical Engineering-
Appears in Collections:Bioengineering / Biyomühendislik
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
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