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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The characterization of a thermostable and cambialistic superoxide dismutase from Thermus filiformis

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Mandelli, F. [1, 2] ; Franco Cairo, J. P. L. [1] ; Citadini, A. P. S. [1] ; Buechli, F. [1] ; Alvarez, T. M. [1] ; Oliveira, R. J. [3] ; Leite, V. B. P. [3] ; Paes Leme, A. F. [4] ; Mercadante, A. Z. [2] ; Squina, F. M. [1]
Total Authors: 10
[1] CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, BR-13083970 Campinas, SP - Brazil
[2] Univ Estadual Campinas, Fac Engn Alimentos, Dept Ciencia Alimentos, Campinas, SP - Brazil
[3] Univ Estadual Paulista, Inst Biociencias Letras & Ciencias Exatas, Dept Fis, Sao Jose Do Rio Preto - Brazil
[4] CNPEM, Lab Nacl Biociencias LNBio, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: Letters in Applied Microbiology; v. 57, n. 1, p. 40-46, JUL 2013.
Web of Science Citations: 10

The superoxide dismutase (TfSOD) gene from the extremely thermophilic bacterium Thermus filiformis was cloned and expressed at high levels in mesophilic host. The purified enzyme displayed approximately 25 kDa band in the SDS-PAGE, which was further confirmed as TfSOD by mass spectrometry. The TfSOD was characterized as a cambialistic enzyme once it had enzymatic activity with either manganese or iron as cofactor. TfSOD showed thermostability at 65, 70 and 80 degrees C. The amount of enzyme required to inhibit 50% of pyrogallol autoxidation was 0 center dot 41, 0 center dot 56 and 13 center dot 73mg at 65, 70 and 80 degrees C, respectively. According to the circular dichroism (CD) spectra data, the secondary structure was progressively lost after increasing the temperature above 70 degrees C. The 3-dimensional model of TfSOD with the predicted cofactor binding corroborated with functional and CD analysis. Significance and Impact of the Study This manuscript describes the expression and characterization of a superoxide dismutase (SOD) from Thermus filiformis with thermophilic and cambialistic characteristics. The SODs are among the most potent antioxidants known in nature, and their stability and pharmacokinetics can vary widely in accordance to their biological source. Although the currently clinical research work has been focused on human and bovine SODs, alternative sources may become more biotechnological attractive in the near future. Our study brings new insights for the research field of antioxidant enzymes with potential application on pharmaceutical, cosmetics and food formulations. (AU)

FAPESP's process: 11/17658-3 - Computational studies on protein folding and applications in the study of enzymes involved in bioethanol production
Grantee:Vitor Barbanti Pereira Leite
Support type: Regular Research Grants
FAPESP's process: 08/58037-9 - Library generation for biomass-conversion enzymes from soil metagenome
Grantee:Fábio Márcio Squina
Support type: Program for Research on Bioenergy (BIOEN) - Young Investigators Grants